HEADER    OXIDOREDUCTASE (CH-OH(D)-NAD(A))        29-SEP-95   1CDO
TITLE     ALCOHOL DEHYDROGENASE (E.C.1.1.1.1) (EE ISOZYME) COMPLEXED
TITLE    2 WITH NICOTINAMIDE ADENINE DINUCLEOTIDE (NAD), AND ZINC
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALCOHOL DEHYDROGENASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 1.1.1.1;
COMPND   5 HETEROGEN: COENZYME NAD;
COMPND   6 HETEROGEN: ZN
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GADUS CALLARIAS;
SOURCE   3 ORGANISM_COMMON: COD FISH;
SOURCE   4 ORGAN: LIVER
KEYWDS    OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    RAMASWAMY.S.H.EKLUND
REVDAT   1   08-MAR-96 1CDO    0
JRNL        AUTH   S.RAMASWAMY,M.EL AHMAD,O.DANIELSSON,H.JORNVALL,
JRNL        AUTH 2 H.EKLUND
JRNL        TITL   THE THREE-DIMENSIONAL STRUCTURE AT 2.1 ANGSTROMS
JRNL        TITL 2 RESOLUTION OF A COD LIVER CLASS I ALCOHOL
JRNL        TITL 3 DEHYDROGENASE WITH CLASS-MIXED PROPERTIES
JRNL        REF    TO BE PUBLISHED
JRNL        REFN                                                  0353
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.RAMASWAMY,H.EKLUND,B.V.PLAPP
REMARK   1  TITL   STRUCTURES OF HORSE LIVER ALCOHOL DEHYDROGENASE
REMARK   1  TITL 2 COMPLEXED WITH NAD+ AND SUBSTITUTED BENZYL ALCOHOLS
REMARK   1  REF    BIOCHEMISTRY                  V.  33  5230 1994
REMARK   1  REFN   ASTM BICHAW  US ISSN 0006-2960                 0033
REMARK   2
REMARK   2 RESOLUTION. 2.05 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM                    X-PLOR
REMARK   3   AUTHORS                    BRUNGER
REMARK   3   R VALUE                    0.177
REMARK   3   FREE R VALUE               0.248
REMARK   3   MEAN B VALUE               11.4   ANGSTROMS**2
REMARK   3   RMSD BOND DISTANCES        0.010  ANGSTROMS
REMARK   3   RMSD BOND ANGLES           1.60   DEGREES
REMARK   3   RMSD DIHEDRAL ANGLES       25.1   DEGREES
REMARK   3   RMSD IMPROPER ANGLES       1.3    DEGREES
REMARK   3
REMARK   3   NUMBER OF REFLECTIONS      39749
REMARK   3   RESOLUTION RANGE       7.0 - 2.05 ANGSTROMS
REMARK   3   DATA CUTOFF                0.0    SIGMA(F)
REMARK   3
REMARK   3  DATA COLLECTION.
REMARK   3   NUMBER OF UNIQUE REFLECTIONS      39749
REMARK   3   COMPLETENESS OF DATA              86.9   %
REMARK   3
REMARK   3  NUMBER OF ATOMS USED IN REFINEMENT.
REMARK   3   NUMBER OF PROTEIN ATOMS                       5606
REMARK   3   NUMBER OF NUCLEIC ACID ATOMS                     0
REMARK   3   NUMBER OF HETEROGEN ATOMS                       92
REMARK   3   NUMBER OF SOLVENT ATOMS                        648
REMARK   4
REMARK   4 SITE
REMARK   4  SITE_IDENTIFIER: ZIN
REMARK   4   CATALYTIC SITE.
REMARK   5
REMARK   5 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK   5 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK   5 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK   5 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK   5 NUMBER; I=INSERTION CODE):
REMARK   5
REMARK   5  M RES CSSEQI
REMARK   5  0 HOH    973      DISTANCE =  6.58 ANGSTROMS
REMARK   5  0 HOH   1000      DISTANCE =  5.25 ANGSTROMS
REMARK   5  0 HOH   1054      DISTANCE =  8.30 ANGSTROMS
REMARK   5  0 HOH   1185      DISTANCE =  5.14 ANGSTROMS
REMARK   5  0 HOH   1290      DISTANCE =  5.66 ANGSTROMS
REMARK  18
REMARK  18 EXPERIMENTAL DETAILS.
REMARK  18  DATE OF DATA COLLECTION        : MAY-94
REMARK  18  SOURCE                         : DESY
REMARK  18  BEAMLINE                       : X11
REMARK  18  MONOCHROMATIC (Y/N)            : Y
REMARK  18  LAUE (Y/N)                     : N
REMARK  18  WAVELENGTH OR RANGE (A)        : 0.89
REMARK  18  DETECTOR TYPE                  : IMAGE PLATE
REMARK  18  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK  18  INTENSITY-INTEGRATION SOFTWARE : DENZO/CCP4
REMARK  18  DATA REDUNDANCY                : 2.1
REMARK  18  MERGING R VALUE (INTENSITY)    : 0.12
REMARK 999
REMARK 999 FOR CHAIN "A" -   1 C-TERMINAL RESIDUES NOT IN ATOMS LIST
REMARK 999
REMARK 999 FOR CHAIN "B" -   1 C-TERMINAL RESIDUES NOT IN ATOMS LIST
DBREF  1CDO A    1   374  SWS    P26325   ADH_GADCA        1    374
DBREF  1CDO B    1   374  SWS    P26325   ADH_GADCA        1    374
SEQRES   1 A  374  ALA THR VAL GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL
SEQRES   2 A  374  ALA TRP GLU ALA ASN LYS PRO LEU VAL ILE GLU GLU ILE
SEQRES   3 A  374  GLU VAL ASP VAL PRO HIS ALA ASN GLU ILE ARG ILE LYS
SEQRES   4 A  374  ILE ILE ALA THR GLY VAL CYS HIS THR ASP LEU TYR HIS
SEQRES   5 A  374  LEU PHE GLU GLY LYS HIS LYS ASP GLY PHE PRO VAL VAL
SEQRES   6 A  374  LEU GLY HIS GLU GLY ALA GLY ILE VAL GLU SER VAL GLY
SEQRES   7 A  374  PRO GLY VAL THR GLU PHE GLN PRO GLY GLU LYS VAL ILE
SEQRES   8 A  374  PRO LEU PHE ILE SER GLN CYS GLY GLU CYS ARG PHE CYS
SEQRES   9 A  374  GLN SER PRO LYS THR ASN GLN CYS VAL LYS GLY TRP ALA
SEQRES  10 A  374  ASN GLU SER PRO ASP VAL MET SER PRO LYS GLU THR ARG
SEQRES  11 A  374  PHE THR CYS LYS GLY ARG LYS VAL LEU GLN PHE LEU GLY
SEQRES  12 A  374  THR SER THR PHE SER GLN TYR THR VAL VAL ASN GLN ILE
SEQRES  13 A  374  ALA VAL ALA LYS ILE ASP PRO SER ALA PRO LEU ASP THR
SEQRES  14 A  374  VAL CYS LEU LEU GLY CYS GLY VAL SER THR GLY PHE GLY
SEQRES  15 A  374  ALA ALA VAL ASN THR ALA LYS VAL GLU PRO GLY SER THR
SEQRES  16 A  374  CYS ALA VAL PHE GLY LEU GLY ALA VAL GLY LEU ALA ALA
SEQRES  17 A  374  VAL MET GLY CYS HIS SER ALA GLY ALA LYS ARG ILE ILE
SEQRES  18 A  374  ALA VAL ASP LEU ASN PRO ASP LYS PHE GLU LYS ALA LYS
SEQRES  19 A  374  VAL PHE GLY ALA THR ASP PHE VAL ASN PRO ASN ASP HIS
SEQRES  20 A  374  SER GLU PRO ILE SER GLN VAL LEU SER LYS MET THR ASN
SEQRES  21 A  374  GLY GLY VAL ASP PHE SER LEU GLU CYS VAL GLY ASN VAL
SEQRES  22 A  374  GLY VAL MET ARG ASN ALA LEU GLU SER CYS LEU LYS GLY
SEQRES  23 A  374  TRP GLY VAL SER VAL LEU VAL GLY TRP THR ASP LEU HIS
SEQRES  24 A  374  ASP VAL ALA THR ARG PRO ILE GLN LEU ILE ALA GLY ARG
SEQRES  25 A  374  THR TRP LYS GLY SER MET PHE GLY GLY PHE LYS GLY LYS
SEQRES  26 A  374  ASP GLY VAL PRO LYS MET VAL LYS ALA TYR LEU ASP LYS
SEQRES  27 A  374  LYS VAL LYS LEU ASP GLU PHE ILE THR HIS ARG MET PRO
SEQRES  28 A  374  LEU GLU SER VAL ASN ASP ALA ILE ASP LEU MET LYS HIS
SEQRES  29 A  374  GLY LYS CYS ILE ARG THR VAL LEU SER LEU
SEQRES   1 B  374  ALA THR VAL GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL
SEQRES   2 B  374  ALA TRP GLU ALA ASN LYS PRO LEU VAL ILE GLU GLU ILE
SEQRES   3 B  374  GLU VAL ASP VAL PRO HIS ALA ASN GLU ILE ARG ILE LYS
SEQRES   4 B  374  ILE ILE ALA THR GLY VAL CYS HIS THR ASP LEU TYR HIS
SEQRES   5 B  374  LEU PHE GLU GLY LYS HIS LYS ASP GLY PHE PRO VAL VAL
SEQRES   6 B  374  LEU GLY HIS GLU GLY ALA GLY ILE VAL GLU SER VAL GLY
SEQRES   7 B  374  PRO GLY VAL THR GLU PHE GLN PRO GLY GLU LYS VAL ILE
SEQRES   8 B  374  PRO LEU PHE ILE SER GLN CYS GLY GLU CYS ARG PHE CYS
SEQRES   9 B  374  GLN SER PRO LYS THR ASN GLN CYS VAL LYS GLY TRP ALA
SEQRES  10 B  374  ASN GLU SER PRO ASP VAL MET SER PRO LYS GLU THR ARG
SEQRES  11 B  374  PHE THR CYS LYS GLY ARG LYS VAL LEU GLN PHE LEU GLY
SEQRES  12 B  374  THR SER THR PHE SER GLN TYR THR VAL VAL ASN GLN ILE
SEQRES  13 B  374  ALA VAL ALA LYS ILE ASP PRO SER ALA PRO LEU ASP THR
SEQRES  14 B  374  VAL CYS LEU LEU GLY CYS GLY VAL SER THR GLY PHE GLY
SEQRES  15 B  374  ALA ALA VAL ASN THR ALA LYS VAL GLU PRO GLY SER THR
SEQRES  16 B  374  CYS ALA VAL PHE GLY LEU GLY ALA VAL GLY LEU ALA ALA
SEQRES  17 B  374  VAL MET GLY CYS HIS SER ALA GLY ALA LYS ARG ILE ILE
SEQRES  18 B  374  ALA VAL ASP LEU ASN PRO ASP LYS PHE GLU LYS ALA LYS
SEQRES  19 B  374  VAL PHE GLY ALA THR ASP PHE VAL ASN PRO ASN ASP HIS
SEQRES  20 B  374  SER GLU PRO ILE SER GLN VAL LEU SER LYS MET THR ASN
SEQRES  21 B  374  GLY GLY VAL ASP PHE SER LEU GLU CYS VAL GLY ASN VAL
SEQRES  22 B  374  GLY VAL MET ARG ASN ALA LEU GLU SER CYS LEU LYS GLY
SEQRES  23 B  374  TRP GLY VAL SER VAL LEU VAL GLY TRP THR ASP LEU HIS
SEQRES  24 B  374  ASP VAL ALA THR ARG PRO ILE GLN LEU ILE ALA GLY ARG
SEQRES  25 B  374  THR TRP LYS GLY SER MET PHE GLY GLY PHE LYS GLY LYS
SEQRES  26 B  374  ASP GLY VAL PRO LYS MET VAL LYS ALA TYR LEU ASP LYS
SEQRES  27 B  374  LYS VAL LYS LEU ASP GLU PHE ILE THR HIS ARG MET PRO
SEQRES  28 B  374  LEU GLU SER VAL ASN ASP ALA ILE ASP LEU MET LYS HIS
SEQRES  29 B  374  GLY LYS CYS ILE ARG THR VAL LEU SER LEU
FTNOTE   1
FTNOTE   1 CIS PROLINE - PRO A    63
FTNOTE   2
FTNOTE   2 CIS PROLINE - PRO B    63
HET    NAD  A 375      44     NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HET     ZN  A 376       1     ZINC ION
HET     ZN  A 377       1     ZINC ION
HET    NAD  B 375      44     NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HET     ZN  B 376       1     ZINC ION
HET     ZN  B 377       1     ZINC ION
FORMUL   3  NAD    2(C21 H27 N7 O14 P2)
FORMUL   4   ZN    4(ZN1 2+)
FORMUL   5  HOH   *648(H2 O1)
HELIX    1   1 HIS A   47  PHE A   54  1
HELIX    2   2 ARG A  102  GLN A  105  1
HELIX    3   3 TRP A  116  ASN A  118  5
HELIX    4   4 PHE A  141  GLY A  143  5
HELIX    5   5 GLN A  155  ALA A  157  5
HELIX    6   6 LEU A  167  GLY A  174  1
HELIX    7   7 GLY A  176  VAL A  185  1
HELIX    8   8 ALA A  203  SER A  214  1
HELIX    9   9 PRO A  227  VAL A  235  5
HELIX   10  10 PRO A  244  ASP A  246  5
HELIX   11  11 ILE A  251  THR A  259  1
HELIX   12  12 VAL A  273  GLU A  281  1
HELIX   13  13 PRO A  305  ILE A  309  1
HELIX   14  14 PHE A  319  GLY A  321  5
HELIX   15  15 GLY A  324  LEU A  336  1
HELIX   16  16 ASP A  343  PHE A  345  5
HELIX   17  17 LEU A  352  HIS A  364  5
HELIX   18  18 HIS B   47  GLU B   55  1
HELIX   19  19 LYS B   59  GLY B   61  5
HELIX   20  20 TRP B  116  GLU B  119  1
HELIX   21  21 PHE B  141  GLY B  143  5
HELIX   22  22 GLN B  155  ALA B  157  5
HELIX   23  23 LEU B  167  GLY B  174  1
HELIX   24  24 GLY B  176  VAL B  185  1
HELIX   25  25 ALA B  203  ALA B  215  1
HELIX   26  26 PRO B  227  PHE B  236  5
HELIX   27  27 PRO B  244  ASP B  246  5
HELIX   28  28 ILE B  251  THR B  259  1
HELIX   29  29 VAL B  273  GLU B  281  1
HELIX   30  30 PRO B  305  ILE B  309  1
HELIX   31  31 PHE B  319  GLY B  321  5
HELIX   32  32 GLY B  324  LEU B  336  1
HELIX   33  33 ASP B  343  PHE B  345  5
HELIX   34  34 LEU B  352  LYS B  363  5
SHEET    1   A 2 ILE A   7  VAL A  13  0
SHEET    2   A 2 VAL A  22  VAL A  28 -1  N  VAL A  28   O  ILE A   7
SHEET    1   B 3 TYR A 150  ASN A 154  0
SHEET    2   B 3 GLU A  35  ILE A  40 -1  N  ILE A  38   O  THR A 151
SHEET    3   B 3 GLY A  72  VAL A  77 -1  N  SER A  76   O  ARG A  37
SHEET    1   C 3 ALA A  42  GLY A  44  0
SHEET    2   C 3 ARG A 369  SER A 373 -1  N  LEU A 372   O  THR A  43
SHEET    3   C 3 ILE A 346  PRO A 351  1  N  THR A 347   O  ARG A 369
SHEET    1   D 2 VAL A  90  PRO A  92  0
SHEET    2   D 2 VAL A 158  LYS A 160 -1  N  ALA A 159   O  ILE A  91
SHEET    1   E 2 PHE A 131  CYS A 133  0
SHEET    2   E 2 ARG A 136  VAL A 138 -1  N  VAL A 138   O  PHE A 131
SHEET    1   F 6 THR A 313  GLY A 316  0
SHEET    2   F 6 VAL A 289  LEU A 292  1  N  SER A 290   O  THR A 313
SHEET    3   F 6 PHE A 265  GLU A 268  1  N  SER A 266   O  VAL A 289
SHEET    4   F 6 THR A 195  PHE A 199  1  N  ALA A 197   O  PHE A 265
SHEET    5   F 6 ARG A 219  VAL A 223  1  N  ARG A 219   O  CYS A 196
SHEET    6   F 6 ASP A 240  VAL A 242  1  N  ASP A 240   O  ALA A 222
SHEET    1   G 2 ASP A 300  ARG A 304  0
SHEET    2   G 2 ASP B 300  ARG B 304 -1  N  THR B 303   O  VAL A 301
SHEET    1   H 2 ILE B   7  VAL B  13  0
SHEET    2   H 2 VAL B  22  VAL B  28 -1  N  VAL B  28   O  ILE B   7
SHEET    1   I 3 TYR B 150  ASN B 154  0
SHEET    2   I 3 GLU B  35  ILE B  40 -1  N  ILE B  38   O  THR B 151
SHEET    3   I 3 GLY B  72  VAL B  77 -1  N  SER B  76   O  ARG B  37
SHEET    1   J 3 ALA B  42  GLY B  44  0
SHEET    2   J 3 ARG B 369  SER B 373 -1  N  LEU B 372   O  THR B  43
SHEET    3   J 3 ILE B 346  PRO B 351  1  N  THR B 347   O  ARG B 369
SHEET    1   K 2 VAL B  90  PRO B  92  0
SHEET    2   K 2 VAL B 158  LYS B 160 -1  N  ALA B 159   O  ILE B  91
SHEET    1   L 6 THR B 313  GLY B 316  0
SHEET    2   L 6 VAL B 289  LEU B 292  1  N  SER B 290   O  THR B 313
SHEET    3   L 6 PHE B 265  GLU B 268  1  N  SER B 266   O  VAL B 289
SHEET    4   L 6 THR B 195  PHE B 199  1  N  ALA B 197   O  PHE B 265
SHEET    5   L 6 ARG B 219  VAL B 223  1  N  ARG B 219   O  CYS B 196
SHEET    6   L 6 ASP B 240  VAL B 242  1  N  ASP B 240   O  ALA B 222
SITE     1 ZIN  6 CYS A  46  GLY A 174  GLY A  67  CYS B  46
SITE     2 ZIN  6 GLY B 174  GLY B  67
CRYST1  102.950   47.600   80.430  90.00 104.66  90.00 P 21          4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.009713  0.000000  0.002541        0.00000
SCALE2      0.000000  0.021008  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012852        0.00000
ATOM      1  N   ALA A   1      44.105   0.676  -0.622  1.00 25.39
ATOM      2  CA  ALA A   1      45.457   1.192  -1.008  1.00 26.20
ATOM      3  C   ALA A   1      46.112   2.008   0.113  1.00 26.06
ATOM      4  O   ALA A   1      47.289   2.353   0.032  1.00 26.35
ATOM      5  CB  ALA A   1      45.348   2.039  -2.279  1.00 26.40
ATOM      6  N   THR A   2      45.337   2.317   1.149  1.00 25.09
ATOM      7  CA  THR A   2      45.821   3.105   2.276  1.00 23.49
ATOM      8  C   THR A   2      45.808   2.342   3.604  1.00 21.32
ATOM      9  O   THR A   2      46.479   2.728   4.560  1.00 21.60
ATOM     10  CB  THR A   2      44.984   4.387   2.414  1.00 23.26
ATOM     11  OG1 THR A   2      43.636   4.130   1.984  1.00 26.24
ATOM     12  CG2 THR A   2      45.576   5.494   1.565  1.00 23.96
ATOM     13  N   VAL A   3      45.059   1.247   3.644  1.00 17.35
ATOM     14  CA  VAL A   3      44.941   0.431   4.844  1.00 20.21
ATOM     15  C   VAL A   3      46.302  -0.033   5.357  1.00 19.52
ATOM     16  O   VAL A   3      47.138  -0.492   4.584  1.00 21.02
ATOM     17  CB  VAL A   3      44.058  -0.812   4.590  1.00 19.49
ATOM     18  CG1 VAL A   3      43.738  -1.518   5.906  1.00 20.15
ATOM     19  CG2 VAL A   3      42.783  -0.415   3.878  1.00 20.04
ATOM     20  N   GLY A   4      46.513   0.117   6.662  1.00 19.79
ATOM     21  CA  GLY A   4      47.755  -0.302   7.289  1.00 18.71
ATOM     22  C   GLY A   4      48.894   0.665   7.067  1.00 18.20
ATOM     23  O   GLY A   4      50.018   0.426   7.504  1.00 18.60
ATOM     24  N   LYS A   5      48.598   1.782   6.420  1.00 18.93
ATOM     25  CA  LYS A   5      49.608   2.781   6.134  1.00 20.03
ATOM     26  C   LYS A   5      49.212   4.139   6.693  1.00 18.55
ATOM     27  O   LYS A   5      48.033   4.409   6.905  1.00 19.39
ATOM     28  CB  LYS A   5      49.777   2.923   4.621  1.00 20.19
ATOM     29  CG  LYS A   5      50.212   1.674   3.888  1.00 25.33
ATOM     30  CD  LYS A   5      50.132   1.918   2.393  1.00 28.28
ATOM     31  CE  LYS A   5      50.568   0.710   1.584  1.00 31.42
ATOM     32  NZ  LYS A   5      50.165   0.870   0.155  1.00 31.36
ATOM     33  N   VAL A   6      50.212   4.979   6.943  1.00 16.25
ATOM     34  CA  VAL A   6      49.991   6.341   7.412  1.00 16.49
ATOM     35  C   VAL A   6      49.497   7.076   6.158  1.00 18.23
ATOM     36  O   VAL A   6      49.948   6.785   5.041  1.00 20.60
ATOM     37  CB  VAL A   6      51.323   6.978   7.895  1.00 16.05
ATOM     38  CG1 VAL A   6      51.129   8.440   8.280  1.00 13.64
ATOM     39  CG2 VAL A   6      51.880   6.203   9.073  1.00 17.29
ATOM     40  N   ILE A   7      48.539   7.978   6.330  1.00 16.63
ATOM     41  CA  ILE A   7      47.993   8.735   5.211  1.00 12.34
ATOM     42  C   ILE A   7      48.470  10.177   5.241  1.00 14.33
ATOM     43  O   ILE A   7      48.563  10.782   6.296  1.00 17.32
ATOM     44  CB  ILE A   7      46.440   8.716   5.231  1.00 11.48
ATOM     45  CG1 ILE A   7      45.915   7.447   4.568  1.00  8.73
ATOM     46  CG2 ILE A   7      45.862   9.939   4.546  1.00  7.42
ATOM     47  CD1 ILE A   7      44.430   7.245   4.747  1.00 12.01
ATOM     48  N   LYS A   8      48.845  10.691   4.077  1.00 13.44
ATOM     49  CA  LYS A   8      49.262  12.072   3.924  1.00 14.27
ATOM     50  C   LYS A   8      48.046  12.675   3.218  1.00 13.69
ATOM     51  O   LYS A   8      47.529  12.086   2.260  1.00 13.14
ATOM     52  CB  LYS A   8      50.506  12.132   3.029  1.00 17.34
ATOM     53  CG  LYS A   8      51.435  13.293   3.296  1.00 23.38
ATOM     54  CD  LYS A   8      51.023  14.578   2.556  1.00 30.46
ATOM     55  CE  LYS A   8      52.208  15.152   1.778  1.00 27.71
ATOM     56  NZ  LYS A   8      53.417  15.229   2.656  1.00 30.87
ATOM     57  N   CYS A   9      47.529  13.783   3.737  1.00 10.57
ATOM     58  CA  CYS A   9      46.359  14.408   3.143  1.00  9.23
ATOM     59  C   CYS A   9      46.279  15.875   3.536  1.00  8.32
ATOM     60  O   CYS A   9      47.143  16.375   4.266  1.00 11.82
ATOM     61  CB  CYS A   9      45.080  13.669   3.574  1.00 11.11
ATOM     62  SG  CYS A   9      44.542  13.934   5.298  1.00  8.80
ATOM     63  N   LYS A  10      45.269  16.568   3.016  1.00  6.16
ATOM     64  CA  LYS A  10      45.057  17.983   3.304  1.00  3.82
ATOM     65  C   LYS A  10      44.126  18.182   4.495  1.00  4.47
ATOM     66  O   LYS A  10      43.087  17.527   4.593  1.00  2.00
ATOM     67  CB  LYS A  10      44.420  18.691   2.100  1.00  4.34
ATOM     68  CG  LYS A  10      45.274  18.763   0.846  1.00  6.56
ATOM     69  CD  LYS A  10      44.617  19.617  -0.229  1.00  8.40
ATOM     70  CE  LYS A  10      43.414  18.926  -0.843  1.00  7.28
ATOM     71  NZ  LYS A  10      42.767  19.769  -1.904  1.00  6.63
ATOM     72  N   ALA A  11      44.464  19.152   5.340  1.00  6.39
ATOM     73  CA  ALA A  11      43.662  19.506   6.513  1.00  8.62
ATOM     74  C   ALA A  11      43.869  20.991   6.809  1.00  8.56
ATOM     75  O   ALA A  11      44.938  21.534   6.514  1.00  9.26
ATOM     76  CB  ALA A  11      44.081  18.666   7.725  1.00  7.36
ATOM     77  N   ALA A  12      42.832  21.665   7.301  1.00  6.02
ATOM     78  CA  ALA A  12      42.941  23.082   7.660  1.00  5.92
ATOM     79  C   ALA A  12      43.419  23.118   9.108  1.00  6.82
ATOM     80  O   ALA A  12      42.681  22.739  10.020  1.00  8.16
ATOM     81  CB  ALA A  12      41.606  23.772   7.534  1.00  4.54
ATOM     82  N   VAL A  13      44.663  23.546   9.307  1.00  8.39
ATOM     83  CA  VAL A  13      45.277  23.606  10.632  1.00  7.06
ATOM     84  C   VAL A  13      45.345  25.009  11.216  1.00  9.46
ATOM     85  O   VAL A  13      45.709  25.967  10.526  1.00 10.83
ATOM     86  CB  VAL A  13      46.727  23.037  10.582  1.00  8.45
ATOM     87  CG1 VAL A  13      47.396  23.079  11.969  1.00  2.00
ATOM     88  CG2 VAL A  13      46.725  21.628  10.020  1.00  6.17
ATOM     89  N   ALA A  14      44.990  25.122  12.491  1.00 12.19
ATOM     90  CA  ALA A  14      45.047  26.388  13.215  1.00 12.95
ATOM     91  C   ALA A  14      46.256  26.289  14.147  1.00 13.89
ATOM     92  O   ALA A  14      46.188  25.644  15.202  1.00  9.90
ATOM     93  CB  ALA A  14      43.776  26.604  14.017  1.00 15.95
ATOM     94  N   TRP A  15      47.365  26.903  13.738  1.00 13.83
ATOM     95  CA  TRP A  15      48.602  26.871  14.516  1.00 12.08
ATOM     96  C   TRP A  15      48.522  27.584  15.861  1.00 13.40
ATOM     97  O   TRP A  15      49.248  27.245  16.799  1.00 11.21
ATOM     98  CB  TRP A  15      49.768  27.406  13.683  1.00  9.52
ATOM     99  CG  TRP A  15      50.172  26.459  12.599  1.00  8.32
ATOM    100  CD1 TRP A  15      49.855  26.549  11.273  1.00  7.38
ATOM    101  CD2 TRP A  15      50.928  25.249  12.747  1.00  6.90
ATOM    102  NE1 TRP A  15      50.358  25.471  10.593  1.00  7.68
ATOM    103  CE2 TRP A  15      51.021  24.654  11.474  1.00  7.29
ATOM    104  CE3 TRP A  15      51.534  24.609  13.844  1.00  8.63
ATOM    105  CZ2 TRP A  15      51.698  23.446  11.255  1.00  5.16
ATOM    106  CZ3 TRP A  15      52.211  23.401  13.624  1.00  6.74
ATOM    107  CH2 TRP A  15      52.284  22.836  12.341  1.00  6.27
ATOM    108  N   GLU A  16      47.688  28.612  15.938  1.00 14.35
ATOM    109  CA  GLU A  16      47.509  29.342  17.182  1.00 15.91
ATOM    110  C   GLU A  16      46.190  30.090  17.145  1.00 16.05
ATOM    111  O   GLU A  16      45.536  30.188  16.097  1.00 17.60
ATOM    112  CB  GLU A  16      48.689  30.291  17.460  1.00 19.33
ATOM    113  CG  GLU A  16      48.851  31.413  16.444  1.00 25.09
ATOM    114  CD  GLU A  16      50.087  32.280  16.687  1.00 28.30
ATOM    115  OE1 GLU A  16      51.202  31.830  16.340  1.00 27.21
ATOM    116  OE2 GLU A  16      49.939  33.405  17.217  1.00 30.26
ATOM    117  N   ALA A  17      45.773  30.567  18.309  1.00 16.76
ATOM    118  CA  ALA A  17      44.525  31.292  18.430  1.00 18.40
ATOM    119  C   ALA A  17      44.571  32.561  17.608  1.00 20.61
ATOM    120  O   ALA A  17      45.641  32.998  17.171  1.00 21.36
ATOM    121  CB  ALA A  17      44.256  31.626  19.885  1.00 16.86
ATOM    122  N   ASN A  18      43.381  33.084  17.334  1.00 20.99
ATOM    123  CA  ASN A  18      43.179  34.329  16.605  1.00 22.94
ATOM    124  C   ASN A  18      43.881  34.491  15.251  1.00 23.38
ATOM    125  O   ASN A  18      43.920  35.605  14.714  1.00 23.42
ATOM    126  CB  ASN A  18      43.532  35.500  17.527  1.00 26.08
ATOM    127  CG  ASN A  18      42.632  36.710  17.332  1.00 29.06
ATOM    128  OD1 ASN A  18      42.629  37.613  18.166  1.00 31.37
ATOM    129  ND2 ASN A  18      41.893  36.754  16.226  1.00 29.26
ATOM    130  N   LYS A  19      44.403  33.400  14.688  1.00 21.31
ATOM    131  CA  LYS A  19      45.092  33.444  13.389  1.00 20.94
ATOM    132  C   LYS A  19      44.279  32.727  12.300  1.00 20.19
ATOM    133  O   LYS A  19      43.482  31.832  12.598  1.00 19.06
ATOM    134  CB  LYS A  19      46.509  32.836  13.474  1.00 20.03
ATOM    135  CG  LYS A  19      47.573  33.761  14.105  1.00 23.37
ATOM    136  CD  LYS A  19      48.955  33.695  13.384  1.00 32.67
ATOM    137  CE  LYS A  19      49.633  32.300  13.403  1.00 35.15
ATOM    138  NZ  LYS A  19      51.140  32.349  13.189  1.00 34.24
ATOM    139  N   PRO A  20      44.402  33.176  11.030  1.00 18.98
ATOM    140  CA  PRO A  20      43.652  32.514   9.955  1.00 17.75
ATOM    141  C   PRO A  20      44.174  31.087   9.795  1.00 17.32
ATOM    142  O   PRO A  20      45.347  30.814  10.084  1.00 15.77
ATOM    143  CB  PRO A  20      44.004  33.367   8.728  1.00 20.11
ATOM    144  CG  PRO A  20      44.231  34.731   9.312  1.00 18.77
ATOM    145  CD  PRO A  20      45.051  34.402  10.537  1.00 19.34
ATOM    146  N   LEU A  21      43.309  30.172   9.367  1.00 15.35
ATOM    147  CA  LEU A  21      43.703  28.777   9.180  1.00 13.54
ATOM    148  C   LEU A  21      44.576  28.584   7.936  1.00 12.90
ATOM    149  O   LEU A  21      44.484  29.359   6.982  1.00 13.99
ATOM    150  CB  LEU A  21      42.467  27.886   9.098  1.00  9.80
ATOM    151  CG  LEU A  21      41.827  27.421  10.409  1.00 10.42
ATOM    152  CD1 LEU A  21      41.675  28.549  11.418  1.00  2.17
ATOM    153  CD2 LEU A  21      40.479  26.795  10.092  1.00 10.10
ATOM    154  N   VAL A  22      45.387  27.527   7.938  1.00 12.22
ATOM    155  CA  VAL A  22      46.291  27.228   6.828  1.00 11.45
ATOM    156  C   VAL A  22      46.081  25.807   6.308  1.00 10.44
ATOM    157  O   VAL A  22      46.112  24.849   7.085  1.00  8.49
ATOM    158  CB  VAL A  22      47.781  27.383   7.268  1.00 12.48
ATOM    159  CG1 VAL A  22      48.728  27.141   6.083  1.00  9.62
ATOM    160  CG2 VAL A  22      48.013  28.758   7.868  1.00 11.62
ATOM    161  N   ILE A  23      45.855  25.673   5.000  1.00 10.66
ATOM    162  CA  ILE A  23      45.666  24.358   4.397  1.00 10.21
ATOM    163  C   ILE A  23      47.046  23.712   4.388  1.00 10.42
ATOM    164  O   ILE A  23      47.974  24.240   3.779  1.00 10.81
ATOM    165  CB  ILE A  23      45.091  24.439   2.950  1.00 10.70
ATOM    166  CG1 ILE A  23      43.767  25.216   2.939  1.00  9.88
ATOM    167  CG2 ILE A  23      44.850  23.036   2.393  1.00 13.41
ATOM    168  CD1 ILE A  23      42.661  24.616   3.811  1.00  2.92
ATOM    169  N   GLU A  24      47.189  22.629   5.147  1.00  8.58
ATOM    170  CA  GLU A  24      48.453  21.916   5.261  1.00 10.10
ATOM    171  C   GLU A  24      48.326  20.459   4.861  1.00 10.33
ATOM    172  O   GLU A  24      47.220  19.916   4.754  1.00  9.85
ATOM    173  CB  GLU A  24      48.939  21.944   6.719  1.00 11.06
ATOM    174  CG  GLU A  24      49.085  23.323   7.342  1.00 13.01
ATOM    175  CD  GLU A  24      50.396  24.000   6.995  1.00 15.70
ATOM    176  OE1 GLU A  24      51.045  23.606   6.003  1.00 18.19
ATOM    177  OE2 GLU A  24      50.784  24.934   7.726  1.00 19.45
ATOM    178  N   GLU A  25      49.471  19.843   4.597  1.00 13.54
ATOM    179  CA  GLU A  25      49.517  18.422   4.287  1.00 14.39
ATOM    180  C   GLU A  25      49.949  17.814   5.610  1.00 13.24
ATOM    181  O   GLU A  25      51.003  18.174   6.147  1.00 11.66
ATOM    182  CB  GLU A  25      50.558  18.104   3.209  1.00 20.41
ATOM    183  CG  GLU A  25      50.285  18.722   1.835  1.00 30.52
ATOM    184  CD  GLU A  25      49.000  18.223   1.178  1.00 34.44
ATOM    185  OE1 GLU A  25      48.007  17.970   1.890  1.00 39.62
ATOM    186  OE2 GLU A  25      48.975  18.104  -0.064  1.00 35.93
ATOM    187  N   ILE A  26      49.081  16.988   6.182  1.00 11.47
ATOM    188  CA  ILE A  26      49.343  16.331   7.453  1.00 10.15
ATOM    189  C   ILE A  26      49.429  14.816   7.249  1.00  8.35
ATOM    190  O   ILE A  26      49.057  14.296   6.193  1.00  9.52
ATOM    191  CB  ILE A  26      48.191  16.599   8.492  1.00  9.26
ATOM    192  CG1 ILE A  26      46.909  15.845   8.089  1.00  6.75
ATOM    193  CG2 ILE A  26      47.925  18.094   8.633  1.00  4.95
ATOM    194  CD1 ILE A  26      45.809  15.859   9.143  1.00  2.00
ATOM    195  N   GLU A  27      49.919  14.127   8.273  1.00  9.58
ATOM    196  CA  GLU A  27      50.014  12.672   8.275  1.00 11.14
ATOM    197  C   GLU A  27      48.948  12.194   9.259  1.00 10.77
ATOM    198  O   GLU A  27      48.820  12.733  10.361  1.00 11.07
ATOM    199  CB  GLU A  27      51.386  12.197   8.762  1.00 13.05
ATOM    200  CG  GLU A  27      52.528  12.464   7.795  1.00 15.92
ATOM    201  CD  GLU A  27      53.760  11.644   8.117  0.50 15.50
ATOM    202  OE1 GLU A  27      54.157  11.593   9.304  0.50 17.14
ATOM    203  OE2 GLU A  27      54.347  11.053   7.176  0.50 13.95
ATOM    204  N   VAL A  28      48.137  11.242   8.832  1.00  9.61
ATOM    205  CA  VAL A  28      47.085  10.685   9.661  1.00  9.09
ATOM    206  C   VAL A  28      47.549   9.272   9.967  1.00 11.24
ATOM    207  O   VAL A  28      47.794   8.478   9.057  1.00 10.20
ATOM    208  CB  VAL A  28      45.723  10.683   8.918  1.00  6.86
ATOM    209  CG1 VAL A  28      44.617  10.143   9.804  1.00  3.21
ATOM    210  CG2 VAL A  28      45.368  12.105   8.469  1.00  5.84
ATOM    211  N   ASP A  29      47.773   8.999  11.247  1.00 12.32
ATOM    212  CA  ASP A  29      48.243   7.688  11.685  1.00 13.64
ATOM    213  C   ASP A  29      47.166   6.625  11.471  1.00 12.87
ATOM    214  O   ASP A  29      46.024   6.939  11.154  1.00 16.66
ATOM    215  CB  ASP A  29      48.642   7.766  13.166  1.00 14.37
ATOM    216  CG  ASP A  29      49.467   6.572  13.639  1.00 18.00
ATOM    217  OD1 ASP A  29      50.051   5.841  12.804  1.00 17.17
ATOM    218  OD2 ASP A  29      49.542   6.384  14.874  1.00 17.55
ATOM    219  N   VAL A  30      47.556   5.365  11.586  1.00 14.16
ATOM    220  CA  VAL A  30      46.636   4.250  11.432  1.00 12.48
ATOM    221  C   VAL A  30      45.777   4.171  12.705  1.00 13.60
ATOM    222  O   VAL A  30      46.264   4.449  13.811  1.00 11.88
ATOM    223  CB  VAL A  30      47.409   2.925  11.227  1.00 15.23
ATOM    224  CG1 VAL A  30      48.150   2.952   9.895  1.00 13.14
ATOM    225  CG2 VAL A  30      48.405   2.713  12.360  1.00 15.30
ATOM    226  N   PRO A  31      44.494   3.781  12.567  1.00 10.40
ATOM    227  CA  PRO A  31      43.586   3.677  13.716  1.00 10.29
ATOM    228  C   PRO A  31      44.027   2.658  14.771  1.00  9.54
ATOM    229  O   PRO A  31      44.323   1.503  14.458  1.00 11.05
ATOM    230  CB  PRO A  31      42.250   3.303  13.069  1.00  4.52
ATOM    231  CG  PRO A  31      42.661   2.532  11.854  1.00 10.27
ATOM    232  CD  PRO A  31      43.830   3.337  11.327  1.00 10.96
ATOM    233  N   HIS A  32      44.083   3.108  16.022  1.00  8.08
ATOM    234  CA  HIS A  32      44.476   2.249  17.129  1.00  7.20
ATOM    235  C   HIS A  32      43.279   1.397  17.534  1.00  7.96
ATOM    236  O   HIS A  32      42.245   1.402  16.859  1.00  5.77
ATOM    237  CB  HIS A  32      44.949   3.091  18.316  1.00  7.17
ATOM    238  CG  HIS A  32      46.104   3.987  17.999  1.00  8.10
ATOM    239  ND1 HIS A  32      46.832   4.634  18.972  1.00  7.57
ATOM    240  CD2 HIS A  32      46.658   4.343  16.814  1.00  5.32
ATOM    241  CE1 HIS A  32      47.785   5.353  18.402  1.00  9.98
ATOM    242  NE2 HIS A  32      47.699   5.192  17.094  1.00  7.15
ATOM    243  N   ALA A  33      43.411   0.677  18.644  1.00 10.60
ATOM    244  CA  ALA A  33      42.326  -0.176  19.133  1.00 10.67
ATOM    245  C   ALA A  33      41.006   0.595  19.298  1.00 10.05
ATOM    246  O   ALA A  33      40.990   1.725  19.810  1.00  8.67
ATOM    247  CB  ALA A  33      42.730  -0.828  20.451  1.00  9.87
ATOM    248  N   ASN A  34      39.917  -0.014  18.827  1.00 10.77
ATOM    249  CA  ASN A  34      38.563   0.552  18.899  1.00 11.18
ATOM    250  C   ASN A  34      38.359   1.884  18.166  1.00 12.60
ATOM    251  O   ASN A  34      37.414   2.623  18.479  1.00 11.44
ATOM    252  CB  ASN A  34      38.117   0.724  20.356  1.00 13.07
ATOM    253  CG  ASN A  34      38.157  -0.567  21.141  1.00 11.41
ATOM    254  OD1 ASN A  34      38.773  -0.627  22.203  1.00 12.52
ATOM    255  ND2 ASN A  34      37.511  -1.603  20.629  1.00  9.92
ATOM    256  N   GLU A  35      39.217   2.186  17.191  1.00  9.52
ATOM    257  CA  GLU A  35      39.119   3.440  16.435  1.00  9.04
ATOM    258  C   GLU A  35      38.686   3.250  14.989  1.00  6.97
ATOM    259  O   GLU A  35      38.858   2.167  14.423  1.00  9.10
ATOM    260  CB  GLU A  35      40.454   4.181  16.475  1.00  7.95
ATOM    261  CG  GLU A  35      40.817   4.711  17.855  1.00 12.26
ATOM    262  CD  GLU A  35      42.164   5.413  17.895  1.00 17.27
ATOM    263  OE1 GLU A  35      42.735   5.690  16.819  1.00 18.01
ATOM    264  OE2 GLU A  35      42.657   5.683  19.010  1.00 18.77
ATOM    265  N   ILE A  36      38.151   4.314  14.389  1.00  8.47
ATOM    266  CA  ILE A  36      37.682   4.291  12.997  1.00  7.95
ATOM    267  C   ILE A  36      38.391   5.393  12.202  1.00  7.20
ATOM    268  O   ILE A  36      38.503   6.521  12.695  1.00  8.03
ATOM    269  CB  ILE A  36      36.130   4.585  12.898  1.00  9.28
ATOM    270  CG1 ILE A  36      35.328   3.762  13.922  1.00 12.72
ATOM    271  CG2 ILE A  36      35.608   4.285  11.493  1.00  5.97
ATOM    272  CD1 ILE A  36      35.364   2.254  13.713  1.00 12.66
ATOM    273  N   ARG A  37      38.937   5.065  11.028  1.00  5.21
ATOM    274  CA  ARG A  37      39.559   6.093  10.187  1.00  6.38
ATOM    275  C   ARG A  37      38.509   6.384   9.124  1.00  5.73
ATOM    276  O   ARG A  37      38.068   5.474   8.410  1.00  5.49
ATOM    277  CB  ARG A  37      40.885   5.655   9.553  1.00  7.72
ATOM    278  CG  ARG A  37      41.621   6.849   8.889  1.00  4.58
ATOM    279  CD  ARG A  37      43.143   6.681   8.826  1.00  3.97
ATOM    280  NE  ARG A  37      43.539   5.575   7.956  1.00  2.45
ATOM    281  CZ  ARG A  37      44.795   5.181   7.753  1.00  6.19
ATOM    282  NH1 ARG A  37      45.809   5.801   8.353  1.00  2.00
ATOM    283  NH2 ARG A  37      45.032   4.147   6.959  1.00  2.00
ATOM    284  N   ILE A  38      38.125   7.654   9.026  1.00  5.02
ATOM    285  CA  ILE A  38      37.061   8.102   8.136  1.00  4.49
ATOM    286  C   ILE A  38      37.452   9.135   7.083  1.00  5.83
ATOM    287  O   ILE A  38      38.124  10.113   7.377  1.00  2.91
ATOM    288  CB  ILE A  38      35.927   8.749   8.995  1.00  5.06
ATOM    289  CG1 ILE A  38      35.471   7.779  10.088  1.00  4.17
ATOM    290  CG2 ILE A  38      34.745   9.166   8.124  1.00  6.64
ATOM    291  CD1 ILE A  38      34.686   8.433  11.214  1.00  5.10
ATOM    292  N   LYS A  39      37.004   8.918   5.852  1.00  8.43
ATOM    293  CA  LYS A  39      37.240   9.879   4.782  1.00  7.77
ATOM    294  C   LYS A  39      36.053  10.860   4.840  1.00  6.42
ATOM    295  O   LYS A  39      34.909  10.480   4.563  1.00  7.18
ATOM    296  CB  LYS A  39      37.268   9.173   3.426  1.00  7.46
ATOM    297  CG  LYS A  39      37.431  10.121   2.240  1.00  6.04
ATOM    298  CD  LYS A  39      37.406   9.359   0.935  1.00  7.80
ATOM    299  CE  LYS A  39      37.292  10.295  -0.261  1.00 11.97
ATOM    300  NZ  LYS A  39      38.347  11.347  -0.261  1.00 13.16
ATOM    301  N   ILE A  40      36.315  12.100   5.253  1.00  7.75
ATOM    302  CA  ILE A  40      35.265  13.117   5.359  1.00  6.79
ATOM    303  C   ILE A  40      34.868  13.674   3.982  1.00  8.20
ATOM    304  O   ILE A  40      35.700  14.194   3.243  1.00  8.76
ATOM    305  CB  ILE A  40      35.686  14.276   6.327  1.00  4.54
ATOM    306  CG1 ILE A  40      35.876  13.741   7.755  1.00  4.37
ATOM    307  CG2 ILE A  40      34.637  15.389   6.341  1.00  2.55
ATOM    308  CD1 ILE A  40      34.615  13.086   8.366  1.00  4.68
ATOM    309  N   ILE A  41      33.587  13.547   3.650  1.00  9.70
ATOM    310  CA  ILE A  41      33.045  14.018   2.372  1.00  8.16
ATOM    311  C   ILE A  41      32.466  15.445   2.468  1.00  7.77
ATOM    312  O   ILE A  41      32.463  16.190   1.484  1.00  9.05
ATOM    313  CB  ILE A  41      31.935  13.051   1.865  1.00  9.44
ATOM    314  CG1 ILE A  41      32.460  11.605   1.822  1.00  7.61
ATOM    315  CG2 ILE A  41      31.396  13.498   0.495  1.00  7.10
ATOM    316  CD1 ILE A  41      33.621  11.379   0.883  1.00  4.42
ATOM    317  N   ALA A  42      31.977  15.821   3.646  1.00  7.59
ATOM    318  CA  ALA A  42      31.398  17.148   3.852  1.00  3.77
ATOM    319  C   ALA A  42      31.370  17.496   5.335  1.00  6.19
ATOM    320  O   ALA A  42      31.212  16.611   6.179  1.00  4.23
ATOM    321  CB  ALA A  42      29.982  17.196   3.284  1.00  4.40
ATOM    322  N   THR A  43      31.530  18.782   5.647  1.00  6.63
ATOM    323  CA  THR A  43      31.494  19.254   7.027  1.00  8.16
ATOM    324  C   THR A  43      30.979  20.699   7.115  1.00  8.95
ATOM    325  O   THR A  43      31.363  21.559   6.313  1.00  6.65
ATOM    326  CB  THR A  43      32.888  19.145   7.734  1.00  7.62
ATOM    327  OG1 THR A  43      32.766  19.568   9.102  1.00  7.12
ATOM    328  CG2 THR A  43      33.938  20.000   7.036  1.00  3.14
ATOM    329  N   GLY A  44      30.024  20.925   8.015  1.00  6.48
ATOM    330  CA  GLY A  44      29.500  22.262   8.206  1.00  5.18
ATOM    331  C   GLY A  44      30.439  23.017   9.134  1.00  4.73
ATOM    332  O   GLY A  44      31.360  22.431   9.702  1.00  3.27
ATOM    333  N   VAL A  45      30.235  24.321   9.266  1.00  4.36
ATOM    334  CA  VAL A  45      31.051  25.144  10.151  1.00  4.00
ATOM    335  C   VAL A  45      30.101  25.592  11.264  1.00  3.90
ATOM    336  O   VAL A  45      29.020  26.103  10.970  1.00  5.52
ATOM    337  CB  VAL A  45      31.615  26.377   9.388  1.00  6.45
ATOM    338  CG1 VAL A  45      32.427  27.279  10.322  1.00  2.22
ATOM    339  CG2 VAL A  45      32.482  25.912   8.219  1.00  6.08
ATOM    340  N   CYS A  46      30.464  25.342  12.523  1.00  3.58
ATOM    341  CA  __4 A  46      29.619  25.728  13.669  1.00  5.75
ATOM    342  C   CYS A  46      30.251  26.896  14.434  1.00  7.27
ATOM    343  O   CYS A  46      31.462  27.134  14.333  1.00  5.54
ATOM    344  CB  CYS A  46      29.398  24.514  14.602  1.00  6.39
ATOM    345  SG  CYS A  46      28.494  24.789  16.196  1.00  8.49
ATOM    346  N   HIS A  47      29.449  27.631  15.204  1.00  7.11
ATOM    347  CA  HIS A  47      30.013  28.748  15.956  1.00  6.78
ATOM    348  C   HIS A  47      30.956  28.304  17.066  1.00  5.43
ATOM    349  O   HIS A  47      31.756  29.104  17.554  1.00  8.53
ATOM    350  CB  HIS A  47      28.940  29.661  16.540  1.00  6.34
ATOM    351  CG  HIS A  47      29.502  30.801  17.332  1.00  8.59
ATOM    352  ND1 HIS A  47      30.024  31.935  16.745  1.00  8.81
ATOM    353  CD2 HIS A  47      29.667  30.963  18.666  1.00 13.94
ATOM    354  CE1 HIS A  47      30.481  32.747  17.679  1.00  9.68
ATOM    355  NE2 HIS A  47      30.279  32.178  18.857  1.00 14.13
ATOM    356  N   THR A  48      30.831  27.056  17.508  1.00  5.13
ATOM    357  CA  THR A  48      31.709  26.534  18.559  1.00  4.98
ATOM    358  C   THR A  48      33.155  26.425  18.046  1.00  6.68
ATOM    359  O   THR A  48      34.108  26.521  18.823  1.00  5.79
ATOM    360  CB  THR A  48      31.200  25.187  19.099  1.00  5.40
ATOM    361  OG1 THR A  48      29.881  25.364  19.628  1.00  8.63
ATOM    362  CG2 THR A  48      32.101  24.669  20.202  1.00  7.97
ATOM    363  N   ASP A  49      33.311  26.264  16.732  1.00  4.39
ATOM    364  CA  ASP A  49      34.637  26.205  16.120  1.00  5.27
ATOM    365  C   ASP A  49      35.255  27.597  16.306  1.00  4.44
ATOM    366  O   ASP A  49      36.417  27.727  16.697  1.00  6.15
ATOM    367  CB  ASP A  49      34.542  25.877  14.619  1.00  2.00
ATOM    368  CG  ASP A  49      34.143  24.439  14.352  1.00  2.00
ATOM    369  OD1 ASP A  49      34.849  23.528  14.827  1.00  2.57
ATOM    370  OD2 ASP A  49      33.134  24.214  13.647  1.00  2.00
ATOM    371  N   LEU A  50      34.450  28.633  16.088  1.00  3.30
ATOM    372  CA  LEU A  50      34.933  30.000  16.245  1.00  5.05
ATOM    373  C   LEU A  50      35.245  30.317  17.713  1.00  8.16
ATOM    374  O   LEU A  50      36.240  30.985  18.013  1.00  5.43
ATOM    375  CB  LEU A  50      33.911  31.018  15.721  1.00  7.10
ATOM    376  CG  LEU A  50      33.339  30.936  14.301  1.00 10.39
ATOM    377  CD1 LEU A  50      33.226  32.343  13.713  1.00  5.97
ATOM    378  CD2 LEU A  50      34.192  30.053  13.410  1.00  9.30
ATOM    379  N   TYR A  51      34.389  29.848  18.621  1.00  7.44
ATOM    380  CA  TYR A  51      34.578  30.096  20.050  1.00  9.12
ATOM    381  C   TYR A  51      36.005  29.774  20.524  1.00  9.21
ATOM    382  O   TYR A  51      36.651  30.593  21.180  1.00  9.70
ATOM    383  CB  TYR A  51      33.546  29.306  20.879  1.00  7.93
ATOM    384  CG  TYR A  51      33.729  29.439  22.383  1.00  6.11
ATOM    385  CD1 TYR A  51      34.623  28.615  23.073  1.00  3.30
ATOM    386  CD2 TYR A  51      33.015  30.393  23.114  1.00  2.10
ATOM    387  CE1 TYR A  51      34.802  28.742  24.454  1.00  8.39
ATOM    388  CE2 TYR A  51      33.190  30.523  24.499  1.00  6.08
ATOM    389  CZ  TYR A  51      34.086  29.696  25.157  1.00  6.53
ATOM    390  OH  TYR A  51      34.293  29.828  26.512  1.00  8.71
ATOM    391  N   HIS A  52      36.490  28.584  20.190  1.00 11.66
ATOM    392  CA  HIS A  52      37.834  28.171  20.581  1.00 11.35
ATOM    393  C   HIS A  52      38.895  29.065  19.934  1.00 11.85
ATOM    394  O   HIS A  52      39.815  29.539  20.605  1.00  8.63
ATOM    395  CB  HIS A  52      38.077  26.706  20.191  1.00  6.55
ATOM    396  CG  HIS A  52      39.437  26.194  20.567  1.00  8.45
ATOM    397  ND1 HIS A  52      39.894  26.178  21.868  1.00  8.30
ATOM    398  CD2 HIS A  52      40.438  25.678  19.813  1.00  6.14
ATOM    399  CE1 HIS A  52      41.118  25.676  21.900  1.00  8.82
ATOM    400  NE2 HIS A  52      41.469  25.365  20.664  1.00  8.56
ATOM    401  N   LEU A  53      38.731  29.313  18.638  1.00 13.10
ATOM    402  CA  LEU A  53      39.667  30.114  17.850  1.00 14.00
ATOM    403  C   LEU A  53      39.739  31.603  18.206  1.00 14.91
ATOM    404  O   LEU A  53      40.819  32.203  18.198  1.00 14.91
ATOM    405  CB  LEU A  53      39.312  29.962  16.361  1.00 14.34
ATOM    406  CG  LEU A  53      40.144  30.639  15.266  1.00 11.17
ATOM    407  CD1 LEU A  53      41.533  30.026  15.175  1.00  9.28
ATOM    408  CD2 LEU A  53      39.434  30.458  13.942  1.00 10.51
ATOM    409  N   PHE A  54      38.593  32.192  18.527  1.00 16.58
ATOM    410  CA  PHE A  54      38.521  33.612  18.829  1.00 17.23
ATOM    411  C   PHE A  54      38.182  34.001  20.269  1.00 19.62
ATOM    412  O   PHE A  54      38.678  35.016  20.754  1.00 22.57
ATOM    413  CB  PHE A  54      37.507  34.284  17.895  1.00 18.75
ATOM    414  CG  PHE A  54      37.836  34.166  16.426  1.00 17.47
ATOM    415  CD1 PHE A  54      39.079  34.555  15.939  1.00 18.21
ATOM    416  CD2 PHE A  54      36.878  33.708  15.524  1.00 19.18
ATOM    417  CE1 PHE A  54      39.365  34.494  14.579  1.00 17.85
ATOM    418  CE2 PHE A  54      37.151  33.642  14.158  1.00 20.45
ATOM    419  CZ  PHE A  54      38.399  34.037  13.686  1.00 20.36
ATOM    420  N   GLU A  55      37.306  33.239  20.928  1.00 19.80
ATOM    421  CA  GLU A  55      36.874  33.547  22.299  1.00 18.38
ATOM    422  C   GLU A  55      37.639  32.874  23.436  1.00 20.04
ATOM    423  O   GLU A  55      38.285  33.550  24.230  1.00 22.19
ATOM    424  CB  GLU A  55      35.386  33.241  22.465  1.00 16.20
ATOM    425  CG  GLU A  55      34.467  34.042  21.570  1.00 14.82
ATOM    426  CD  GLU A  55      33.017  33.626  21.713  1.00 13.25
ATOM    427  OE1 GLU A  55      32.495  33.669  22.845  1.00 11.71
ATOM    428  OE2 GLU A  55      32.401  33.244  20.696  1.00 13.28
ATOM    429  N   GLY A  56      37.478  31.558  23.572  1.00 20.34
ATOM    430  CA  GLY A  56      38.159  30.822  24.626  1.00 18.44
ATOM    431  C   GLY A  56      39.662  30.861  24.459  1.00 19.94
ATOM    432  O   GLY A  56      40.396  31.206  25.388  1.00 19.27
ATOM    433  N   LYS A  57      40.122  30.479  23.269  1.00 20.41
ATOM    434  CA  LYS A  57      41.545  30.478  22.942  1.00 19.81
ATOM    435  C   LYS A  57      42.450  29.832  23.986  1.00 22.11
ATOM    436  O   LYS A  57      43.543  30.350  24.263  1.00 22.01
ATOM    437  CB  LYS A  57      42.000  31.918  22.686  1.00 18.68
ATOM    438  CG  LYS A  57      41.216  32.628  21.608  1.00 19.92
ATOM    439  CD  LYS A  57      41.625  34.083  21.512  1.00 18.35
ATOM    440  CE  LYS A  57      41.151  34.873  22.721  1.00 20.82
ATOM    441  NZ  LYS A  57      41.631  36.279  22.669  1.00 17.90
ATOM    442  N   HIS A  58      42.032  28.697  24.548  1.00 22.02
ATOM    443  CA  HIS A  58      42.859  28.038  25.559  1.00 24.65
ATOM    444  C   HIS A  58      44.260  27.820  25.003  1.00 25.19
ATOM    445  O   HIS A  58      44.442  27.147  23.986  1.00 25.57
ATOM    446  CB  HIS A  58      42.245  26.732  26.032  1.00 26.64
ATOM    447  CG  HIS A  58      42.962  26.132  27.209  1.00 29.71
ATOM    448  ND1 HIS A  58      43.998  25.253  27.086  1.00 31.13
ATOM    449  CD2 HIS A  58      42.808  26.359  28.542  1.00 29.99
ATOM    450  CE1 HIS A  58      44.472  24.940  28.268  1.00 30.95
ATOM    451  NE2 HIS A  58      43.769  25.599  29.185  1.00 29.35
ATOM    452  N   LYS A  59      45.255  28.291  25.744  1.00 26.51
ATOM    453  CA  LYS A  59      46.652  28.239  25.306  1.00 28.68
ATOM    454  C   LYS A  59      47.269  26.880  25.043  1.00 25.84
ATOM    455  O   LYS A  59      48.177  26.764  24.206  1.00 25.82
ATOM    456  CB  LYS A  59      47.514  29.060  26.255  1.00 33.31
ATOM    457  CG  LYS A  59      47.045  30.520  26.300  1.00 39.25
ATOM    458  CD  LYS A  59      47.881  31.344  27.261  1.00 43.98
ATOM    459  CE  LYS A  59      47.429  32.804  27.255  1.00 46.13
ATOM    460  NZ  LYS A  59      48.223  33.613  28.237  1.00 48.86
ATOM    461  N   ASP A  60      46.791  25.826  25.719  1.00 22.59
ATOM    462  CA  ASP A  60      47.332  24.487  25.511  1.00 18.96
ATOM    463  C   ASP A  60      46.531  23.751  24.425  1.00 18.33
ATOM    464  O   ASP A  60      46.823  22.597  24.118  1.00 18.81
ATOM    465  CB  ASP A  60      47.296  23.674  26.816  1.00 18.69
ATOM    466  CG  ASP A  60      48.407  24.059  27.806  1.00 19.36
ATOM    467  OD1 ASP A  60      49.445  24.609  27.387  1.00 12.12
ATOM    468  OD2 ASP A  60      48.238  23.786  29.016  1.00 23.42
ATOM    469  N   GLY A  61      45.538  24.431  23.854  1.00 15.97
ATOM    470  CA  GLY A  61      44.708  23.808  22.839  1.00 12.75
ATOM    471  C   GLY A  61      45.092  24.067  21.392  1.00 12.12
ATOM    472  O   GLY A  61      44.255  23.936  20.494  1.00 13.01
ATOM    473  N   PHE A  62      46.344  24.450  21.164  1.00 12.69
ATOM    474  CA  PHE A  62      46.860  24.735  19.825  1.00  9.77
ATOM    475  C   PHE A  62      48.238  24.084  19.710  1.00 11.68
ATOM    476  O   PHE A  62      48.914  23.895  20.724  1.00 14.36
ATOM    477  CB  PHE A  62      46.993  26.251  19.616  1.00  7.44
ATOM    478  CG  PHE A  62      45.692  26.993  19.679  1.00  5.59
ATOM    479  CD1 PHE A  62      44.910  27.156  18.540  1.00  6.62
ATOM    480  CD2 PHE A  62      45.233  27.508  20.881  1.00  6.32
ATOM    481  CE1 PHE A  62      43.685  27.822  18.605  1.00  6.93
ATOM    482  CE2 PHE A  62      44.008  28.176  20.959  1.00  6.22
ATOM    483  CZ  PHE A  62      43.233  28.333  19.824  1.00  5.43
ATOM    484  N   PRO A  63      48.646  23.667  18.495  1.00 11.82   1
ATOM    485  CA  ___ A  63      47.926  23.762  17.217  1.00 13.38   1
ATOM    486  C   PRO A  63      46.781  22.743  17.129  1.00 10.71   1
ATOM    487  O   PRO A  63      46.831  21.698  17.782  1.00 12.51   1
ATOM    488  CB  PRO A  63      49.030  23.494  16.186  1.00 12.82   1
ATOM    489  CG  PRO A  63      49.968  22.586  16.913  1.00 12.35   1
ATOM    490  CD  PRO A  63      50.040  23.232  18.276  1.00 10.73   1
ATOM    491  N   VAL A  64      45.781  23.018  16.292  1.00  9.84
ATOM    492  CA  VAL A  64      44.625  22.123  16.185  1.00  7.60
ATOM    493  C   VAL A  64      43.858  22.155  14.861  1.00  7.03
ATOM    494  O   VAL A  64      43.881  23.146  14.135  1.00  9.39
ATOM    495  CB  VAL A  64      43.609  22.453  17.323  1.00  8.24
ATOM    496  CG1 VAL A  64      42.972  23.813  17.078  1.00  8.77
ATOM    497  CG2 VAL A  64      42.551  21.374  17.463  1.00  2.00
ATOM    498  N   VAL A  65      43.225  21.035  14.529  1.00  7.96
ATOM    499  CA  VAL A  65      42.376  20.946  13.344  1.00  5.53
ATOM    500  C   VAL A  65      40.947  20.971  13.910  1.00  6.15
ATOM    501  O   VAL A  65      40.569  20.090  14.689  1.00  5.40
ATOM    502  CB  VAL A  65      42.611  19.652  12.551  1.00  2.67
ATOM    503  CG1 VAL A  65      41.545  19.486  11.480  1.00  2.00
ATOM    504  CG2 VAL A  65      43.996  19.683  11.906  1.00  5.12
ATOM    505  N   LEU A  66      40.204  22.028  13.588  1.00  4.11
ATOM    506  CA  LEU A  66      38.837  22.210  14.057  1.00  3.23
ATOM    507  C   LEU A  66      37.869  21.360  13.229  1.00  3.25
ATOM    508  O   LEU A  66      38.296  20.582  12.380  1.00  4.84
ATOM    509  CB  LEU A  66      38.459  23.699  13.984  1.00  3.87
ATOM    510  CG  LEU A  66      39.305  24.733  14.758  1.00  2.94
ATOM    511  CD1 LEU A  66      38.984  26.142  14.276  1.00  2.00
ATOM    512  CD2 LEU A  66      39.061  24.635  16.254  1.00  3.46
ATOM    513  N   GLY A  67      36.571  21.504  13.483  1.00  3.34
ATOM    514  CA  __1 A  67      35.565  20.746  12.754  1.00  2.00
ATOM    515  C   GLY A  67      34.927  19.644  13.582  1.00  2.64
ATOM    516  O   GLY A  67      35.628  18.830  14.165  1.00  2.00
ATOM    517  N   HIS A  68      33.594  19.613  13.623  1.00  3.90
ATOM    518  CA  __5 A  68      32.849  18.615  14.395  1.00  4.03
ATOM    519  C   HIS A  68      31.397  18.457  13.920  1.00  4.91
ATOM    520  O   HIS A  68      30.502  18.179  14.723  1.00  2.00
ATOM    521  CB  HIS A  68      32.861  18.991  15.883  1.00  7.63
ATOM    522  CG  HIS A  68      32.186  20.295  16.189  1.00  5.83
ATOM    523  ND1 HIS A  68      32.806  21.524  16.114  1.00  5.87
ATOM    524  CD2 HIS A  68      30.912  20.551  16.581  1.00  5.42
ATOM    525  CE1 HIS A  68      31.913  22.463  16.454  1.00  3.53
ATOM    526  NE2 HIS A  68      30.744  21.924  16.746  1.00  5.09
ATOM    527  N   GLU A  69      31.171  18.623  12.617  1.00  5.08
ATOM    528  CA  GLU A  69      29.832  18.519  12.027  1.00  4.19
ATOM    529  C   GLU A  69      29.969  17.938  10.611  1.00  3.74
ATOM    530  O   GLU A  69      29.504  18.521   9.630  1.00  4.05
ATOM    531  CB  GLU A  69      29.195  19.915  11.986  1.00  5.60
ATOM    532  CG  GLU A  69      27.722  19.952  11.629  1.00  2.17
ATOM    533  CD  GLU A  69      27.139  21.350  11.741  1.00  5.95
ATOM    534  OE1 GLU A  69      26.908  21.808  12.882  1.00  4.75
ATOM    535  OE2 GLU A  69      26.912  21.998  10.694  1.00  2.38
ATOM    536  N   GLY A  70      30.619  16.785  10.516  1.00  3.61
ATOM    537  CA  GLY A  70      30.837  16.162   9.226  1.00  2.14
ATOM    538  C   GLY A  70      30.135  14.836   9.037  1.00  3.91
ATOM    539  O   GLY A  70      29.403  14.378   9.921  1.00  2.00
ATOM    540  N   ALA A  71      30.335  14.247   7.858  1.00  4.01
ATOM    541  CA  ALA A  71      29.761  12.954   7.491  1.00  5.66
ATOM    542  C   ALA A  71      30.701  12.303   6.467  1.00  7.05
ATOM    543  O   ALA A  71      31.218  12.981   5.563  1.00  5.97
ATOM    544  CB  ALA A  71      28.352  13.133   6.899  1.00  4.87
ATOM    545  N   GLY A  72      30.944  11.002   6.619  1.00  5.53
ATOM    546  CA  GLY A  72      31.838  10.329   5.702  1.00  3.47
ATOM    547  C   GLY A  72      31.651   8.839   5.516  1.00  4.27
ATOM    548  O   GLY A  72      30.619   8.259   5.869  1.00  3.27
ATOM    549  N   ILE A  73      32.680   8.231   4.936  1.00  4.32
ATOM    550  CA  ILE A  73      32.724   6.806   4.617  1.00  5.46
ATOM    551  C   ILE A  73      33.900   6.164   5.354  1.00  3.21
ATOM    552  O   ILE A  73      34.997   6.730   5.384  1.00  2.00
ATOM    553  CB  ILE A  73      32.911   6.616   3.078  1.00  5.93
ATOM    554  CG1 ILE A  73      31.662   7.108   2.334  1.00  4.26
ATOM    555  CG2 ILE A  73      33.215   5.166   2.740  1.00  5.89
ATOM    556  CD1 ILE A  73      31.869   7.355   0.837  1.00  6.00
ATOM    557  N   VAL A  74      33.658   5.015   5.983  1.00  3.68
ATOM    558  CA  VAL A  74      34.713   4.317   6.716  1.00  7.13
ATOM    559  C   VAL A  74      35.809   3.915   5.735  1.00  8.77
ATOM    560  O   VAL A  74      35.515   3.440   4.637  1.00 12.74
ATOM    561  CB  VAL A  74      34.191   3.036   7.430  1.00  9.11
ATOM    562  CG1 VAL A  74      35.341   2.332   8.155  1.00  8.74
ATOM    563  CG2 VAL A  74      33.086   3.381   8.434  1.00  5.17
ATOM    564  N   GLU A  75      37.060   4.148   6.113  1.00  7.87
ATOM    565  CA  GLU A  75      38.193   3.794   5.271  1.00  7.92
ATOM    566  C   GLU A  75      38.866   2.517   5.814  1.00 11.06
ATOM    567  O   GLU A  75      39.247   1.623   5.046  1.00 10.70
ATOM    568  CB  GLU A  75      39.164   4.980   5.188  1.00  7.53
ATOM    569  CG  GLU A  75      40.436   4.738   4.371  1.00  6.20
ATOM    570  CD  GLU A  75      41.588   4.233   5.212  1.00  8.12
ATOM    571  OE1 GLU A  75      41.422   4.117   6.439  1.00  4.99
ATOM    572  OE2 GLU A  75      42.671   3.966   4.655  1.00  9.70
ATOM    573  N   SER A  76      39.016   2.434   7.135  1.00 12.38
ATOM    574  CA  SER A  76      39.604   1.255   7.783  1.00 10.00
ATOM    575  C   SER A  76      39.312   1.330   9.275  1.00 10.85
ATOM    576  O   SER A  76      39.011   2.413   9.789  1.00 11.08
ATOM    577  CB  SER A  76      41.115   1.153   7.522  1.00  7.72
ATOM    578  OG  SER A  76      41.860   2.174   8.164  1.00  8.58
ATOM    579  N   VAL A  77      39.338   0.183   9.953  1.00  9.02
ATOM    580  CA  VAL A  77      39.060   0.135  11.387  1.00  9.54
ATOM    581  C   VAL A  77      40.204  -0.493  12.184  1.00 11.58
ATOM    582  O   VAL A  77      40.954  -1.324  11.669  1.00 12.04
ATOM    583  CB  VAL A  77      37.739  -0.640  11.698  1.00  7.06
ATOM    584  CG1 VAL A  77      36.544   0.021  11.017  1.00  4.37
ATOM    585  CG2 VAL A  77      37.857  -2.107  11.292  1.00  7.93
ATOM    586  N   GLY A  78      40.343  -0.072  13.435  1.00 11.92
ATOM    587  CA  GLY A  78      41.385  -0.611  14.282  1.00 12.61
ATOM    588  C   GLY A  78      40.961  -1.923  14.913  1.00 15.14
ATOM    589  O   GLY A  78      39.800  -2.346  14.783  1.00 14.19
ATOM    590  N   PRO A  79      41.887  -2.613  15.596  1.00 13.02
ATOM    591  CA  PRO A  79      41.520  -3.884  16.223  1.00 13.86
ATOM    592  C   PRO A  79      40.367  -3.740  17.215  1.00 14.72
ATOM    593  O   PRO A  79      40.141  -2.662  17.776  1.00 14.74
ATOM    594  CB  PRO A  79      42.826  -4.330  16.892  1.00 14.15
ATOM    595  CG  PRO A  79      43.627  -3.076  17.020  1.00 12.30
ATOM    596  CD  PRO A  79      43.321  -2.339  15.759  1.00 11.59
ATOM    597  N   GLY A  80      39.626  -4.828  17.403  1.00 14.41
ATOM    598  CA  GLY A  80      38.495  -4.817  18.313  1.00 13.10
ATOM    599  C   GLY A  80      37.223  -4.221  17.724  1.00 14.52
ATOM    600  O   GLY A  80      36.202  -4.124  18.417  1.00 16.47
ATOM    601  N   VAL A  81      37.257  -3.822  16.456  1.00 11.34
ATOM    602  CA  VAL A  81      36.070  -3.227  15.849  1.00  9.27
ATOM    603  C   VAL A  81      35.344  -4.220  14.965  1.00  9.33
ATOM    604  O   VAL A  81      35.950  -4.834  14.091  1.00  8.68
ATOM    605  CB  VAL A  81      36.410  -1.960  15.028  1.00 10.35
ATOM    606  CG1 VAL A  81      35.129  -1.310  14.510  1.00  7.93
ATOM    607  CG2 VAL A  81      37.196  -0.972  15.877  1.00  6.82
ATOM    608  N   THR A  82      34.048  -4.395  15.214  1.00  8.05
ATOM    609  CA  THR A  82      33.231  -5.314  14.424  1.00  9.45
ATOM    610  C   THR A  82      31.939  -4.677  13.904  1.00  9.88
ATOM    611  O   THR A  82      31.277  -5.233  13.024  1.00 10.87
ATOM    612  CB  THR A  82      32.871  -6.586  15.234  1.00 10.26
ATOM    613  OG1 THR A  82      32.110  -6.222  16.392  1.00 14.53
ATOM    614  CG2 THR A  82      34.134  -7.309  15.680  1.00  8.09
ATOM    615  N   GLU A  83      31.598  -3.502  14.427  1.00  7.66
ATOM    616  CA  GLU A  83      30.379  -2.811  14.018  1.00  8.33
ATOM    617  C   GLU A  83      30.539  -2.085  12.688  1.00  6.92
ATOM    618  O   GLU A  83      29.585  -1.976  11.921  1.00  7.63
ATOM    619  CB  GLU A  83      29.935  -1.799  15.082  1.00  7.94
ATOM    620  CG  GLU A  83      28.670  -1.057  14.697  1.00 11.62
ATOM    621  CD  GLU A  83      28.365   0.150  15.572  1.00 12.29
ATOM    622  OE1 GLU A  83      29.088   0.405  16.561  1.00 14.12
ATOM    623  OE2 GLU A  83      27.384   0.852  15.255  1.00 16.59
ATOM    624  N   PHE A  84      31.735  -1.561  12.433  1.00  4.59
ATOM    625  CA  PHE A  84      31.985  -0.826  11.199  1.00  8.74
ATOM    626  C   PHE A  84      32.926  -1.554  10.247  1.00  9.29
ATOM    627  O   PHE A  84      33.838  -2.252  10.684  1.00  6.60
ATOM    628  CB  PHE A  84      32.585   0.566  11.498  1.00  8.58
ATOM    629  CG  PHE A  84      31.721   1.441  12.378  1.00  8.48
ATOM    630  CD1 PHE A  84      30.645   2.145  11.844  1.00  6.94
ATOM    631  CD2 PHE A  84      31.995   1.563  13.741  1.00  8.79
ATOM    632  CE1 PHE A  84      29.852   2.955  12.646  1.00  3.49
ATOM    633  CE2 PHE A  84      31.208   2.372  14.557  1.00  8.49
ATOM    634  CZ  PHE A  84      30.134   3.069  14.009  1.00  8.03
ATOM    635  N   GLN A  85      32.686  -1.384   8.947  1.00 11.28
ATOM    636  CA  GLN A  85      33.539  -1.950   7.902  1.00 12.29
ATOM    637  C   GLN A  85      33.658  -0.924   6.765  1.00 12.22
ATOM    638  O   GLN A  85      32.786  -0.064   6.613  1.00 13.94
ATOM    639  CB  GLN A  85      33.021  -3.298   7.415  1.00 14.70
ATOM    640  CG  GLN A  85      31.570  -3.360   7.025  1.00 19.81
ATOM    641  CD  GLN A  85      31.133  -4.789   6.771  1.00 24.57
ATOM    642  OE1 GLN A  85      31.967  -5.686   6.651  1.00 28.15
ATOM    643  NE2 GLN A  85      29.829  -5.018   6.734  1.00 28.84
ATOM    644  N   PRO A  86      34.779  -0.943   6.016  1.00 11.66
ATOM    645  CA  PRO A  86      35.029  -0.015   4.909  1.00 10.24
ATOM    646  C   PRO A  86      33.890   0.198   3.910  1.00 10.53
ATOM    647  O   PRO A  86      33.237  -0.751   3.464  1.00 10.97
ATOM    648  CB  PRO A  86      36.275  -0.605   4.255  1.00 11.10
ATOM    649  CG  PRO A  86      37.033  -1.115   5.434  1.00  9.69
ATOM    650  CD  PRO A  86      35.941  -1.831   6.210  1.00 11.09
ATOM    651  N   GLY A  87      33.647   1.462   3.577  1.00  9.21
ATOM    652  CA  __2 A  87      32.586   1.786   2.643  1.00  6.07
ATOM    653  C   GLY A  87      31.253   2.162   3.273  1.00  7.19
ATOM    654  O   GLY A  87      30.363   2.634   2.565  1.00  2.40
ATOM    655  N   GLU A  88      31.095   1.971   4.583  1.00  5.53
ATOM    656  CA  GLU A  88      29.828   2.312   5.231  1.00  5.84
ATOM    657  C   GLU A  88      29.762   3.799   5.559  1.00  6.14
ATOM    658  O   GLU A  88      30.785   4.418   5.853  1.00  5.22
ATOM    659  CB  GLU A  88      29.600   1.476   6.501  1.00  7.10
ATOM    660  CG  GLU A  88      29.380  -0.016   6.256  1.00  9.32
ATOM    661  CD  GLU A  88      28.932  -0.767   7.504  1.00  9.51
ATOM    662  OE1 GLU A  88      29.708  -0.854   8.476  1.00 15.09
ATOM    663  OE2 GLU A  88      27.793  -1.272   7.517  1.00 13.44
ATOM    664  N   LYS A  89      28.556   4.366   5.496  1.00  7.17
ATOM    665  CA  LYS A  89      28.352   5.782   5.780  1.00  5.50
ATOM    666  C   LYS A  89      28.227   6.039   7.279  1.00  9.11
ATOM    667  O   LYS A  89      27.454   5.362   7.966  1.00  6.24
ATOM    668  CB  LYS A  89      27.116   6.286   5.041  1.00  3.75
ATOM    669  CG  LYS A  89      27.298   6.325   3.516  1.00  2.94
ATOM    670  CD  LYS A  89      26.010   6.717   2.794  1.00  2.00
ATOM    671  CE  LYS A  89      26.289   7.026   1.334  1.00  4.34
ATOM    672  NZ  LYS A  89      25.059   7.362   0.560  1.00  2.00
ATOM    673  N   VAL A  90      28.975   7.026   7.780  1.00  8.64
ATOM    674  CA  VAL A  90      28.962   7.361   9.203  1.00  6.21
ATOM    675  C   VAL A  90      29.002   8.859   9.495  1.00  5.85
ATOM    676  O   VAL A  90      29.254   9.686   8.598  1.00  3.68
ATOM    677  CB  VAL A  90      30.173   6.724   9.943  1.00  5.99
ATOM    678  CG1 VAL A  90      30.194   5.209   9.750  1.00  4.15
ATOM    679  CG2 VAL A  90      31.484   7.341   9.457  1.00  4.48
ATOM    680  N   ILE A  91      28.759   9.191  10.762  1.00  5.06
ATOM    681  CA  ILE A  91      28.794  10.569  11.260  1.00  3.84
ATOM    682  C   ILE A  91      29.514  10.570  12.610  1.00  3.39
ATOM    683  O   ILE A  91      29.064   9.931  13.555  1.00  2.00
ATOM    684  CB  ILE A  91      27.354  11.182  11.457  1.00  6.17
ATOM    685  CG1 ILE A  91      26.655  11.370  10.102  1.00  4.21
ATOM    686  CG2 ILE A  91      27.437  12.535  12.185  1.00  5.21
ATOM    687  CD1 ILE A  91      25.237  11.936  10.192  1.00  6.69
ATOM    688  N   PRO A  92      30.695  11.203  12.685  1.00  2.17
ATOM    689  CA  PRO A  92      31.436  11.256  13.948  1.00  3.80
ATOM    690  C   PRO A  92      30.683  12.155  14.949  1.00  5.03
ATOM    691  O   PRO A  92      29.866  12.995  14.551  1.00  6.15
ATOM    692  CB  PRO A  92      32.793  11.825  13.525  1.00  2.58
ATOM    693  CG  PRO A  92      32.464  12.669  12.342  1.00  4.73
ATOM    694  CD  PRO A  92      31.467  11.823  11.593  1.00  4.34
ATOM    695  N   LEU A  93      30.928  11.951  16.239  1.00  3.68
ATOM    696  CA  LEU A  93      30.243  12.703  17.292  1.00  4.93
ATOM    697  C   LEU A  93      31.195  13.357  18.309  1.00  7.29
ATOM    698  O   LEU A  93      32.225  12.775  18.669  1.00  5.33
ATOM    699  CB  LEU A  93      29.289  11.764  18.043  1.00  2.76
ATOM    700  CG  LEU A  93      28.379  10.870  17.204  1.00  2.00
ATOM    701  CD1 LEU A  93      27.743   9.827  18.089  1.00  2.72
ATOM    702  CD2 LEU A  93      27.331  11.694  16.483  1.00  2.95
ATOM    703  N   PHE A  94      30.823  14.541  18.800  1.00  5.01
ATOM    704  CA  PHE A  94      31.651  15.244  19.771  1.00  7.01
ATOM    705  C   PHE A  94      31.437  14.798  21.229  1.00  8.14
ATOM    706  O   PHE A  94      32.088  15.311  22.139  1.00  9.79
ATOM    707  CB  PHE A  94      31.557  16.772  19.598  1.00  5.77
ATOM    708  CG  PHE A  94      30.192  17.356  19.863  1.00  6.42
ATOM    709  CD1 PHE A  94      29.266  17.489  18.840  1.00  7.25
ATOM    710  CD2 PHE A  94      29.857  17.828  21.131  1.00 11.42
ATOM    711  CE1 PHE A  94      28.021  18.091  19.074  1.00 14.11
ATOM    712  CE2 PHE A  94      28.611  18.433  21.378  1.00 12.84
ATOM    713  CZ  PHE A  94      27.696  18.565  20.347  1.00 11.09
ATOM    714  N   ILE A  95      30.518  13.853  21.437  1.00  8.88
ATOM    715  CA  ILE A  95      30.230  13.285  22.763  1.00  6.87
ATOM    716  C   ILE A  95      30.211  11.770  22.616  1.00  6.85
ATOM    717  O   ILE A  95      29.827  11.255  21.550  1.00  6.47
ATOM    718  CB  ILE A  95      28.862  13.740  23.359  1.00  9.45
ATOM    719  CG1 ILE A  95      27.704  13.333  22.445  1.00  7.23
ATOM    720  CG2 ILE A  95      28.883  15.230  23.647  1.00  5.01
ATOM    721  CD1 ILE A  95      26.344  13.597  23.029  1.00  8.73
ATOM    722  N   SER A  96      30.572  11.063  23.687  1.00  5.82
ATOM    723  CA  SER A  96      30.630   9.597  23.677  1.00  6.75
ATOM    724  C   SER A  96      29.410   8.843  24.226  1.00 10.70
ATOM    725  O   SER A  96      28.590   9.397  24.971  1.00 12.45
ATOM    726  CB  SER A  96      31.871   9.126  24.442  1.00  5.62
ATOM    727  OG  SER A  96      33.070   9.503  23.785  1.00  4.32
ATOM    728  N   GLN A  97      29.322   7.563  23.866  1.00  8.73
ATOM    729  CA  GLN A  97      28.259   6.673  24.336  1.00  8.07
ATOM    730  C   GLN A  97      28.853   5.267  24.449  1.00  8.78
ATOM    731  O   GLN A  97      28.646   4.429  23.569  1.00  7.76
ATOM    732  CB  GLN A  97      27.055   6.661  23.381  1.00  4.15
ATOM    733  CG  GLN A  97      25.910   5.732  23.827  1.00  3.84
ATOM    734  CD  GLN A  97      24.670   5.814  22.935  1.00  4.29
ATOM    735  OE1 GLN A  97      24.616   6.606  21.994  1.00  2.00
ATOM    736  NE2 GLN A  97      23.652   5.011  23.251  1.00  6.78
ATOM    737  N   CYS A  98      29.607   5.025  25.525  1.00  7.44
ATOM    738  CA  CYS A  98      30.241   3.723  25.757  1.00  8.38
ATOM    739  C   CYS A  98      29.226   2.611  25.994  1.00  7.44
ATOM    740  O   CYS A  98      29.575   1.437  25.960  1.00  7.85
ATOM    741  CB  CYS A  98      31.218   3.780  26.940  1.00  8.03
ATOM    742  SG  CYS A  98      30.451   3.679  28.581  1.00  7.79
ATOM    743  N   GLY A  99      27.984   2.984  26.284  1.00  5.40
ATOM    744  CA  GLY A  99      26.950   1.991  26.512  1.00  6.64
ATOM    745  C   GLY A  99      27.056   1.115  27.752  1.00  8.34
ATOM    746  O   GLY A  99      26.164   0.305  27.992  1.00 10.03
ATOM    747  N   GLU A 100      28.112   1.245  28.549  1.00  8.98
ATOM    748  CA  GLU A 100      28.219   0.408  29.749  1.00 12.32
ATOM    749  C   GLU A 100      28.215   1.143  31.100  1.00 12.85
ATOM    750  O   GLU A 100      28.001   0.525  32.135  1.00 12.27
ATOM    751  CB  GLU A 100      29.424  -0.548  29.648  1.00 13.55
ATOM    752  CG  GLU A 100      29.223  -1.759  28.713  1.00 22.44
ATOM    753  CD  GLU A 100      28.471  -2.935  29.365  1.00 29.22
ATOM    754  OE1 GLU A 100      29.086  -3.658  30.181  1.00 32.11
ATOM    755  OE2 GLU A 100      27.275  -3.156  29.051  1.00 32.46
ATOM    756  N   CYS A 101      28.419   2.458  31.101  1.00 11.92
ATOM    757  CA  CYS A 101      28.438   3.199  32.367  1.00  9.44
ATOM    758  C   CYS A 101      27.033   3.566  32.846  1.00  8.14
ATOM    759  O   CYS A 101      26.061   3.435  32.095  1.00  8.08
ATOM    760  CB  CYS A 101      29.310   4.451  32.262  1.00  6.32
ATOM    761  SG  CYS A 101      28.552   5.823  31.396  1.00  9.28
ATOM    762  N   ARG A 102      26.942   4.058  34.081  1.00  7.64
ATOM    763  CA  ARG A 102      25.664   4.441  34.698  1.00  6.67
ATOM    764  C   ARG A 102      24.872   5.499  33.927  1.00  7.45
ATOM    765  O   ARG A 102      23.637   5.499  33.933  1.00  4.43
ATOM    766  CB  ARG A 102      25.902   4.936  36.134  1.00  7.34
ATOM    767  CG  ARG A 102      26.679   6.235  36.214  1.00  5.48
ATOM    768  CD  ARG A 102      27.405   6.406  37.536  1.00  9.28
ATOM    769  NE  ARG A 102      26.529   6.799  38.636  1.00 10.34
ATOM    770  CZ  ARG A 102      26.882   7.637  39.609  1.00  8.66
ATOM    771  NH1 ARG A 102      28.092   8.179  39.626  1.00 11.88
ATOM    772  NH2 ARG A 102      26.021   7.939  40.568  1.00 12.16
ATOM    773  N   PHE A 103      25.583   6.415  33.278  1.00  8.16
ATOM    774  CA  PHE A 103      24.928   7.481  32.526  1.00  8.17
ATOM    775  C   PHE A 103      24.325   6.999  31.212  1.00  8.69
ATOM    776  O   PHE A 103      23.212   7.382  30.868  1.00  8.25
ATOM    777  CB  PHE A 103      25.905   8.629  32.285  1.00  5.85
ATOM    778  CG  PHE A 103      26.480   9.208  33.555  1.00  5.72
ATOM    779  CD1 PHE A 103      25.699  10.011  34.392  1.00  6.39
ATOM    780  CD2 PHE A 103      27.800   8.959  33.909  1.00  3.92
ATOM    781  CE1 PHE A 103      26.233  10.555  35.564  1.00  8.19
ATOM    782  CE2 PHE A 103      28.343   9.499  35.082  1.00  6.98
ATOM    783  CZ  PHE A 103      27.558  10.300  35.909  1.00  6.43
ATOM    784  N   CYS A 104      25.057   6.140  30.505  1.00  8.83
ATOM    785  CA  CYS A 104      24.619   5.587  29.223  1.00  5.22
ATOM    786  C   CYS A 104      23.420   4.673  29.420  1.00  4.48
ATOM    787  O   CYS A 104      22.595   4.496  28.522  1.00  2.00
ATOM    788  CB  CYS A 104      25.758   4.793  28.562  1.00  3.41
ATOM    789  SG  CYS A 104      27.070   5.758  27.713  1.00  2.82
ATOM    790  N   GLN A 105      23.349   4.067  30.598  1.00  6.56
ATOM    791  CA  GLN A 105      22.264   3.157  30.934  1.00  9.30
ATOM    792  C   GLN A 105      20.959   3.835  31.360  1.00  8.20
ATOM    793  O   GLN A 105      19.900   3.205  31.348  1.00  9.12
ATOM    794  CB  GLN A 105      22.735   2.173  32.007  1.00 10.16
ATOM    795  CG  GLN A 105      23.814   1.241  31.498  1.00 17.11
ATOM    796  CD  GLN A 105      24.483   0.458  32.597  1.00 20.84
ATOM    797  OE1 GLN A 105      24.507   0.875  33.756  1.00 20.61
ATOM    798  NE2 GLN A 105      25.059  -0.680  32.235  1.00 27.77
ATOM    799  N   SER A 106      21.026   5.114  31.714  1.00  6.82
ATOM    800  CA  SER A 106      19.836   5.839  32.141  1.00  4.55
ATOM    801  C   SER A 106      19.131   6.571  31.009  1.00  5.26
ATOM    802  O   SER A 106      19.759   7.261  30.218  1.00  3.12
ATOM    803  CB  SER A 106      20.194   6.850  33.234  1.00  6.84
ATOM    804  OG  SER A 106      19.132   7.768  33.463  1.00  6.92
ATOM    805  N   PRO A 107      17.792   6.492  30.968  1.00  7.81
ATOM    806  CA  PRO A 107      17.034   7.177  29.918  1.00  8.41
ATOM    807  C   PRO A 107      16.923   8.678  30.218  1.00  7.13
ATOM    808  O   PRO A 107      16.411   9.441  29.403  1.00 10.05
ATOM    809  CB  PRO A 107      15.672   6.492  29.993  1.00  8.86
ATOM    810  CG  PRO A 107      15.529   6.219  31.463  1.00 10.99
ATOM    811  CD  PRO A 107      16.902   5.679  31.817  1.00  9.38
ATOM    812  N   LYS A 108      17.447   9.102  31.365  1.00  5.55
ATOM    813  CA  LYS A 108      17.392  10.507  31.769  1.00  8.20
ATOM    814  C   LYS A 108      18.489  11.415  31.199  1.00  7.01
ATOM    815  O   LYS A 108      18.361  12.643  31.232  1.00  7.10
ATOM    816  CB  LYS A 108      17.466  10.616  33.298  1.00 11.22
ATOM    817  CG  LYS A 108      16.329   9.975  34.076  1.00 14.90
ATOM    818  CD  LYS A 108      16.443  10.337  35.552  1.00 13.78
ATOM    819  CE  LYS A 108      15.243   9.840  36.352  1.00 17.02
ATOM    820  NZ  LYS A 108      15.189  10.430  37.722  1.00 13.65
ATOM    821  N   THR A 109      19.536  10.833  30.631  1.00  6.03
ATOM    822  CA  THR A 109      20.656  11.652  30.176  1.00  4.25
ATOM    823  C   THR A 109      21.397  11.115  28.947  1.00  4.32
ATOM    824  O   THR A 109      21.143  10.000  28.496  1.00  2.00
ATOM    825  CB  THR A 109      21.660  11.770  31.361  1.00  2.59
ATOM    826  OG1 THR A 109      22.863  12.436  30.958  1.00  3.39
ATOM    827  CG2 THR A 109      22.021  10.376  31.882  1.00  2.11
ATOM    828  N   ASN A 110      22.270  11.950  28.386  1.00  3.59
ATOM    829  CA  ASN A 110      23.102  11.560  27.248  1.00  6.05
ATOM    830  C   ASN A 110      24.568  11.701  27.661  1.00  5.76
ATOM    831  O   ASN A 110      25.459  11.802  26.827  1.00  4.61
ATOM    832  CB  ASN A 110      22.790  12.376  25.973  1.00  5.11
ATOM    833  CG  ASN A 110      23.157  13.848  26.086  1.00  6.61
ATOM    834  OD1 ASN A 110      23.283  14.406  27.182  1.00  8.80
ATOM    835  ND2 ASN A 110      23.282  14.498  24.939  1.00  3.14
ATOM    836  N   GLN A 111      24.799  11.699  28.971  1.00  6.47
ATOM    837  CA  GLN A 111      26.143  11.806  29.520  1.00  5.69
ATOM    838  C   GLN A 111      26.856  10.463  29.428  1.00  5.39
ATOM    839  O   GLN A 111      26.233   9.428  29.192  1.00  7.78
ATOM    840  CB  GLN A 111      26.085  12.263  30.982  1.00  6.44
ATOM    841  CG  GLN A 111      25.732  13.737  31.168  1.00  6.35
ATOM    842  CD  GLN A 111      26.884  14.644  30.809  1.00  7.93
ATOM    843  OE1 GLN A 111      28.044  14.236  30.852  1.00 12.06
ATOM    844  NE2 GLN A 111      26.576  15.874  30.442  1.00 13.42
ATOM    845  N   CYS A 112      28.160  10.483  29.663  1.00  4.37
ATOM    846  CA  CYS A 112      28.979   9.286  29.621  1.00  4.96
ATOM    847  C   CYS A 112      30.225   9.567  30.445  1.00  4.09
ATOM    848  O   CYS A 112      30.471  10.713  30.826  1.00  3.61
ATOM    849  CB  CYS A 112      29.371   8.962  28.176  1.00  4.50
ATOM    850  SG  CYS A 112      30.405   7.475  27.976  1.00  4.71
ATOM    851  N   VAL A 113      30.972   8.521  30.785  1.00  3.83
ATOM    852  CA  VAL A 113      32.198   8.721  31.552  1.00  5.58
ATOM    853  C   VAL A 113      33.439   8.842  30.658  1.00  4.81
ATOM    854  O   VAL A 113      34.526   9.137  31.152  1.00  2.00
ATOM    855  CB  VAL A 113      32.421   7.613  32.617  1.00  2.23
ATOM    856  CG1 VAL A 113      31.250   7.600  33.601  1.00  3.59
ATOM    857  CG2 VAL A 113      32.614   6.240  31.947  1.00  2.00
ATOM    858  N   LYS A 114      33.270   8.619  29.353  1.00  3.38
ATOM    859  CA  LYS A 114      34.385   8.705  28.398  1.00  4.85
ATOM    860  C   LYS A 114      34.351   9.984  27.550  1.00  3.98
ATOM    861  O   LYS A 114      33.333  10.676  27.488  1.00  4.38
ATOM    862  CB  LYS A 114      34.385   7.501  27.457  1.00  2.75
ATOM    863  CG  LYS A 114      34.247   6.154  28.139  1.00  4.73
ATOM    864  CD  LYS A 114      35.442   5.816  28.990  1.00 11.63
ATOM    865  CE  LYS A 114      35.215   4.504  29.730  1.00 15.85
ATOM    866  NZ  LYS A 114      36.388   4.121  30.572  1.00 19.44
ATOM    867  N   GLY A 115      35.465  10.271  26.882  1.00  3.22
ATOM    868  CA  GLY A 115      35.548  11.434  26.026  1.00  4.07
ATOM    869  C   GLY A 115      36.500  12.524  26.483  1.00  6.59
ATOM    870  O   GLY A 115      36.856  12.617  27.652  1.00  8.11
ATOM    871  N   TRP A 116      36.861  13.393  25.547  1.00  7.59
ATOM    872  CA  TRP A 116      37.760  14.507  25.807  1.00  9.68
ATOM    873  C   TRP A 116      37.255  15.361  26.968  1.00  8.97
ATOM    874  O   TRP A 116      38.035  15.820  27.785  1.00  9.80
ATOM    875  CB  TRP A 116      37.921  15.373  24.541  1.00  9.24
ATOM    876  CG  TRP A 116      36.638  15.995  24.059  1.00  8.88
ATOM    877  CD1 TRP A 116      35.694  15.415  23.259  1.00 10.96
ATOM    878  CD2 TRP A 116      36.118  17.282  24.424  1.00  6.76
ATOM    879  NE1 TRP A 116      34.612  16.256  23.117  1.00  7.45
ATOM    880  CE2 TRP A 116      34.847  17.407  23.820  1.00  5.81
ATOM    881  CE3 TRP A 116      36.603  18.341  25.205  1.00  9.35
ATOM    882  CZ2 TRP A 116      34.046  18.548  23.983  1.00  8.38
ATOM    883  CZ3 TRP A 116      35.811  19.473  25.368  1.00  8.25
ATOM    884  CH2 TRP A 116      34.543  19.568  24.756  1.00  5.52
ATOM    885  N   ALA A 117      35.942  15.532  27.064  1.00 13.02
ATOM    886  CA  ALA A 117      35.359  16.342  28.126  1.00 15.61
ATOM    887  C   ALA A 117      35.694  15.815  29.522  1.00 17.62
ATOM    888  O   ALA A 117      35.891  16.598  30.449  1.00 17.27
ATOM    889  CB  ALA A 117      33.844  16.460  27.942  1.00 14.77
ATOM    890  N   ASN A 118      35.785  14.494  29.667  1.00 17.95
ATOM    891  CA  ASN A 118      36.095  13.886  30.963  1.00 18.24
ATOM    892  C   ASN A 118      37.587  13.766  31.263  1.00 18.95
ATOM    893  O   ASN A 118      37.968  13.133  32.247  1.00 21.35
ATOM    894  CB  ASN A 118      35.460  12.498  31.068  1.00 16.40
ATOM    895  CG  ASN A 118      33.970  12.532  30.884  1.00 16.92
ATOM    896  OD1 ASN A 118      33.455  12.123  29.847  1.00 16.65
ATOM    897  ND2 ASN A 118      33.263  13.048  31.877  1.00 18.58
ATOM    898  N   GLU A 119      38.426  14.372  30.433  1.00 20.14
ATOM    899  CA  GLU A 119      39.872  14.301  30.628  1.00 23.58
ATOM    900  C   GLU A 119      40.545  15.639  30.371  1.00 23.82
ATOM    901  O   GLU A 119      41.346  16.102  31.182  1.00 24.44
ATOM    902  CB  GLU A 119      40.485  13.241  29.707  1.00 25.09
ATOM    903  CG  GLU A 119      40.027  13.362  28.267  1.00 28.14
ATOM    904  CD  GLU A 119      40.925  12.636  27.287  1.00 29.91
ATOM    905  OE1 GLU A 119      42.020  13.158  26.984  1.00 27.11
ATOM    906  OE2 GLU A 119      40.517  11.557  26.802  1.00 30.72
ATOM    907  N   SER A 120      40.198  16.260  29.247  1.00 25.87
ATOM    908  CA  SER A 120      40.752  17.548  28.843  1.00 26.63
ATOM    909  C   SER A 120      39.620  18.475  28.389  1.00 26.22
ATOM    910  O   SER A 120      39.541  18.846  27.213  1.00 29.07
ATOM    911  CB  SER A 120      41.737  17.349  27.685  1.00 27.74
ATOM    912  OG  SER A 120      42.686  16.333  27.964  1.00 30.53
ATOM    913  N   PRO A 121      38.727  18.864  29.313  1.00 22.99
ATOM    914  CA  PRO A 121      37.610  19.748  28.968  1.00 21.72
ATOM    915  C   PRO A 121      38.009  21.172  28.569  1.00 19.23
ATOM    916  O   PRO A 121      37.530  21.695  27.568  1.00 21.21
ATOM    917  CB  PRO A 121      36.750  19.714  30.231  1.00 21.27
ATOM    918  CG  PRO A 121      37.755  19.516  31.321  1.00 21.33
ATOM    919  CD  PRO A 121      38.655  18.458  30.728  1.00 24.63
ATOM    920  N   ASP A 122      38.901  21.789  29.336  1.00 17.98
ATOM    921  CA  ASP A 122      39.358  23.152  29.054  1.00 14.99
ATOM    922  C   ASP A 122      40.127  23.282  27.747  1.00 14.06
ATOM    923  O   ASP A 122      40.167  24.355  27.143  1.00 15.16
ATOM    924  CB  ASP A 122      40.259  23.650  30.180  1.00 19.12
ATOM    925  CG  ASP A 122      39.505  23.947  31.452  1.00 21.62
ATOM    926  OD1 ASP A 122      38.348  23.494  31.607  1.00 23.25
ATOM    927  OD2 ASP A 122      40.090  24.648  32.304  1.00 28.56
ATOM    928  N   VAL A 123      40.832  22.222  27.383  1.00 11.11
ATOM    929  CA  VAL A 123      41.621  22.197  26.158  1.00 11.35
ATOM    930  C   VAL A 123      40.729  22.068  24.910  1.00 11.55
ATOM    931  O   VAL A 123      41.080  22.569  23.841  1.00 11.73
ATOM    932  CB  VAL A 123      42.641  21.030  26.203  1.00  9.58
ATOM    933  CG1 VAL A 123      43.588  21.081  25.009  1.00  9.04
ATOM    934  CG2 VAL A 123      43.435  21.086  27.503  1.00 12.61
ATOM    935  N   MET A 124      39.567  21.432  25.077  1.00 11.10
ATOM    936  CA  MET A 124      38.594  21.191  24.001  1.00  9.77
ATOM    937  C   MET A 124      39.053  20.123  22.997  1.00  8.43
ATOM    938  O   MET A 124      38.488  19.994  21.909  1.00  7.36
ATOM    939  CB  MET A 124      38.194  22.495  23.292  1.00  8.36
ATOM    940  CG  MET A 124      37.370  23.453  24.166  1.00  6.42
ATOM    941  SD  MET A 124      36.601  24.856  23.271  1.00 12.60
ATOM    942  CE  MET A 124      35.040  24.107  22.687  1.00  8.87
ATOM    943  N   SER A 125      40.039  19.330  23.405  1.00  8.59
ATOM    944  CA  SER A 125      40.601  18.247  22.587  1.00 10.14
ATOM    945  C   SER A 125      41.169  17.138  23.484  1.00 10.69
ATOM    946  O   SER A 125      41.588  17.394  24.612  1.00 12.00
ATOM    947  CB  SER A 125      41.729  18.783  21.688  1.00 12.46
ATOM    948  OG  SER A 125      41.224  19.574  20.626  1.00 19.37
ATOM    949  N   PRO A 126      41.088  15.867  23.005  1.00 12.28
ATOM    950  CA  PRO A 126      41.627  14.739  23.786  1.00 12.16
ATOM    951  C   PRO A 126      43.132  14.927  23.929  1.00 14.57
ATOM    952  O   PRO A 126      43.728  15.784  23.275  1.00 15.16
ATOM    953  CB  PRO A 126      41.276  13.508  22.929  1.00 12.58
ATOM    954  CG  PRO A 126      40.552  13.988  21.732  1.00 10.71
ATOM    955  CD  PRO A 126      40.254  15.455  21.886  1.00 10.70
ATOM    956  N   LYS A 127      43.746  14.189  24.844  1.00 15.24
ATOM    957  CA  LYS A 127      45.178  14.303  25.075  1.00 18.22
ATOM    958  C   LYS A 127      45.947  13.600  23.942  1.00 15.75
ATOM    959  O   LYS A 127      47.085  13.951  23.631  1.00 15.82
ATOM    960  CB  LYS A 127      45.569  13.665  26.415  1.00 22.53
ATOM    961  CG  LYS A 127      44.791  14.062  27.667  1.00 27.96
ATOM    962  CD  LYS A 127      45.058  12.998  28.730  1.00 34.15
ATOM    963  CE  LYS A 127      44.798  11.605  28.136  1.00 36.57
ATOM    964  NZ  LYS A 127      43.441  11.015  28.391  1.00 38.38
ATOM    965  N   GLU A 128      45.315  12.594  23.345  1.00 14.50
ATOM    966  CA  GLU A 128      45.934  11.845  22.265  1.00 13.32
ATOM    967  C   GLU A 128      45.453  12.327  20.911  1.00 10.04
ATOM    968  O   GLU A 128      44.296  12.722  20.739  1.00  4.92
ATOM    969  CB  GLU A 128      45.625  10.357  22.392  1.00 16.05
ATOM    970  CG  GLU A 128      46.675   9.553  23.125  1.00 19.35
ATOM    971  CD  GLU A 128      46.695   8.127  22.627  1.00 22.85
ATOM    972  OE1 GLU A 128      45.727   7.389  22.923  1.00 24.48
ATOM    973  OE2 GLU A 128      47.649   7.754  21.894  1.00 22.19
ATOM    974  N   THR A 129      46.351  12.262  19.941  1.00  8.69
ATOM    975  CA  THR A 129      46.021  12.676  18.596  1.00 10.20
ATOM    976  C   THR A 129      46.697  11.812  17.550  1.00 10.37
ATOM    977  O   THR A 129      47.781  11.267  17.777  1.00 11.23
ATOM    978  CB  THR A 129      46.395  14.125  18.349  1.00  9.35
ATOM    979  OG1 THR A 129      46.059  14.450  17.001  1.00  8.63
ATOM    980  CG2 THR A 129      47.891  14.338  18.566  1.00 11.08
ATOM    981  N   ARG A 130      46.035  11.686  16.408  1.00 11.57
ATOM    982  CA  ARG A 130      46.534  10.894  15.294  1.00 11.15
ATOM    983  C   ARG A 130      47.086  11.784  14.175  1.00 10.45
ATOM    984  O   ARG A 130      47.488  11.285  13.120  1.00 10.32
ATOM    985  CB  ARG A 130      45.407  10.000  14.764  1.00 11.10
ATOM    986  CG  ARG A 130      44.752   9.131  15.844  1.00  9.40
ATOM    987  CD  ARG A 130      45.745   8.145  16.448  1.00  8.10
ATOM    988  NE  ARG A 130      45.212   7.464  17.627  1.00  7.37
ATOM    989  CZ  ARG A 130      45.653   7.653  18.872  1.00  9.27
ATOM    990  NH1 ARG A 130      46.648   8.499  19.124  1.00  6.95
ATOM    991  NH2 ARG A 130      45.073   7.021  19.881  1.00  8.38
ATOM    992  N   PHE A 131      47.103  13.095  14.409  1.00 10.29
ATOM    993  CA  PHE A 131      47.597  14.060  13.423  1.00 11.68
ATOM    994  C   PHE A 131      49.022  14.564  13.706  1.00 11.08
ATOM    995  O   PHE A 131      49.364  14.893  14.848  1.00 10.24
ATOM    996  CB  PHE A 131      46.653  15.275  13.321  1.00  5.90
ATOM    997  CG  PHE A 131      45.295  14.968  12.712  1.00  7.02
ATOM    998  CD1 PHE A 131      45.049  13.754  12.070  1.00  5.04
ATOM    999  CD2 PHE A 131      44.255  15.896  12.800  1.00  2.00
ATOM   1000  CE1 PHE A 131      43.788  13.463  11.529  1.00  2.12
ATOM   1001  CE2 PHE A 131      42.995  15.616  12.264  1.00  2.00
ATOM   1002  CZ  PHE A 131      42.762  14.395  11.629  1.00  2.00
ATOM   1003  N   THR A 132      49.818  14.668  12.642  1.00 10.47
ATOM   1004  CA  THR A 132      51.193  15.165  12.704  1.00 10.12
ATOM   1005  C   THR A 132      51.381  16.084  11.504  1.00 10.78
ATOM   1006  O   THR A 132      50.817  15.836  10.428  1.00  7.27
ATOM   1007  CB  THR A 132      52.232  14.042  12.577  1.00  9.39
ATOM   1008  OG1 THR A 132      52.032  13.074  13.607  1.00 18.34
ATOM   1009  CG2 THR A 132      53.630  14.601  12.725  1.00 14.12
ATOM   1010  N   CYS A 133      52.196  17.120  11.675  1.00 10.67
ATOM   1011  CA  CYS A 133      52.466  18.076  10.603  1.00 15.01
ATOM   1012  C   CYS A 133      53.787  18.804  10.869  1.00 15.91
ATOM   1013  O   CYS A 133      53.960  19.429  11.915  1.00 15.03
ATOM   1014  CB  CYS A 133      51.318  19.082  10.494  1.00 12.59
ATOM   1015  SG  CYS A 133      51.466  20.214   9.105  1.00 17.99
ATOM   1016  N   LYS A 134      54.725  18.699   9.930  1.00 18.46
ATOM   1017  CA  LYS A 134      56.041  19.332  10.078  1.00 19.40
ATOM   1018  C   LYS A 134      56.704  18.800  11.346  1.00 19.83
ATOM   1019  O   LYS A 134      57.271  19.564  12.125  1.00 20.13
ATOM   1020  CB  LYS A 134      55.893  20.857  10.187  1.00 16.18
ATOM   1021  CG  LYS A 134      55.200  21.507   9.021  1.00 19.25
ATOM   1022  CD  LYS A 134      54.805  22.922   9.375  1.00 21.05
ATOM   1023  CE  LYS A 134      54.068  23.562   8.221  1.00 24.89
ATOM   1024  NZ  LYS A 134      54.987  23.937   7.115  1.00 25.30
ATOM   1025  N   GLY A 135      56.598  17.490  11.562  1.00 22.59
ATOM   1026  CA  GLY A 135      57.176  16.877  12.750  1.00 22.28
ATOM   1027  C   GLY A 135      56.573  17.349  14.066  1.00 23.18
ATOM   1028  O   GLY A 135      57.060  16.983  15.143  1.00 23.32
ATOM   1029  N   ARG A 136      55.507  18.147  13.975  1.00 23.79
ATOM   1030  CA  ARG A 136      54.783  18.703  15.117  1.00 23.29
ATOM   1031  C   ARG A 136      53.449  17.960  15.294  1.00 22.21
ATOM   1032  O   ARG A 136      52.795  17.617  14.310  1.00 22.61
ATOM   1033  CB  ARG A 136      54.526  20.212  14.917  1.00 26.50
ATOM   1034  CG  ARG A 136      55.359  21.117  15.849  1.00 31.39
ATOM   1035  CD  ARG A 136      55.183  22.613  15.551  1.00 34.60
ATOM   1036  NE  ARG A 136      54.253  23.282  16.464  1.00 36.15
ATOM   1037  CZ  ARG A 136      54.148  24.604  16.588  1.00 36.84
ATOM   1038  NH1 ARG A 136      54.913  25.415  15.858  1.00 37.90
ATOM   1039  NH2 ARG A 136      53.260  25.122  17.428  1.00 36.94
ATOM   1040  N   LYS A 137      53.095  17.633  16.535  1.00 19.63
ATOM   1041  CA  LYS A 137      51.832  16.943  16.809  1.00 16.92
ATOM   1042  C   LYS A 137      50.722  17.987  16.733  1.00 14.44
ATOM   1043  O   LYS A 137      50.889  19.102  17.229  1.00 14.05
ATOM   1044  CB  LYS A 137      51.824  16.357  18.222  1.00 20.95
ATOM   1045  CG  LYS A 137      52.985  15.428  18.566  1.00 29.35
ATOM   1046  CD  LYS A 137      52.721  13.992  18.131  1.00 33.46
ATOM   1047  CE  LYS A 137      53.258  13.013  19.170  1.00 36.77
ATOM   1048  NZ  LYS A 137      52.823  13.404  20.554  1.00 40.07
ATOM   1049  N   VAL A 138      49.582  17.626  16.154  1.00 10.72
ATOM   1050  CA  VAL A 138      48.460  18.561  16.041  1.00  8.75
ATOM   1051  C   VAL A 138      47.196  17.931  16.635  1.00  7.85
ATOM   1052  O   VAL A 138      46.788  16.857  16.212  1.00  5.82
ATOM   1053  CB  VAL A 138      48.186  18.944  14.553  1.00  9.24
ATOM   1054  CG1 VAL A 138      47.082  19.997  14.474  1.00  7.49
ATOM   1055  CG2 VAL A 138      49.461  19.432  13.877  1.00  2.01
ATOM   1056  N   LEU A 139      46.567  18.627  17.579  1.00  4.13
ATOM   1057  CA  LEU A 139      45.357  18.152  18.257  1.00  6.48
ATOM   1058  C   LEU A 139      44.099  18.041  17.370  1.00  7.96
ATOM   1059  O   LEU A 139      43.946  18.780  16.400  1.00  5.99
ATOM   1060  CB  LEU A 139      45.043  19.080  19.438  1.00  8.96
ATOM   1061  CG  LEU A 139      46.080  19.298  20.539  1.00  5.24
ATOM   1062  CD1 LEU A 139      45.580  20.404  21.451  1.00  5.06
ATOM   1063  CD2 LEU A 139      46.319  18.022  21.322  1.00  5.92
ATOM   1064  N   GLN A 140      43.182  17.154  17.762  1.00  7.15
ATOM   1065  CA  GLN A 140      41.921  16.912  17.057  1.00  7.30
ATOM   1066  C   GLN A 140      40.766  17.494  17.862  1.00  9.66
ATOM   1067  O   GLN A 140      40.344  16.906  18.869  1.00 10.08
ATOM   1068  CB  GLN A 140      41.682  15.411  16.875  1.00  7.85
ATOM   1069  CG  GLN A 140      42.741  14.703  16.052  1.00  6.70
ATOM   1070  CD  GLN A 140      42.452  13.235  15.860  1.00 10.42
ATOM   1071  OE1 GLN A 140      43.235  12.372  16.281  1.00 10.28
ATOM   1072  NE2 GLN A 140      41.332  12.931  15.214  1.00 11.35
ATOM   1073  N   PHE A 141      40.223  18.614  17.390  1.00  8.79
ATOM   1074  CA  PHE A 141      39.116  19.293  18.067  1.00  5.95
ATOM   1075  C   PHE A 141      37.978  18.340  18.416  1.00  5.79
ATOM   1076  O   PHE A 141      37.496  17.603  17.553  1.00  5.70
ATOM   1077  CB  PHE A 141      38.579  20.413  17.182  1.00  6.19
ATOM   1078  CG  PHE A 141      37.780  21.452  17.921  1.00  3.58
ATOM   1079  CD1 PHE A 141      38.294  22.064  19.065  1.00  5.98
ATOM   1080  CD2 PHE A 141      36.535  21.852  17.449  1.00  2.00
ATOM   1081  CE1 PHE A 141      37.580  23.067  19.729  1.00  5.31
ATOM   1082  CE2 PHE A 141      35.810  22.855  18.102  1.00  5.33
ATOM   1083  CZ  PHE A 141      36.337  23.466  19.246  1.00  6.74
ATOM   1084  N   LEU A 142      37.602  18.327  19.695  1.00  3.64
ATOM   1085  CA  LEU A 142      36.512  17.495  20.223  1.00  2.00
ATOM   1086  C   LEU A 142      36.596  16.014  19.876  1.00  3.48
ATOM   1087  O   LEU A 142      35.602  15.290  19.999  1.00  4.28
ATOM   1088  CB  LEU A 142      35.153  18.035  19.758  1.00  2.45
ATOM   1089  CG  LEU A 142      34.868  19.533  19.874  1.00  2.00
ATOM   1090  CD1 LEU A 142      33.392  19.795  19.595  1.00  3.67
ATOM   1091  CD2 LEU A 142      35.253  20.043  21.247  1.00  2.27
ATOM   1092  N   GLY A 143      37.778  15.561  19.464  1.00  3.33
ATOM   1093  CA  GLY A 143      37.962  14.169  19.087  1.00  2.00
ATOM   1094  C   GLY A 143      37.342  13.836  17.735  1.00  3.58
ATOM   1095  O   GLY A 143      37.311  12.669  17.334  1.00  3.82
ATOM   1096  N   THR A 144      36.855  14.853  17.029  1.00  4.58
ATOM   1097  CA  THR A 144      36.229  14.658  15.716  1.00  4.91
ATOM   1098  C   THR A 144      37.075  15.209  14.561  1.00  5.42
ATOM   1099  O   THR A 144      37.202  14.547  13.534  1.00  5.21
ATOM   1100  CB  THR A 144      34.843  15.336  15.646  1.00  2.90
ATOM   1101  OG1 THR A 144      34.988  16.732  15.928  1.00  2.00
ATOM   1102  CG2 THR A 144      33.885  14.722  16.645  1.00  2.00
ATOM   1103  N   SER A 145      37.594  16.431  14.725  1.00  2.74
ATOM   1104  CA  SER A 145      38.421  17.120  13.719  1.00  4.39
ATOM   1105  C   SER A 145      38.005  16.859  12.261  1.00  5.55
ATOM   1106  O   SER A 145      38.724  16.210  11.488  1.00  2.00
ATOM   1107  CB  SER A 145      39.909  16.810  13.927  1.00  3.07
ATOM   1108  OG  SER A 145      40.149  15.418  14.036  1.00  3.77
ATOM   1109  N   THR A 146      36.859  17.415  11.880  1.00  5.62
ATOM   1110  CA  THR A 146      36.323  17.217  10.540  1.00  6.67
ATOM   1111  C   THR A 146      36.870  18.095   9.403  1.00  8.36
ATOM   1112  O   THR A 146      36.528  17.865   8.241  1.00  7.38
ATOM   1113  CB  THR A 146      34.773  17.231  10.554  1.00  7.49
ATOM   1114  OG1 THR A 146      34.288  18.495  11.038  1.00  3.83
ATOM   1115  CG2 THR A 146      34.251  16.113  11.456  1.00  2.00
ATOM   1116  N   PHE A 147      37.708  19.089   9.723  1.00 10.49
ATOM   1117  CA  PHE A 147      38.310  19.960   8.696  1.00  8.36
ATOM   1118  C   PHE A 147      39.554  19.251   8.113  1.00  8.50
ATOM   1119  O   PHE A 147      40.621  19.851   7.968  1.00  5.66
ATOM   1120  CB  PHE A 147      38.741  21.328   9.279  1.00  5.35
ATOM   1121  CG  PHE A 147      37.598  22.274   9.611  1.00  7.28
ATOM   1122  CD1 PHE A 147      36.265  21.884   9.494  1.00  5.47
ATOM   1123  CD2 PHE A 147      37.873  23.558  10.090  1.00  5.89
ATOM   1124  CE1 PHE A 147      35.227  22.760   9.852  1.00  4.40
ATOM   1125  CE2 PHE A 147      36.847  24.437  10.448  1.00  2.00
ATOM   1126  CZ  PHE A 147      35.522  24.035  10.332  1.00  2.00
ATOM   1127  N   SER A 148      39.417  17.964   7.822  1.00  9.91
ATOM   1128  CA  SER A 148      40.509  17.172   7.276  1.00 11.00
ATOM   1129  C   SER A 148      39.893  16.143   6.352  1.00 12.07
ATOM   1130  O   SER A 148      38.768  15.686   6.580  1.00 11.40
ATOM   1131  CB  SER A 148      41.274  16.451   8.393  1.00 10.14
ATOM   1132  OG  SER A 148      42.304  15.626   7.863  1.00  9.60
ATOM   1133  N   GLN A 149      40.628  15.793   5.302  1.00 10.35
ATOM   1134  CA  GLN A 149      40.154  14.806   4.348  1.00  8.87
ATOM   1135  C   GLN A 149      39.924  13.482   5.055  1.00  7.94
ATOM   1136  O   GLN A 149      38.977  12.753   4.734  1.00  8.66
ATOM   1137  CB  GLN A 149      41.153  14.647   3.198  1.00  5.03
ATOM   1138  CG  GLN A 149      41.297  15.917   2.374  1.00  4.39
ATOM   1139  CD  GLN A 149      42.102  15.733   1.100  1.00  6.08
ATOM   1140  OE1 GLN A 149      43.315  15.522   1.137  1.00  6.75
ATOM   1141  NE2 GLN A 149      41.439  15.865  -0.037  1.00  2.65
ATOM   1142  N   TYR A 150      40.768  13.201   6.045  1.00  8.03
ATOM   1143  CA  TYR A 150      40.683  11.970   6.819  1.00  8.04
ATOM   1144  C   TYR A 150      40.825  12.259   8.311  1.00  8.05
ATOM   1145  O   TYR A 150      41.660  13.074   8.715  1.00  7.51
ATOM   1146  CB  TYR A 150      41.789  10.993   6.394  1.00  8.82
ATOM   1147  CG  TYR A 150      41.572  10.327   5.048  1.00 10.93
ATOM   1148  CD1 TYR A 150      40.876   9.120   4.951  1.00  7.66
ATOM   1149  CD2 TYR A 150      42.068  10.899   3.871  1.00  9.51
ATOM   1150  CE1 TYR A 150      40.676   8.497   3.714  1.00  9.02
ATOM   1151  CE2 TYR A 150      41.874  10.285   2.625  1.00  8.89
ATOM   1152  CZ  TYR A 150      41.178   9.083   2.556  1.00 11.45
ATOM   1153  OH  TYR A 150      41.000   8.459   1.339  1.00 11.63
ATOM   1154  N   THR A 151      39.988  11.616   9.121  1.00  7.44
ATOM   1155  CA  THR A 151      40.062  11.768  10.577  1.00  7.12
ATOM   1156  C   THR A 151      39.981  10.392  11.230  1.00  6.93
ATOM   1157  O   THR A 151      39.673   9.402  10.569  1.00  4.49
ATOM   1158  CB  THR A 151      38.959  12.701  11.164  1.00  5.74
ATOM   1159  OG1 THR A 151      39.186  12.870  12.570  1.00  2.00
ATOM   1160  CG2 THR A 151      37.566  12.122  10.965  1.00  2.00
ATOM   1161  N   VAL A 152      40.300  10.329  12.516  1.00  6.77
ATOM   1162  CA  VAL A 152      40.263   9.078  13.260  1.00  6.23
ATOM   1163  C   VAL A 152      39.474   9.359  14.535  1.00  7.59
ATOM   1164  O   VAL A 152      39.811  10.271  15.296  1.00 10.14
ATOM   1165  CB  VAL A 152      41.691   8.585  13.616  1.00  6.21
ATOM   1166  CG1 VAL A 152      41.634   7.205  14.241  1.00  7.96
ATOM   1167  CG2 VAL A 152      42.562   8.543  12.369  1.00  7.93
ATOM   1168  N   VAL A 153      38.408   8.597  14.748  1.00  6.28
ATOM   1169  CA  VAL A 153      37.557   8.787  15.916  1.00  4.82
ATOM   1170  C   VAL A 153      37.271   7.441  16.594  1.00  2.88
ATOM   1171  O   VAL A 153      37.179   6.414  15.923  1.00  4.78
ATOM   1172  CB  VAL A 153      36.217   9.448  15.497  1.00  2.94
ATOM   1173  CG1 VAL A 153      35.338   9.711  16.720  1.00  2.00
ATOM   1174  CG2 VAL A 153      36.479  10.758  14.752  1.00  3.03
ATOM   1175  N   ASN A 154      37.191   7.431  17.922  1.00  3.74
ATOM   1176  CA  ASN A 154      36.887   6.193  18.644  1.00  5.55
ATOM   1177  C   ASN A 154      35.467   5.771  18.271  1.00  6.19
ATOM   1178  O   ASN A 154      34.579   6.615  18.168  1.00  9.19
ATOM   1179  CB  ASN A 154      36.977   6.401  20.158  1.00  7.34
ATOM   1180  CG  ASN A 154      36.795   5.104  20.940  1.00  4.94
ATOM   1181  OD1 ASN A 154      35.691   4.565  21.036  1.00  6.02
ATOM   1182  ND2 ASN A 154      37.876   4.614  21.518  1.00  4.53
ATOM   1183  N   GLN A 155      35.241   4.467  18.153  1.00  5.73
ATOM   1184  CA  GLN A 155      33.933   3.942  17.771  1.00  6.27
ATOM   1185  C   GLN A 155      32.725   4.339  18.623  1.00  6.10
ATOM   1186  O   GLN A 155      31.614   4.423  18.098  1.00  6.87
ATOM   1187  CB  GLN A 155      33.985   2.420  17.630  1.00  3.89
ATOM   1188  CG  GLN A 155      34.069   1.668  18.935  1.00  2.00
ATOM   1189  CD  GLN A 155      34.310   0.192  18.736  1.00  7.19
ATOM   1190  OE1 GLN A 155      34.956  -0.452  19.560  1.00  8.65
ATOM   1191  NE2 GLN A 155      33.807  -0.356  17.631  1.00  7.78
ATOM   1192  N   ILE A 156      32.919   4.577  19.921  1.00  4.35
ATOM   1193  CA  ILE A 156      31.789   4.958  20.778  1.00  3.73
ATOM   1194  C   ILE A 156      31.327   6.388  20.468  1.00  4.60
ATOM   1195  O   ILE A 156      30.288   6.840  20.953  1.00  2.07
ATOM   1196  CB  ILE A 156      32.105   4.784  22.296  1.00  2.00
ATOM   1197  CG1 ILE A 156      33.207   5.752  22.736  1.00  5.25
ATOM   1198  CG2 ILE A 156      32.511   3.345  22.582  1.00  2.00
ATOM   1199  CD1 ILE A 156      33.549   5.693  24.232  1.00  8.08
ATOM   1200  N   ALA A 157      32.110   7.090  19.652  1.00  3.73
ATOM   1201  CA  ALA A 157      31.785   8.449  19.236  1.00  3.97
ATOM   1202  C   ALA A 157      31.488   8.490  17.729  1.00  3.51
ATOM   1203  O   ALA A 157      31.741   9.494  17.064  1.00  4.55
ATOM   1204  CB  ALA A 157      32.933   9.403  19.579  1.00  2.00
ATOM   1205  N   VAL A 158      30.970   7.396  17.180  1.00  5.49
ATOM   1206  CA  VAL A 158      30.643   7.360  15.757  1.00  3.25
ATOM   1207  C   VAL A 158      29.321   6.655  15.554  1.00  3.17
ATOM   1208  O   VAL A 158      29.077   5.619  16.155  1.00  4.45
ATOM   1209  CB  VAL A 158      31.731   6.641  14.904  1.00  2.87
ATOM   1210  CG1 VAL A 158      31.321   6.631  13.428  1.00  2.89
ATOM   1211  CG2 VAL A 158      33.081   7.337  15.049  1.00  2.00
ATOM   1212  N   ALA A 159      28.454   7.249  14.736  1.00  3.75
ATOM   1213  CA  ALA A 159      27.154   6.665  14.433  1.00  3.05
ATOM   1214  C   ALA A 159      27.103   6.190  12.983  1.00  3.54
ATOM   1215  O   ALA A 159      27.532   6.911  12.080  1.00  2.52
ATOM   1216  CB  ALA A 159      26.045   7.684  14.685  1.00  5.92
ATOM   1217  N   LYS A 160      26.625   4.963  12.772  1.00  3.92
ATOM   1218  CA  LYS A 160      26.480   4.400  11.425  1.00  4.47
ATOM   1219  C   LYS A 160      25.106   4.835  10.918  1.00  5.02
ATOM   1220  O   LYS A 160      24.136   4.850  11.679  1.00  3.15
ATOM   1221  CB  LYS A 160      26.565   2.871  11.448  1.00  3.99
ATOM   1222  CG  LYS A 160      26.530   2.236  10.059  1.00  5.50
ATOM   1223  CD  LYS A 160      26.209   0.748  10.128  1.00  4.35
ATOM   1224  CE  LYS A 160      27.395  -0.064  10.633  1.00  6.89
ATOM   1225  NZ  LYS A 160      27.113  -1.543  10.630  1.00  7.06
ATOM   1226  N   ILE A 161      25.007   5.173   9.637  1.00  5.61
ATOM   1227  CA  ILE A 161      23.736   5.648   9.087  1.00  7.96
ATOM   1228  C   ILE A 161      23.257   4.948   7.808  1.00  7.54
ATOM   1229  O   ILE A 161      23.985   4.153   7.212  1.00  9.20
ATOM   1230  CB  ILE A 161      23.798   7.170   8.833  1.00  5.55
ATOM   1231  CG1 ILE A 161      24.916   7.482   7.835  1.00  7.20
ATOM   1232  CG2 ILE A 161      24.027   7.916  10.144  1.00  5.92
ATOM   1233  CD1 ILE A 161      24.945   8.908   7.344  1.00  6.46
ATOM   1234  N   ASP A 162      22.032   5.265   7.389  1.00  6.45
ATOM   1235  CA  ASP A 162      21.428   4.682   6.191  1.00  7.45
ATOM   1236  C   ASP A 162      22.334   4.788   4.947  1.00 10.10
ATOM   1237  O   ASP A 162      22.809   5.875   4.590  1.00  7.91
ATOM   1238  CB  ASP A 162      20.068   5.333   5.915  1.00  6.33
ATOM   1239  CG  ASP A 162      19.212   4.528   4.949  1.00  7.98
ATOM   1240  OD1 ASP A 162      19.545   4.462   3.749  1.00  5.91
ATOM   1241  OD2 ASP A 162      18.192   3.963   5.389  1.00  4.15
ATOM   1242  N   PRO A 163      22.535   3.654   4.245  1.00  9.03
ATOM   1243  CA  PRO A 163      23.362   3.533   3.040  1.00  9.86
ATOM   1244  C   PRO A 163      23.020   4.475   1.889  1.00  9.15
ATOM   1245  O   PRO A 163      23.862   4.741   1.038  1.00  9.33
ATOM   1246  CB  PRO A 163      23.165   2.068   2.646  1.00 11.51
ATOM   1247  CG  PRO A 163      22.969   1.396   3.970  1.00 10.39
ATOM   1248  CD  PRO A 163      22.002   2.335   4.634  1.00  8.07
ATOM   1249  N   SER A 164      21.785   4.958   1.842  1.00  8.56
ATOM   1250  CA  SER A 164      21.375   5.863   0.776  1.00  8.31
ATOM   1251  C   SER A 164      21.312   7.333   1.213  1.00  8.23
ATOM   1252  O   SER A 164      20.747   8.169   0.513  1.00  7.53
ATOM   1253  CB  SER A 164      20.019   5.418   0.220  1.00  8.09
ATOM   1254  OG  SER A 164      19.099   5.167   1.270  1.00  9.28
ATOM   1255  N   ALA A 165      21.914   7.653   2.355  1.00  9.50
ATOM   1256  CA  ALA A 165      21.899   9.015   2.881  1.00  7.14
ATOM   1257  C   ALA A 165      22.835   9.981   2.161  1.00  7.21
ATOM   1258  O   ALA A 165      23.993   9.650   1.879  1.00  7.38
ATOM   1259  CB  ALA A 165      22.228   8.991   4.363  1.00  6.13
ATOM   1260  N   PRO A 166      22.342  11.188   1.824  1.00  4.00
ATOM   1261  CA  PRO A 166      23.208  12.151   1.138  1.00  3.60
ATOM   1262  C   PRO A 166      24.186  12.820   2.106  1.00  4.41
ATOM   1263  O   PRO A 166      23.817  13.757   2.809  1.00  5.98
ATOM   1264  CB  PRO A 166      22.212  13.159   0.542  1.00  2.72
ATOM   1265  CG  PRO A 166      21.036  13.103   1.483  1.00  2.00
ATOM   1266  CD  PRO A 166      20.928  11.625   1.795  1.00  3.30
ATOM   1267  N   LEU A 167      25.444  12.377   2.081  1.00  5.23
ATOM   1268  CA  LEU A 167      26.495  12.890   2.971  1.00  6.15
ATOM   1269  C   LEU A 167      26.706  14.390   2.960  1.00  6.61
ATOM   1270  O   LEU A 167      27.130  14.963   3.964  1.00  6.55
ATOM   1271  CB  LEU A 167      27.832  12.204   2.683  1.00  4.81
ATOM   1272  CG  LEU A 167      27.798  10.678   2.831  1.00  2.00
ATOM   1273  CD1 LEU A 167      29.018  10.100   2.156  1.00  2.00
ATOM   1274  CD2 LEU A 167      27.712  10.286   4.291  1.00  2.26
ATOM   1275  N   ASP A 168      26.398  15.024   1.838  1.00  4.86
ATOM   1276  CA  ASP A 168      26.577  16.465   1.702  1.00  4.68
ATOM   1277  C   ASP A 168      25.522  17.287   2.437  1.00  5.24
ATOM   1278  O   ASP A 168      25.599  18.525   2.446  1.00  4.52
ATOM   1279  CB  ASP A 168      26.582  16.847   0.218  1.00  7.23
ATOM   1280  CG  ASP A 168      27.909  16.510  -0.438  0.50  9.00
ATOM   1281  OD1 ASP A 168      28.430  15.396  -0.236  0.50 12.75
ATOM   1282  OD2 ASP A 168      28.443  17.379  -1.158  0.50 14.48
ATOM   1283  N   THR A 169      24.528  16.615   3.027  1.00  3.78
ATOM   1284  CA  THR A 169      23.455  17.306   3.758  1.00  4.33
ATOM   1285  C   THR A 169      23.298  16.766   5.188  1.00  5.07
ATOM   1286  O   THR A 169      23.190  17.546   6.144  1.00  4.66
ATOM   1287  CB  THR A 169      22.113  17.179   3.010  1.00  3.58
ATOM   1288  OG1 THR A 169      22.258  17.753   1.701  1.00  4.44
ATOM   1289  CG2 THR A 169      20.991  17.904   3.754  1.00  4.49
ATOM   1290  N   VAL A 170      23.318  15.439   5.340  1.00  4.14
ATOM   1291  CA  VAL A 170      23.148  14.834   6.659  1.00  2.05
ATOM   1292  C   VAL A 170      24.260  15.182   7.646  1.00  2.32
ATOM   1293  O   VAL A 170      24.109  14.983   8.851  1.00  2.00
ATOM   1294  CB  VAL A 170      22.936  13.301   6.568  1.00  2.00
ATOM   1295  CG1 VAL A 170      21.749  12.994   5.668  1.00  2.55
ATOM   1296  CG2 VAL A 170      24.193  12.605   6.066  1.00  2.59
ATOM   1297  N   CYS A 171      25.350  15.761   7.146  1.00  2.97
ATOM   1298  CA  CYS A 171      26.470  16.150   8.005  1.00  2.68
ATOM   1299  C   CYS A 171      26.018  17.144   9.080  1.00  3.72
ATOM   1300  O   CYS A 171      26.628  17.251  10.148  1.00  3.50
ATOM   1301  CB  CYS A 171      27.623  16.724   7.164  1.00  4.30
ATOM   1302  SG  CYS A 171      27.247  18.183   6.156  1.00  2.00
ATOM   1303  N   LEU A 172      24.919  17.840   8.807  1.00  4.42
ATOM   1304  CA  LEU A 172      24.350  18.808   9.747  1.00  4.81
ATOM   1305  C   LEU A 172      23.956  18.130  11.068  1.00  3.79
ATOM   1306  O   LEU A 172      23.942  18.764  12.127  1.00  3.04
ATOM   1307  CB  LEU A 172      23.124  19.475   9.121  1.00  4.62
ATOM   1308  CG  LEU A 172      23.383  20.347   7.886  1.00  6.71
ATOM   1309  CD1 LEU A 172      22.074  20.695   7.201  1.00  4.91
ATOM   1310  CD2 LEU A 172      24.115  21.607   8.292  1.00  7.38
ATOM   1311  N   LEU A 173      23.635  16.841  10.989  1.00  3.79
ATOM   1312  CA  LEU A 173      23.246  16.044  12.149  1.00  2.83
ATOM   1313  C   LEU A 173      24.412  15.783  13.096  1.00  3.08
ATOM   1314  O   LEU A 173      24.206  15.355  14.245  1.00  2.00
ATOM   1315  CB  LEU A 173      22.609  14.729  11.690  1.00  2.24
ATOM   1316  CG  LEU A 173      21.083  14.724  11.550  1.00  7.18
ATOM   1317  CD1 LEU A 173      20.544  16.118  11.341  1.00  7.72
ATOM   1318  CD2 LEU A 173      20.655  13.787  10.430  1.00  5.34
ATOM   1319  N   GLY A 174      25.624  16.070  12.615  1.00  2.00
ATOM   1320  CA  GLY A 174      26.825  15.903  13.413  1.00  2.00
ATOM   1321  C   GLY A 174      26.835  16.843  14.611  1.00  4.57
ATOM   1322  O   GLY A 174      27.553  16.604  15.591  1.00  2.00
ATOM   1323  N   CYS A 175      26.080  17.942  14.520  1.00  2.88
ATOM   1324  CA  __6 A 175      26.001  18.887  15.628  1.00  4.74
ATOM   1325  C   CYS A 175      24.767  19.797  15.638  1.00  4.93
ATOM   1326  O   CYS A 175      23.750  19.471  16.269  1.00  4.74
ATOM   1327  CB  CYS A 175      27.290  19.718  15.731  1.00  5.63
ATOM   1328  SG  CYS A 175      27.263  21.020  17.015  1.00  6.06
ATOM   1329  N   GLY A 176      24.846  20.890  14.878  1.00  2.37
ATOM   1330  CA  GLY A 176      23.805  21.905  14.815  1.00  2.64
ATOM   1331  C   GLY A 176      22.332  21.549  14.834  1.00  2.00
ATOM   1332  O   GLY A 176      21.606  21.995  15.720  1.00  3.13
ATOM   1333  N   VAL A 177      21.878  20.781  13.853  1.00  2.00
ATOM   1334  CA  VAL A 177      20.467  20.413  13.765  1.00  2.22
ATOM   1335  C   VAL A 177      19.992  19.474  14.889  1.00  3.20
ATOM   1336  O   VAL A 177      18.868  19.624  15.393  1.00  2.04
ATOM   1337  CB  VAL A 177      20.115  19.851  12.351  1.00  3.02
ATOM   1338  CG1 VAL A 177      18.640  19.480  12.269  1.00  2.15
ATOM   1339  CG2 VAL A 177      20.449  20.884  11.284  1.00  2.00
ATOM   1340  N   SER A 178      20.822  18.514  15.286  1.00  2.00
ATOM   1341  CA  SER A 178      20.434  17.611  16.375  1.00  3.63
ATOM   1342  C   SER A 178      20.389  18.381  17.679  1.00  4.07
ATOM   1343  O   SER A 178      19.521  18.156  18.519  1.00  5.82
ATOM   1344  CB  SER A 178      21.401  16.430  16.510  1.00  4.03
ATOM   1345  OG  SER A 178      20.940  15.005  15.500  1.00  5.15
ATOM   1346  N   THR A 179      21.307  19.324  17.825  1.00  3.40
ATOM   1347  CA  THR A 179      21.377  20.130  19.026  1.00  2.93
ATOM   1348  C   THR A 179      20.109  20.959  19.230  1.00  5.06
ATOM   1349  O   THR A 179      19.423  20.793  20.245  1.00  7.54
ATOM   1350  CB  THR A 179      22.639  21.034  19.024  1.00  3.42
ATOM   1351  OG1 THR A 179      23.821  20.212  19.044  1.00  2.00
ATOM   1352  CG2 THR A 179      22.648  21.948  20.250  1.00  4.71
ATOM   1353  N   GLY A 180      19.779  21.802  18.253  1.00  4.30
ATOM   1354  CA  GLY A 180      18.605  22.657  18.345  1.00  4.93
ATOM   1355  C   GLY A 180      17.287  21.917  18.480  1.00  5.34
ATOM   1356  O   GLY A 180      16.528  22.134  19.432  1.00  2.09
ATOM   1357  N   PHE A 181      17.020  21.047  17.517  1.00  2.00
ATOM   1358  CA  PHE A 181      15.806  20.235  17.484  1.00  4.72
ATOM   1359  C   PHE A 181      15.672  19.433  18.786  1.00  4.40
ATOM   1360  O   PHE A 181      14.607  19.417  19.429  1.00  3.81
ATOM   1361  CB  PHE A 181      15.907  19.276  16.288  1.00  3.21
ATOM   1362  CG  PHE A 181      14.670  18.479  16.023  1.00  2.67
ATOM   1363  CD1 PHE A 181      13.659  18.996  15.221  1.00  2.28
ATOM   1364  CD2 PHE A 181      14.547  17.179  16.508  1.00  2.60
ATOM   1365  CE1 PHE A 181      12.543  18.231  14.901  1.00  4.20
ATOM   1366  CE2 PHE A 181      13.433  16.399  16.194  1.00  2.00
ATOM   1367  CZ  PHE A 181      12.431  16.925  15.387  1.00  2.00
ATOM   1368  N   GLY A 182      16.765  18.783  19.170  1.00  5.01
ATOM   1369  CA  GLY A 182      16.784  17.969  20.372  1.00  4.60
ATOM   1370  C   GLY A 182      16.499  18.757  21.635  1.00  5.36
ATOM   1371  O   GLY A 182      15.750  18.298  22.502  1.00  5.94
ATOM   1372  N   ALA A 183      17.079  19.947  21.742  1.00  2.00
ATOM   1373  CA  ALA A 183      16.873  20.787  22.919  1.00  2.00
ATOM   1374  C   ALA A 183      15.388  21.102  23.153  1.00  2.00
ATOM   1375  O   ALA A 183      14.953  21.255  24.292  1.00  2.00
ATOM   1376  CB  ALA A 183      17.682  22.067  22.797  1.00  2.00
ATOM   1377  N   ALA A 184      14.623  21.172  22.068  1.00  2.30
ATOM   1378  CA  ALA A 184      13.193  21.456  22.125  1.00  3.42
ATOM   1379  C   ALA A 184      12.388  20.216  22.510  1.00  2.55
ATOM   1380  O   ALA A 184      11.643  20.217  23.490  1.00  2.00
ATOM   1381  CB  ALA A 184      12.709  21.991  20.768  1.00  2.00
ATOM   1382  N   VAL A 185      12.562  19.163  21.720  1.00  2.00
ATOM   1383  CA  VAL A 185      11.872  17.899  21.897  1.00  3.82
ATOM   1384  C   VAL A 185      12.304  17.068  23.112  1.00  4.75
ATOM   1385  O   VAL A 185      11.454  16.616  23.866  1.00  2.24
ATOM   1386  CB  VAL A 185      11.986  17.046  20.602  1.00  7.85
ATOM   1387  CG1 VAL A 185      11.220  15.734  20.742  1.00  9.80
ATOM   1388  CG2 VAL A 185      11.454  17.844  19.399  1.00  5.85
ATOM   1389  N   ASN A 186      13.613  16.901  23.312  1.00  2.67
ATOM   1390  CA  ASN A 186      14.155  16.102  24.413  1.00  3.88
ATOM   1391  C   ASN A 186      14.366  16.815  25.754  1.00  5.62
ATOM   1392  O   ASN A 186      14.016  16.281  26.815  1.00  4.90
ATOM   1393  CB  ASN A 186      15.497  15.477  24.008  1.00  5.02
ATOM   1394  CG  ASN A 186      15.410  14.635  22.742  1.00  3.86
ATOM   1395  OD1 ASN A 186      16.314  14.665  21.906  1.00  8.48
ATOM   1396  ND2 ASN A 186      14.352  13.853  22.614  1.00  2.00
ATOM   1397  N   THR A 187      15.022  17.971  25.711  1.00  2.50
ATOM   1398  CA  THR A 187      15.319  18.734  26.918  1.00  3.26
ATOM   1399  C   THR A 187      14.147  19.555  27.480  1.00  3.32
ATOM   1400  O   THR A 187      13.770  19.380  28.640  1.00  3.06
ATOM   1401  CB  THR A 187      16.574  19.603  26.690  1.00  3.97
ATOM   1402  OG1 THR A 187      17.585  18.791  26.079  1.00  3.59
ATOM   1403  CG2 THR A 187      17.128  20.137  27.999  1.00  2.00
ATOM   1404  N   ALA A 188      13.556  20.429  26.666  1.00  2.56
ATOM   1405  CA  ALA A 188      12.431  21.240  27.129  1.00  2.00
ATOM   1406  C   ALA A 188      11.125  20.461  27.194  1.00  3.30
ATOM   1407  O   ALA A 188      10.264  20.733  28.041  1.00  2.60
ATOM   1408  CB  ALA A 188      12.259  22.467  26.248  1.00  2.00
ATOM   1409  N   LYS A 189      10.983  19.493  26.296  1.00  2.63
ATOM   1410  CA  LYS A 189       9.781  18.677  26.207  1.00  2.68
ATOM   1411  C   LYS A 189       8.540  19.520  25.893  1.00  4.51
ATOM   1412  O   LYS A 189       7.527  19.474  26.600  1.00  2.17
ATOM   1413  CB  LYS A 189       9.586  17.837  27.470  1.00  4.93
ATOM   1414  CG  LYS A 189      10.630  16.757  27.644  1.00  5.12
ATOM   1415  CD  LYS A 189      10.187  15.780  28.697  1.00  8.75
ATOM   1416  CE  LYS A 189      11.272  14.792  29.041  1.00 11.74
ATOM   1417  NZ  LYS A 189      12.439  15.449  29.678  1.00 12.05
ATOM   1418  N   VAL A 190       8.653  20.297  24.818  1.00  2.08
ATOM   1419  CA  VAL A 190       7.588  21.158  24.332  1.00  3.15
ATOM   1420  C   VAL A 190       6.326  20.324  24.119  1.00  2.00
ATOM   1421  O   VAL A 190       6.384  19.219  23.582  1.00  2.00
ATOM   1422  CB  VAL A 190       8.004  21.844  23.004  1.00  2.00
ATOM   1423  CG1 VAL A 190       6.839  22.628  22.426  1.00  6.52
ATOM   1424  CG2 VAL A 190       9.199  22.752  23.230  1.00  2.00
ATOM   1425  N   GLU A 191       5.188  20.872  24.513  1.00  2.00
ATOM   1426  CA  GLU A 191       3.922  20.162  24.407  1.00  2.00
ATOM   1427  C   GLU A 191       2.991  20.680  23.314  1.00  2.00
ATOM   1428  O   GLU A 191       3.050  21.852  22.945  1.00  2.71
ATOM   1429  CB  GLU A 191       3.210  20.219  25.753  1.00  2.00
ATOM   1430  CG  GLU A 191       4.037  19.654  26.897  1.00  2.00
ATOM   1431  CD  GLU A 191       3.357  19.778  28.239  1.00  8.61
ATOM   1432  OE1 GLU A 191       2.206  20.253  28.290  1.00 10.92
ATOM   1433  OE2 GLU A 191       3.976  19.401  29.259  1.00 10.50
ATOM   1434  N   PRO A 192       2.137  19.802  22.760  1.00  2.00
ATOM   1435  CA  PRO A 192       1.202  20.222  21.710  1.00  2.78
ATOM   1436  C   PRO A 192       0.246  21.303  22.215  1.00  4.03
ATOM   1437  O   PRO A 192      -0.339  21.168  23.293  1.00  5.82
ATOM   1438  CB  PRO A 192       0.461  18.922  21.355  1.00  2.00
ATOM   1439  CG  PRO A 192       0.713  18.005  22.514  1.00  2.00
ATOM   1440  CD  PRO A 192       2.113  18.340  22.932  1.00  2.00
ATOM   1441  N   GLY A 193       0.118  22.381  21.448  1.00  5.04
ATOM   1442  CA  GLY A 193      -0.764  23.477  21.818  1.00  3.14
ATOM   1443  C   GLY A 193      -0.136  24.539  22.703  1.00  3.17
ATOM   1444  O   GLY A 193      -0.782  25.524  23.045  1.00  6.48
ATOM   1445  N   SER A 194       1.135  24.362  23.042  1.00  4.36
ATOM   1446  CA  SER A 194       1.845  25.295  23.903  1.00  3.79
ATOM   1447  C   SER A 194       2.436  26.504  23.161  1.00  6.08
ATOM   1448  O   SER A 194       2.379  26.579  21.933  1.00  7.15
ATOM   1449  CB  SER A 194       2.963  24.551  24.630  1.00  4.71
ATOM   1450  OG  SER A 194       3.970  24.144  23.715  1.00  7.92
ATOM   1451  N   THR A 195       3.008  27.439  23.920  1.00  3.75
ATOM   1452  CA  THR A 195       3.635  28.638  23.364  1.00  4.64
ATOM   1453  C   THR A 195       5.133  28.600  23.689  1.00  2.37
ATOM   1454  O   THR A 195       5.519  28.313  24.824  1.00  2.01
ATOM   1455  CB  THR A 195       3.007  29.952  23.923  1.00  2.49
ATOM   1456  OG1 THR A 195       3.316  30.099  25.313  1.00  9.21
ATOM   1457  CG2 THR A 195       1.498  29.954  23.750  1.00  2.00
ATOM   1458  N   CYS A 196       5.960  28.894  22.691  1.00  2.00
ATOM   1459  CA  CYS A 196       7.411  28.871  22.832  1.00  3.39
ATOM   1460  C   CYS A 196       8.087  30.136  22.288  1.00  2.90
ATOM   1461  O   CYS A 196       7.492  30.875  21.506  1.00  3.09
ATOM   1462  CB  CYS A 196       7.967  27.676  22.057  1.00  4.15
ATOM   1463  SG  CYS A 196       7.083  26.137  22.314  1.00  5.55
ATOM   1464  N   ALA A 197       9.348  30.336  22.671  1.00  2.00
ATOM   1465  CA  ALA A 197      10.162  31.457  22.210  1.00  3.18
ATOM   1466  C   ALA A 197      11.612  30.989  22.033  1.00  4.17
ATOM   1467  O   ALA A 197      12.197  30.421  22.955  1.00  6.80
ATOM   1468  CB  ALA A 197      10.112  32.604  23.198  1.00  3.99
ATOM   1469  N   VAL A 198      12.179  31.232  20.854  1.00  3.88
ATOM   1470  CA  VAL A 198      13.554  30.849  20.553  1.00  4.76
ATOM   1471  C   VAL A 198      14.427  32.087  20.354  1.00  3.75
ATOM   1472  O   VAL A 198      14.165  32.897  19.453  1.00  4.60
ATOM   1473  CB  VAL A 198      13.633  30.006  19.256  1.00  5.79
ATOM   1474  CG1 VAL A 198      15.090  29.756  18.878  1.00  3.52
ATOM   1475  CG2 VAL A 198      12.884  28.694  19.424  1.00  2.00
ATOM   1476  N   PHE A 199      15.472  32.219  21.170  1.00  2.73
ATOM   1477  CA  PHE A 199      16.391  33.352  21.072  1.00  2.00
ATOM   1478  C   PHE A 199      17.637  32.987  20.272  1.00  3.12
ATOM   1479  O   PHE A 199      18.442  32.152  20.703  1.00  2.75
ATOM   1480  CB  PHE A 199      16.823  33.839  22.455  1.00  2.00
ATOM   1481  CG  PHE A 199      15.726  34.482  23.255  1.00  2.90
ATOM   1482  CD1 PHE A 199      14.695  33.712  23.802  1.00  2.60
ATOM   1483  CD2 PHE A 199      15.746  35.854  23.500  1.00  2.00
ATOM   1484  CE1 PHE A 199      13.705  34.299  24.579  1.00  2.00
ATOM   1485  CE2 PHE A 199      14.764  36.455  24.277  1.00  2.00
ATOM   1486  CZ  PHE A 199      13.739  35.679  24.820  1.00  3.29
ATOM   1487  N   GLY A 200      17.836  33.690  19.161  1.00  2.36
ATOM   1488  CA  GLY A 200      18.981  33.441  18.303  1.00  4.00
ATOM   1489  C   GLY A 200      18.532  32.580  17.150  1.00  4.33
ATOM   1490  O   GLY A 200      18.020  31.471  17.358  1.00  3.38
ATOM   1491  N   LEU A 201      18.718  33.080  15.932  1.00  5.04
ATOM   1492  CA  LEU A 201      18.290  32.355  14.747  1.00  5.15
ATOM   1493  C   LEU A 201      19.381  31.898  13.764  1.00  6.23
ATOM   1494  O   LEU A 201      19.325  32.204  12.579  1.00  6.02
ATOM   1495  CB  LEU A 201      17.195  33.147  14.022  1.00  4.46
ATOM   1496  CG  LEU A 201      15.920  33.458  14.822  1.00  5.34
ATOM   1497  CD1 LEU A 201      15.036  34.375  14.003  1.00  2.78
ATOM   1498  CD2 LEU A 201      15.161  32.179  15.207  1.00  2.64
ATOM   1499  N   GLY A 202      20.394  31.207  14.280  1.00  7.06
ATOM   1500  CA  __3 A 202      21.432  30.648  13.429  1.00  7.03
ATOM   1501  C   GLY A 202      20.920  29.238  13.178  1.00  5.66
ATOM   1502  O   GLY A 202      19.744  28.976  13.416  1.00  6.62
ATOM   1503  N   ALA A 203      21.771  28.302  12.771  1.00  7.34
ATOM   1504  CA  ALA A 203      21.291  26.935  12.532  1.00  4.70
ATOM   1505  C   ALA A 203      20.725  26.251  13.796  1.00  4.72
ATOM   1506  O   ALA A 203      19.701  25.554  13.725  1.00  2.00
ATOM   1507  CB  ALA A 203      22.379  26.074  11.872  1.00  2.00
ATOM   1508  N   VAL A 204      21.351  26.486  14.951  1.00  2.63
ATOM   1509  CA  VAL A 204      20.873  25.886  16.203  1.00  3.19
ATOM   1510  C   VAL A 204      19.497  26.449  16.585  1.00  3.90
ATOM   1511  O   VAL A 204      18.589  25.697  16.945  1.00  5.73
ATOM   1512  CB  VAL A 204      21.875  26.080  17.381  1.00  4.54
ATOM   1513  CG1 VAL A 204      21.327  25.415  18.653  1.00  4.39
ATOM   1514  CG2 VAL A 204      23.241  25.493  17.017  1.00  2.99
ATOM   1515  N   GLY A 205      19.338  27.764  16.488  1.00  3.50
ATOM   1516  CA  GLY A 205      18.057  28.367  16.798  1.00  2.00
ATOM   1517  C   GLY A 205      16.986  27.949  15.805  1.00  2.83
ATOM   1518  O   GLY A 205      15.847  27.662  16.193  1.00  4.72
ATOM   1519  N   LEU A 206      17.332  27.913  14.519  1.00  3.85
ATOM   1520  CA  LEU A 206      16.371  27.518  13.484  1.00  3.89
ATOM   1521  C   LEU A 206      15.922  26.067  13.629  1.00  3.59
ATOM   1522  O   LEU A 206      14.799  25.719  13.240  1.00  2.00
ATOM   1523  CB  LEU A 206      16.933  27.765  12.079  1.00  4.92
ATOM   1524  CG  LEU A 206      17.057  29.241  11.688  1.00  5.26
ATOM   1525  CD1 LEU A 206      17.720  29.350  10.333  1.00  2.09
ATOM   1526  CD2 LEU A 206      15.685  29.901  11.679  1.00  3.73
ATOM   1527  N   ALA A 207      16.816  25.216  14.134  1.00  2.00
ATOM   1528  CA  ALA A 207      16.497  23.806  14.372  1.00  2.00
ATOM   1529  C   ALA A 207      15.585  23.729  15.604  1.00  2.00
ATOM   1530  O   ALA A 207      14.707  22.869  15.693  1.00  2.96
ATOM   1531  CB  ALA A 207      17.768  23.000  14.609  1.00  2.00
ATOM   1532  N   ALA A 208      15.798  24.631  16.557  1.00  2.00
ATOM   1533  CA  ALA A 208      14.966  24.660  17.760  1.00  2.00
ATOM   1534  C   ALA A 208      13.545  25.030  17.345  1.00  2.41
ATOM   1535  O   ALA A 208      12.574  24.441  17.824  1.00  4.74
ATOM   1536  CB  ALA A 208      15.508  25.657  18.758  1.00  2.00
ATOM   1537  N   VAL A 209      13.426  25.971  16.410  1.00  2.22
ATOM   1538  CA  VAL A 209      12.115  26.382  15.910  1.00  2.84
ATOM   1539  C   VAL A 209      11.410  25.173  15.294  1.00  2.12
ATOM   1540  O   VAL A 209      10.245  24.907  15.589  1.00  3.26
ATOM   1541  CB  VAL A 209      12.230  27.510  14.851  1.00  2.00
ATOM   1542  CG1 VAL A 209      10.904  27.709  14.141  1.00  2.00
ATOM   1543  CG2 VAL A 209      12.665  28.812  15.512  1.00  2.00
ATOM   1544  N   MET A 210      12.143  24.420  14.479  1.00  2.99
ATOM   1545  CA  MET A 210      11.615  23.231  13.812  1.00  3.46
ATOM   1546  C   MET A 210      11.111  22.215  14.843  1.00  2.00
ATOM   1547  O   MET A 210      10.028  21.658  14.682  1.00  4.31
ATOM   1548  CB  MET A 210      12.696  22.615  12.905  1.00  3.59
ATOM   1549  CG  MET A 210      12.225  21.472  12.005  1.00  2.00
ATOM   1550  SD  MET A 210      13.441  20.995  10.730  1.00  3.77
ATOM   1551  CE  MET A 210      14.843  20.543  11.723  1.00  2.00
ATOM   1552  N   GLY A 211      11.888  21.997  15.902  1.00  2.22
ATOM   1553  CA  GLY A 211      11.495  21.076  16.960  1.00  3.30
ATOM   1554  C   GLY A 211      10.190  21.492  17.627  1.00  5.20
ATOM   1555  O   GLY A 211       9.315  20.662  17.897  1.00  4.40
ATOM   1556  N   CYS A 212      10.056  22.783  17.911  1.00  5.57
ATOM   1557  CA  CYS A 212       8.834  23.296  18.521  1.00  5.62
ATOM   1558  C   CYS A 212       7.663  23.013  17.596  1.00  4.65
ATOM   1559  O   CYS A 212       6.578  22.630  18.039  1.00  8.29
ATOM   1560  CB  CYS A 212       8.952  24.799  18.768  1.00  2.00
ATOM   1561  SG  CYS A 212      10.059  25.252  20.111  1.00  4.73
ATOM   1562  N   HIS A 213       7.893  23.177  16.298  1.00  6.85
ATOM   1563  CA  HIS A 213       6.848  22.929  15.315  1.00  7.84
ATOM   1564  C   HIS A 213       6.466  21.444  15.295  1.00  8.72
ATOM   1565  O   HIS A 213       5.290  21.118  15.307  1.00  6.53
ATOM   1566  CB  HIS A 213       7.294  23.400  13.924  1.00  7.94
ATOM   1567  CG  HIS A 213       6.279  23.158  12.853  1.00  8.38
ATOM   1568  ND1 HIS A 213       5.243  24.029  12.598  1.00 10.17
ATOM   1569  CD2 HIS A 213       6.119  22.124  11.991  1.00  9.74
ATOM   1570  CE1 HIS A 213       4.486  23.545  11.630  1.00 11.58
ATOM   1571  NE2 HIS A 213       4.997  22.388  11.244  1.00 10.90
ATOM   1572  N   SER A 214       7.463  20.557  15.287  1.00  7.89
ATOM   1573  CA  SER A 214       7.220  19.115  15.270  1.00  9.67
ATOM   1574  C   SER A 214       6.431  18.648  16.490  1.00 10.05
ATOM   1575  O   SER A 214       5.558  17.775  16.369  1.00  5.80
ATOM   1576  CB  SER A 214       8.537  18.334  15.191  1.00  9.81
ATOM   1577  OG  SER A 214       9.244  18.635  14.005  1.00 16.12
ATOM   1578  N   ALA A 215       6.765  19.207  17.657  1.00  7.42
ATOM   1579  CA  ALA A 215       6.088  18.885  18.918  1.00  4.18
ATOM   1580  C   ALA A 215       4.631  19.388  18.952  1.00  5.76
ATOM   1581  O   ALA A 215       3.871  19.046  19.855  1.00  5.81
ATOM   1582  CB  ALA A 215       6.868  19.454  20.084  1.00  2.00
ATOM   1583  N   GLY A 216       4.254  20.213  17.976  1.00  8.32
ATOM   1584  CA  GLY A 216       2.890  20.719  17.892  1.00  5.23
ATOM   1585  C   GLY A 216       2.524  21.987  18.643  1.00  4.03
ATOM   1586  O   GLY A 216       1.342  22.186  18.972  1.00  2.25
ATOM   1587  N   ALA A 217       3.510  22.846  18.891  1.00  4.59
ATOM   1588  CA  ALA A 217       3.313  24.109  19.595  1.00  4.74
ATOM   1589  C   ALA A 217       2.353  24.999  18.800  1.00  6.87
ATOM   1590  O   ALA A 217       2.368  24.998  17.578  1.00  6.52
ATOM   1591  CB  ALA A 217       4.660  24.824  19.800  1.00  2.00
ATOM   1592  N   LYS A 218       1.506  25.725  19.513  1.00  7.79
ATOM   1593  CA  LYS A 218       0.547  26.599  18.865  1.00  7.20
ATOM   1594  C   LYS A 218       1.143  27.934  18.461  1.00  9.74
ATOM   1595  O   LYS A 218       0.731  28.507  17.448  1.00 10.23
ATOM   1596  CB  LYS A 218      -0.668  26.789  19.764  1.00  9.03
ATOM   1597  CG  LYS A 218      -1.785  27.587  19.127  1.00 14.08
ATOM   1598  CD  LYS A 218      -3.119  27.169  19.697  1.00 20.18
ATOM   1599  CE  LYS A 218      -4.214  28.181  19.405  1.00 25.01
ATOM   1600  NZ  LYS A 218      -4.221  28.626  17.985  1.00 26.67
ATOM   1601  N   ARG A 219       2.149  28.418  19.193  1.00  8.49
ATOM   1602  CA  ARG A 219       2.769  29.697  18.861  1.00  5.69
ATOM   1603  C   ARG A 219       4.271  29.623  19.096  1.00  3.44
ATOM   1604  O   ARG A 219       4.696  29.174  20.144  1.00  3.48
ATOM   1605  CB  ARG A 219       2.154  30.808  19.709  1.00  9.03
ATOM   1606  CG  ARG A 219       2.547  32.208  19.300  1.00 10.07
ATOM   1607  CD  ARG A 219       1.905  33.226  20.210  1.00 12.05
ATOM   1608  NE  ARG A 219       1.967  34.570  19.646  1.00 14.51
ATOM   1609  CZ  ARG A 219       1.584  35.671  20.282  1.00 16.86
ATOM   1610  NH1 ARG A 219       1.111  35.602  21.525  1.00 17.72
ATOM   1611  NH2 ARG A 219       1.647  36.842  19.663  1.00 11.13
ATOM   1612  N   ILE A 220       5.065  30.028  18.105  1.00  3.87
ATOM   1613  CA  ILE A 220       6.523  29.992  18.208  1.00  2.77
ATOM   1614  C   ILE A 220       7.047  31.371  17.813  1.00  2.01
ATOM   1615  O   ILE A 220       6.922  31.789  16.661  1.00  4.16
ATOM   1616  CB  ILE A 220       7.115  28.922  17.266  1.00  3.17
ATOM   1617  CG1 ILE A 220       6.440  27.574  17.523  1.00  2.72
ATOM   1618  CG2 ILE A 220       8.621  28.796  17.474  1.00  5.14
ATOM   1619  CD1 ILE A 220       6.640  26.569  16.414  1.00  3.51
ATOM   1620  N   ILE A 221       7.608  32.078  18.783  1.00  2.00
ATOM   1621  CA  ILE A 221       8.121  33.422  18.574  1.00  4.37
ATOM   1622  C   ILE A 221       9.624  33.390  18.340  1.00  3.25
ATOM   1623  O   ILE A 221      10.374  32.846  19.156  1.00  4.27
ATOM   1624  CB  ILE A 221       7.753  34.315  19.793  1.00  4.65
ATOM   1625  CG1 ILE A 221       6.245  34.210  20.049  1.00  4.04
ATOM   1626  CG2 ILE A 221       8.121  35.786  19.532  1.00  2.00
ATOM   1627  CD1 ILE A 221       5.799  34.641  21.444  1.00  7.20
ATOM   1628  N   ALA A 222      10.045  33.905  17.185  1.00  5.05
ATOM   1629  CA  ALA A 222      11.462  33.963  16.809  1.00  5.77
ATOM   1630  C   ALA A 222      12.057  35.311  17.227  1.00  6.30
ATOM   1631  O   ALA A 222      11.506  36.362  16.896  1.00  8.30
ATOM   1632  CB  ALA A 222      11.617  33.752  15.302  1.00  3.24
ATOM   1633  N   VAL A 223      13.176  35.285  17.949  1.00  5.62
ATOM   1634  CA  VAL A 223      13.801  36.518  18.421  1.00  6.08
ATOM   1635  C   VAL A 223      15.255  36.661  17.961  1.00  4.97
ATOM   1636  O   VAL A 223      16.094  35.807  18.263  1.00  3.55
ATOM   1637  CB  VAL A 223      13.770  36.595  19.974  1.00  6.71
ATOM   1638  CG1 VAL A 223      14.153  37.989  20.438  1.00  7.84
ATOM   1639  CG2 VAL A 223      12.392  36.192  20.516  1.00  3.56
ATOM   1640  N   ASP A 224      15.561  37.751  17.260  1.00  4.79
ATOM   1641  CA  ASP A 224      16.927  37.995  16.774  1.00  3.99
ATOM   1642  C   ASP A 224      17.121  39.489  16.491  1.00  3.22
ATOM   1643  O   ASP A 224      16.175  40.180  16.117  1.00  2.00
ATOM   1644  CB  ASP A 224      17.194  37.175  15.497  1.00  2.00
ATOM   1645  CG  ASP A 224      18.686  36.942  15.229  1.00  4.38
ATOM   1646  OD1 ASP A 224      19.493  37.890  15.270  1.00  2.22
ATOM   1647  OD2 ASP A 224      19.063  35.793  14.957  1.00  4.08
ATOM   1648  N   LEU A 225      18.336  39.985  16.727  1.00  5.67
ATOM   1649  CA  LEU A 225      18.678  41.394  16.476  1.00  7.62
ATOM   1650  C   LEU A 225      18.801  41.642  14.963  1.00  9.38
ATOM   1651  O   LEU A 225      18.676  42.778  14.494  1.00 12.33
ATOM   1652  CB  LEU A 225      20.012  41.750  17.148  1.00  8.34
ATOM   1653  CG  LEU A 225      20.101  41.660  18.673  1.00  6.59
ATOM   1654  CD1 LEU A 225      21.536  41.730  19.111  1.00  6.01
ATOM   1655  CD2 LEU A 225      19.290  42.751  19.329  1.00  4.78
ATOM   1656  N   ASN A 226      19.127  40.579  14.228  1.00  9.82
ATOM   1657  CA  ASN A 226      19.279  40.608  12.773  1.00  9.98
ATOM   1658  C   ASN A 226      18.007  40.066  12.122  1.00  9.51
ATOM   1659  O   ASN A 226      17.814  38.849  12.004  1.00  9.60
ATOM   1660  CB  ASN A 226      20.493  39.767  12.348  1.00  7.91
ATOM   1661  CG  ASN A 226      20.641  39.657  10.833  1.00  7.15
ATOM   1662  OD1 ASN A 226      19.798  40.137  10.071  1.00  4.00
ATOM   1663  ND2 ASN A 226      21.713  39.009  10.394  1.00  3.67
ATOM   1664  N   PRO A 227      17.136  40.973  11.662  1.00  9.41
ATOM   1665  CA  PRO A 227      15.864  40.656  11.012  1.00 11.05
ATOM   1666  C   PRO A 227      15.938  39.868   9.700  1.00 13.21
ATOM   1667  O   PRO A 227      14.906  39.400   9.204  1.00 11.43
ATOM   1668  CB  PRO A 227      15.229  42.036  10.823  1.00  9.70
ATOM   1669  CG  PRO A 227      16.410  42.927  10.676  1.00 11.15
ATOM   1670  CD  PRO A 227      17.323  42.432  11.753  1.00  8.60
ATOM   1671  N   ASP A 228      17.138  39.720   9.138  1.00 13.08
ATOM   1672  CA  ASP A 228      17.305  38.969   7.898  1.00 12.83
ATOM   1673  C   ASP A 228      17.025  37.487   8.101  1.00 13.17
ATOM   1674  O   ASP A 228      16.797  36.764   7.131  1.00 12.66
ATOM   1675  CB  ASP A 228      18.723  39.113   7.346  1.00 11.64
ATOM   1676  CG  ASP A 228      19.023  40.501   6.839  1.00 15.48
ATOM   1677  OD1 ASP A 228      18.075  41.266   6.554  1.00 17.71
ATOM   1678  OD2 ASP A 228      20.226  40.820   6.720  1.00 14.31
ATOM   1679  N   LYS A 229      17.072  37.030   9.352  1.00 11.79
ATOM   1680  CA  LYS A 229      16.829  35.620   9.669  1.00 10.40
ATOM   1681  C   LYS A 229      15.347  35.238   9.769  1.00 11.24
ATOM   1682  O   LYS A 229      15.003  34.050   9.731  1.00 10.67
ATOM   1683  CB  LYS A 229      17.517  35.236  10.983  1.00 10.91
ATOM   1684  CG  LYS A 229      19.002  35.537  11.054  1.00 11.83
ATOM   1685  CD  LYS A 229      19.772  34.738  10.030  1.00 10.42
ATOM   1686  CE  LYS A 229      21.276  34.821  10.257  1.00 11.64
ATOM   1687  NZ  LYS A 229      21.719  34.093  11.482  1.00 12.23
ATOM   1688  N   PHE A 230      14.470  36.232   9.847  1.00 10.28
ATOM   1689  CA  PHE A 230      13.036  35.983   9.990  1.00 10.53
ATOM   1690  C   PHE A 230      12.390  35.152   8.885  1.00 12.05
ATOM   1691  O   PHE A 230      11.496  34.341   9.152  1.00 11.06
ATOM   1692  CB  PHE A 230      12.298  37.300  10.199  1.00  9.26
ATOM   1693  CG  PHE A 230      12.663  37.998  11.487  1.00 11.18
ATOM   1694  CD1 PHE A 230      13.243  37.290  12.539  1.00  8.54
ATOM   1695  CD2 PHE A 230      12.414  39.359  11.656  1.00  9.68
ATOM   1696  CE1 PHE A 230      13.564  37.928  13.737  1.00  9.01
ATOM   1697  CE2 PHE A 230      12.734  40.005  12.854  1.00  7.68
ATOM   1698  CZ  PHE A 230      13.309  39.288  13.893  1.00  6.13
ATOM   1699  N   GLU A 231      12.871  35.333   7.659  1.00 13.47
ATOM   1700  CA  GLU A 231      12.384  34.606   6.486  1.00 13.24
ATOM   1701  C   GLU A 231      12.540  33.085   6.674  1.00 10.44
ATOM   1702  O   GLU A 231      11.603  32.310   6.450  1.00  7.59
ATOM   1703  CB  GLU A 231      13.194  35.057   5.268  1.00 18.37
ATOM   1704  CG  GLU A 231      12.615  34.662   3.922  1.00 26.24
ATOM   1705  CD  GLU A 231      11.397  35.485   3.543  1.00 32.58
ATOM   1706  OE1 GLU A 231      11.299  36.658   3.972  1.00 35.00
ATOM   1707  OE2 GLU A 231      10.535  34.958   2.810  1.00 36.84
ATOM   1708  N   LYS A 232      13.735  32.671   7.088  1.00  9.06
ATOM   1709  CA  LYS A 232      14.040  31.250   7.321  1.00  9.35
ATOM   1710  C   LYS A 232      13.302  30.749   8.574  1.00  6.31
ATOM   1711  O   LYS A 232      12.948  29.573   8.671  1.00  2.19
ATOM   1712  CB  LYS A 232      15.551  31.032   7.502  1.00 10.75
ATOM   1713  CG  LYS A 232      16.388  31.115   6.234  1.00  9.51
ATOM   1714  CD  LYS A 232      16.283  29.852   5.387  1.00  8.69
ATOM   1715  CE  LYS A 232      17.190  29.960   4.173  1.00  5.61
ATOM   1716  NZ  LYS A 232      17.150  28.753   3.323  1.00  4.51
ATOM   1717  N   ALA A 233      13.112  31.630   9.551  1.00  4.80
ATOM   1718  CA  ALA A 233      12.391  31.244  10.765  1.00  7.09
ATOM   1719  C   ALA A 233      10.970  30.851  10.363  1.00  6.27
ATOM   1720  O   ALA A 233      10.428  29.859  10.856  1.00  6.74
ATOM   1721  CB  ALA A 233      12.372  32.387  11.776  1.00  5.13
ATOM   1722  N   LYS A 234      10.396  31.604   9.427  1.00  7.93
ATOM   1723  CA  LYS A 234       9.048  31.332   8.931  1.00  9.71
ATOM   1724  C   LYS A 234       9.039  30.009   8.177  1.00  8.58
ATOM   1725  O   LYS A 234       8.126  29.200   8.333  1.00  6.79
ATOM   1726  CB  LYS A 234       8.568  32.466   8.028  1.00 12.24
ATOM   1727  CG  LYS A 234       7.173  32.251   7.479  1.00 19.20
ATOM   1728  CD  LYS A 234       6.523  33.559   7.082  1.00 23.69
ATOM   1729  CE  LYS A 234       5.146  33.310   6.492  1.00 28.61
ATOM   1730  NZ  LYS A 234       5.247  32.817   5.089  1.00 27.69
ATOM   1731  N   VAL A 235      10.084  29.776   7.389  1.00  8.50
ATOM   1732  CA  VAL A 235      10.224  28.536   6.633  1.00  6.19
ATOM   1733  C   VAL A 235      10.170  27.339   7.588  1.00  7.71
ATOM   1734  O   VAL A 235       9.462  26.363   7.334  1.00  6.29
ATOM   1735  CB  VAL A 235      11.553  28.535   5.831  1.00  6.01
ATOM   1736  CG1 VAL A 235      11.897  27.141   5.328  1.00  5.75
ATOM   1737  CG2 VAL A 235      11.434  29.493   4.647  1.00  5.03
ATOM   1738  N   PHE A 236      10.826  27.474   8.737  1.00  7.15
ATOM   1739  CA  PHE A 236      10.870  26.407   9.735  1.00  5.98
ATOM   1740  C   PHE A 236       9.678  26.295  10.699  1.00  6.71
ATOM   1741  O   PHE A 236       9.696  25.457  11.607  1.00  7.67
ATOM   1742  CB  PHE A 236      12.208  26.444  10.493  1.00  2.67
ATOM   1743  CG  PHE A 236      13.390  26.054   9.640  1.00  2.24
ATOM   1744  CD1 PHE A 236      13.584  24.727   9.262  1.00  2.00
ATOM   1745  CD2 PHE A 236      14.289  27.018   9.187  1.00  2.00
ATOM   1746  CE1 PHE A 236      14.661  24.361   8.439  1.00  4.55
ATOM   1747  CE2 PHE A 236      15.362  26.671   8.368  1.00  3.79
ATOM   1748  CZ  PHE A 236      15.552  25.333   7.991  1.00  2.00
ATOM   1749  N   GLY A 237       8.644  27.113  10.503  1.00  5.95
ATOM   1750  CA  GLY A 237       7.464  27.022  11.354  1.00  4.75
ATOM   1751  C   GLY A 237       7.149  28.106  12.374  1.00  5.44
ATOM   1752  O   GLY A 237       6.223  27.936  13.168  1.00  6.03
ATOM   1753  N   ALA A 238       7.902  29.203  12.390  1.00  5.42
ATOM   1754  CA  ALA A 238       7.631  30.276  13.353  1.00  4.88
ATOM   1755  C   ALA A 238       6.338  31.026  13.059  1.00  6.55
ATOM   1756  O   ALA A 238       5.987  31.256  11.907  1.00  7.24
ATOM   1757  CB  ALA A 238       8.786  31.249  13.409  1.00  4.42
ATOM   1758  N   THR A 239       5.670  31.485  14.110  1.00  7.01
ATOM   1759  CA  THR A 239       4.427  32.204  13.923  1.00  7.45
ATOM   1760  C   THR A 239       4.560  33.698  14.182  1.00  5.54
ATOM   1761  O   THR A 239       3.767  34.482  13.668  1.00  7.29
ATOM   1762  CB  THR A 239       3.294  31.623  14.804  1.00  5.90
ATOM   1763  OG1 THR A 239       3.609  31.808  16.191  1.00  5.71
ATOM   1764  CG2 THR A 239       3.122  30.140  14.532  1.00  8.11
ATOM   1765  N   ASP A 240       5.552  34.089  14.979  1.00  4.58
ATOM   1766  CA  ASP A 240       5.769  35.492  15.314  1.00  3.47
ATOM   1767  C   ASP A 240       7.237  35.829  15.141  1.00  4.55
ATOM   1768  O   ASP A 240       8.103  34.957  15.257  1.00  4.69
ATOM   1769  CB  ASP A 240       5.343  35.787  16.758  1.00  6.19
ATOM   1770  CG  ASP A 240       3.854  35.643  16.973  1.00  7.88
ATOM   1771  OD1 ASP A 240       3.361  34.497  17.027  1.00  6.58
ATOM   1772  OD2 ASP A 240       3.174  36.680  17.094  1.00 10.57
ATOM   1773  N   PHE A 241       7.526  37.110  14.955  1.00  4.38
ATOM   1774  CA  PHE A 241       8.896  37.545  14.725  1.00  5.81
ATOM   1775  C   PHE A 241       9.151  38.829  15.485  1.00  7.52
ATOM   1776  O   PHE A 241       8.430  39.809  15.305  1.00  9.85
ATOM   1777  CB  PHE A 241       9.094  37.757  13.218  1.00  2.56
ATOM   1778  CG  PHE A 241       8.588  36.608  12.384  1.00  3.03
ATOM   1779  CD1 PHE A 241       9.398  35.506  12.132  1.00  3.35
ATOM   1780  CD2 PHE A 241       7.275  36.598  11.913  1.00  6.49
ATOM   1781  CE1 PHE A 241       8.911  34.405  11.435  1.00  5.03
ATOM   1782  CE2 PHE A 241       6.771  35.495  11.209  1.00  5.81
ATOM   1783  CZ  PHE A 241       7.591  34.399  10.972  1.00  5.81
ATOM   1784  N   VAL A 242      10.177  38.825  16.331  1.00  7.60
ATOM   1785  CA  VAL A 242      10.509  39.993  17.139  1.00  7.87
ATOM   1786  C   VAL A 242      11.990  40.359  17.091  1.00  8.82
ATOM   1787  O   VAL A 242      12.862  39.509  17.289  1.00 10.44
ATOM   1788  CB  VAL A 242      10.111  39.791  18.643  1.00  9.06
ATOM   1789  CG1 VAL A 242      10.533  41.001  19.478  1.00  4.99
ATOM   1790  CG2 VAL A 242       8.611  39.554  18.791  1.00  3.37
ATOM   1791  N   ASN A 243      12.262  41.622  16.779  1.00  9.09
ATOM   1792  CA  ASN A 243      13.621  42.138  16.766  1.00 10.87
ATOM   1793  C   ASN A 243      13.681  43.018  18.011  1.00 11.01
ATOM   1794  O   ASN A 243      12.931  43.992  18.120  1.00 13.40
ATOM   1795  CB  ASN A 243      13.886  42.991  15.520  1.00  8.76
ATOM   1796  CG  ASN A 243      15.274  43.631  15.533  1.00 11.72
ATOM   1797  OD1 ASN A 243      15.934  43.703  16.573  1.00  9.29
ATOM   1798  ND2 ASN A 243      15.718  44.102  14.375  1.00 13.20
ATOM   1799  N   PRO A 244      14.536  42.665  18.987  1.00 13.19
ATOM   1800  CA  PRO A 244      14.677  43.436  20.230  1.00 13.77
ATOM   1801  C   PRO A 244      14.879  44.946  20.021  1.00 14.91
ATOM   1802  O   PRO A 244      14.304  45.759  20.743  1.00 15.37
ATOM   1803  CB  PRO A 244      15.906  42.798  20.882  1.00 10.47
ATOM   1804  CG  PRO A 244      15.791  41.367  20.450  1.00 14.03
ATOM   1805  CD  PRO A 244      15.437  41.496  18.992  1.00 11.81
ATOM   1806  N   ASN A 245      15.651  45.314  19.002  1.00 16.76
ATOM   1807  CA  ASN A 245      15.943  46.723  18.709  1.00 14.94
ATOM   1808  C   ASN A 245      14.728  47.604  18.392  1.00 14.44
ATOM   1809  O   ASN A 245      14.818  48.836  18.444  1.00 13.41
ATOM   1810  CB  ASN A 245      16.969  46.830  17.575  1.00 14.10
ATOM   1811  CG  ASN A 245      18.363  46.387  17.998  1.00 15.86
ATOM   1812  OD1 ASN A 245      18.686  46.340  19.184  1.00 16.07
ATOM   1813  ND2 ASN A 245      19.197  46.071  17.027  1.00 17.52
ATOM   1814  N   ASP A 246      13.607  46.986  18.030  1.00 13.25
ATOM   1815  CA  ASP A 246      12.391  47.732  17.710  1.00 11.92
ATOM   1816  C   ASP A 246      11.526  48.035  18.926  1.00 13.43
ATOM   1817  O   ASP A 246      10.373  48.449  18.778  1.00 12.94
ATOM   1818  CB  ASP A 246      11.543  46.962  16.707  1.00 12.89
ATOM   1819  CG  ASP A 246      12.226  46.794  15.358  1.00 13.94
ATOM   1820  OD1 ASP A 246      13.119  47.606  15.012  1.00 13.67
ATOM   1821  OD2 ASP A 246      11.851  45.840  14.643  1.00 10.92
ATOM   1822  N   HIS A 247      12.043  47.763  20.118  1.00 12.68
ATOM   1823  CA  HIS A 247      11.290  48.013  21.326  1.00 13.24
ATOM   1824  C   HIS A 247      12.153  48.673  22.375  1.00 14.44
ATOM   1825  O   HIS A 247      13.335  48.343  22.523  1.00 15.91
ATOM   1826  CB  HIS A 247      10.723  46.684  21.888  1.00 13.06
ATOM   1827  CG  HIS A 247       9.887  45.921  20.904  1.00  9.04
ATOM   1828  ND1 HIS A 247       8.575  46.241  20.631  1.00  9.83
ATOM   1829  CD2 HIS A 247      10.199  44.889  20.083  1.00 12.19
ATOM   1830  CE1 HIS A 247       8.113  45.448  19.683  1.00  7.16
ATOM   1831  NE2 HIS A 247       9.078  44.617  19.333  1.00 11.73
ATOM   1832  N   SER A 248      11.564  49.659  23.040  1.00 16.86
ATOM   1833  CA  SER A 248      12.208  50.330  24.142  1.00 19.02
ATOM   1834  C   SER A 248      12.301  49.477  25.390  1.00 19.76
ATOM   1835  O   SER A 248      13.298  49.562  26.096  1.00 21.12
ATOM   1836  CB  SER A 248      11.525  51.692  24.442  1.00 20.24
ATOM   1837  OG  SER A 248      11.194  52.409  23.249  1.00 24.58
ATOM   1838  N   GLU A 249      11.258  48.702  25.691  1.00 16.28
ATOM   1839  CA  GLU A 249      11.193  47.819  26.896  1.00 16.45
ATOM   1840  C   GLU A 249      12.110  46.655  26.747  1.00 14.49
ATOM   1841  O   GLU A 249      12.463  46.242  25.639  1.00 15.10
ATOM   1842  CB  GLU A 249       9.874  47.116  26.928  1.00 16.31
ATOM   1843  CG  GLU A 249       8.824  48.010  26.940  1.00 21.30
ATOM   1844  CD  GLU A 249       7.729  47.639  28.065  0.50 20.99
ATOM   1845  OE1 GLU A 249       6.965  46.792  27.765  0.50 22.42
ATOM   1846  OE2 GLU A 249       7.621  48.310  29.182  0.50 24.24
ATOM   1847  N   PRO A 250      12.568  46.110  27.849  1.00 14.51
ATOM   1848  CA  PRO A 250      13.448  44.953  27.851  1.00 12.52
ATOM   1849  C   PRO A 250      12.705  43.856  27.146  1.00 10.76
ATOM   1850  O   PRO A 250      11.507  43.769  27.305  1.00 11.50
ATOM   1851  CB  PRO A 250      13.601  44.657  29.360  1.00 14.62
ATOM   1852  CG  PRO A 250      13.567  46.021  29.937  1.00 15.47
ATOM   1853  CD  PRO A 250      12.465  46.693  29.197  1.00 13.75
ATOM   1854  N   ILE A 251      13.416  43.001  26.427  1.00 10.37
ATOM   1855  CA  ILE A 251      12.788  41.927  25.659  1.00  9.60
ATOM   1856  C   ILE A 251      11.802  41.031  26.446  1.00  7.55
ATOM   1857  O   ILE A 251      10.734  40.667  25.932  1.00  8.33
ATOM   1858  CB  ILE A 251      13.845  41.040  24.917  1.00  5.58
ATOM   1859  CG1 ILE A 251      13.158  40.022  23.997  1.00  2.36
ATOM   1860  CG2 ILE A 251      14.763  40.329  25.911  1.00  2.83
ATOM   1861  CD1 ILE A 251      12.275  40.654  22.908  1.00  3.88
ATOM   1862  N   SER A 252      12.136  40.723  27.698  1.00  7.13
ATOM   1863  CA  SER A 252      11.300  39.878  28.540  1.00  7.15
ATOM   1864  C   SER A 252       9.914  40.482  28.742  1.00  7.92
ATOM   1865  O   SER A 252       8.915  39.763  28.814  1.00  5.28
ATOM   1866  CB  SER A 252      11.985  39.653  29.883  1.00  7.66
ATOM   1867  OG  SER A 252      12.268  40.883  30.519  1.00 14.96
ATOM   1868  N   GLN A 253       9.852  41.809  28.805  1.00  7.12
ATOM   1869  CA  GLN A 253       8.586  42.499  28.990  1.00  9.68
ATOM   1870  C   GLN A 253       7.752  42.488  27.723  1.00  7.96
ATOM   1871  O   GLN A 253       6.525  42.419  27.792  1.00  7.46
ATOM   1872  CB  GLN A 253       8.819  43.929  29.459  1.00 11.00
ATOM   1873  CG  GLN A 253       9.569  43.985  30.770  1.00 16.65
ATOM   1874  CD  GLN A 253       9.578  45.358  31.406  1.00 21.33
ATOM   1875  OE1 GLN A 253      10.253  45.572  32.417  1.00 20.96
ATOM   1876  NE2 GLN A 253       8.829  46.296  30.829  1.00 18.88
ATOM   1877  N   VAL A 254       8.419  42.548  26.574  1.00  6.71
ATOM   1878  CA  VAL A 254       7.728  42.533  25.288  1.00  6.49
ATOM   1879  C   VAL A 254       7.010  41.197  25.167  1.00  7.82
ATOM   1880  O   VAL A 254       5.802  41.143  24.919  1.00 11.77
ATOM   1881  CB  VAL A 254       8.714  42.664  24.089  1.00  6.32
ATOM   1882  CG1 VAL A 254       7.948  42.604  22.767  1.00  2.00
ATOM   1883  CG2 VAL A 254       9.506  43.960  24.187  1.00  3.78
ATOM   1884  N   LEU A 255       7.759  40.124  25.390  1.00  8.74
ATOM   1885  CA  LEU A 255       7.215  38.778  25.308  1.00  8.00
ATOM   1886  C   LEU A 255       6.079  38.544  26.310  1.00  9.54
ATOM   1887  O   LEU A 255       5.019  38.041  25.938  1.00  9.35
ATOM   1888  CB  LEU A 255       8.328  37.751  25.489  1.00  5.52
ATOM   1889  CG  LEU A 255       9.480  37.813  24.471  1.00  6.90
ATOM   1890  CD1 LEU A 255      10.263  36.531  24.549  1.00  4.12
ATOM   1891  CD2 LEU A 255       8.972  37.999  23.052  1.00  5.17
ATOM   1892  N   SER A 256       6.277  38.944  27.563  1.00  8.97
ATOM   1893  CA  SER A 256       5.238  38.762  28.565  1.00  9.11
ATOM   1894  C   SER A 256       3.952  39.450  28.112  1.00  9.46
ATOM   1895  O   SER A 256       2.884  38.840  28.118  1.00  7.73
ATOM   1896  CB  SER A 256       5.693  39.295  29.927  1.00 10.89
ATOM   1897  OG  SER A 256       4.672  39.147  30.909  1.00  7.79
ATOM   1898  N   LYS A 257       4.062  40.699  27.667  1.00 11.70
ATOM   1899  CA  LYS A 257       2.894  41.438  27.202  1.00 14.73
ATOM   1900  C   LYS A 257       2.202  40.744  26.035  1.00 15.59
ATOM   1901  O   LYS A 257       0.970  40.759  25.941  1.00 16.66
ATOM   1902  CB  LYS A 257       3.279  42.846  26.769  1.00 20.10
ATOM   1903  CG  LYS A 257       3.475  43.849  27.879  1.00 25.39
ATOM   1904  CD  LYS A 257       3.506  45.232  27.250  1.00 31.74
ATOM   1905  CE  LYS A 257       3.853  46.338  28.231  1.00 35.79
ATOM   1906  NZ  LYS A 257       4.243  47.544  27.435  1.00 35.63
ATOM   1907  N   MET A 258       2.996  40.138  25.154  1.00 12.85
ATOM   1908  CA  MET A 258       2.476  39.433  23.984  1.00 10.63
ATOM   1909  C   MET A 258       1.713  38.178  24.348  1.00  8.33
ATOM   1910  O   MET A 258       0.855  37.733  23.590  1.00  6.94
ATOM   1911  CB  MET A 258       3.620  39.015  23.048  1.00 11.97
ATOM   1912  CG  MET A 258       4.287  40.154  22.298  1.00 14.98
ATOM   1913  SD  MET A 258       5.658  39.595  21.256  1.00 18.32
ATOM   1914  CE  MET A 258       4.819  38.395  20.239  1.00 14.83
ATOM   1915  N   THR A 259       2.044  37.600  25.498  1.00  7.51
ATOM   1916  CA  THR A 259       1.431  36.351  25.938  1.00  8.58
ATOM   1917  C   THR A 259       0.561  36.396  27.196  1.00 11.14
ATOM   1918  O   THR A 259       0.001  35.367  27.589  1.00 13.17
ATOM   1919  CB  THR A 259       2.521  35.295  26.181  1.00  6.63
ATOM   1920  OG1 THR A 259       3.556  35.876  26.991  1.00  2.00
ATOM   1921  CG2 THR A 259       3.117  34.789  24.845  1.00  3.36
ATOM   1922  N   ASN A 260       0.479  37.553  27.845  1.00  9.88
ATOM   1923  CA  ASN A 260      -0.315  37.701  29.068  1.00  7.85
ATOM   1924  C   ASN A 260       0.395  37.008  30.235  1.00  7.13
ATOM   1925  O   ASN A 260      -0.213  36.241  30.984  1.00  5.74
ATOM   1926  CB  ASN A 260      -1.736  37.135  28.855  1.00 12.31
ATOM   1927  CG  ASN A 260      -2.676  37.423  30.013  1.00 15.88
ATOM   1928  OD1 ASN A 260      -2.711  38.532  30.546  1.00 19.17
ATOM   1929  ND2 ASN A 260      -3.483  36.432  30.374  1.00 19.93
ATOM   1930  N   GLY A 261       1.706  37.223  30.342  1.00  5.24
ATOM   1931  CA  GLY A 261       2.449  36.621  31.438  1.00  4.59
ATOM   1932  C   GLY A 261       3.795  35.989  31.135  1.00  6.24
ATOM   1933  O   GLY A 261       4.699  36.013  31.978  1.00  4.44
ATOM   1934  N   GLY A 262       3.913  35.360  29.970  1.00  6.61
ATOM   1935  CA  GLY A 262       5.160  34.726  29.591  1.00  3.36
ATOM   1936  C   GLY A 262       4.857  33.472  28.804  1.00  4.76
ATOM   1937  O   GLY A 262       3.726  32.977  28.823  1.00  2.12
ATOM   1938  N   VAL A 263       5.849  32.956  28.092  1.00  4.06
ATOM   1939  CA  VAL A 263       5.636  31.746  27.304  1.00  3.37
ATOM   1940  C   VAL A 263       5.800  30.477  28.142  1.00  3.20
ATOM   1941  O   VAL A 263       6.373  30.508  29.237  1.00  2.00
ATOM   1942  CB  VAL A 263       6.572  31.703  26.064  1.00  3.63
ATOM   1943  CG1 VAL A 263       6.361  32.961  25.208  1.00  6.18
ATOM   1944  CG2 VAL A 263       8.027  31.580  26.497  1.00  5.29
ATOM   1945  N   ASP A 264       5.297  29.363  27.618  1.00  4.38
ATOM   1946  CA  ASP A 264       5.387  28.072  28.304  1.00  3.77
ATOM   1947  C   ASP A 264       6.799  27.487  28.244  1.00  3.83
ATOM   1948  O   ASP A 264       7.280  26.909  29.224  1.00  6.32
ATOM   1949  CB  ASP A 264       4.416  27.074  27.675  1.00  2.65
ATOM   1950  CG  ASP A 264       2.985  27.531  27.738  1.00  2.00
ATOM   1951  OD1 ASP A 264       2.621  28.272  28.671  1.00  2.22
ATOM   1952  OD2 ASP A 264       2.210  27.132  26.852  1.00  2.93
ATOM   1953  N   PHE A 265       7.452  27.625  27.092  1.00  3.27
ATOM   1954  CA  PHE A 265       8.804  27.105  26.892  1.00  4.64
ATOM   1955  C   PHE A 265       9.648  28.133  26.153  1.00  5.57
ATOM   1956  O   PHE A 265       9.138  28.844  25.276  1.00  4.86
ATOM   1957  CB  PHE A 265       8.778  25.822  26.040  1.00  2.97
ATOM   1958  CG  PHE A 265       7.936  24.713  26.608  1.00  2.00
ATOM   1959  CD1 PHE A 265       6.567  24.668  26.359  1.00  2.00
ATOM   1960  CD2 PHE A 265       8.510  23.705  27.382  1.00  5.43
ATOM   1961  CE1 PHE A 265       5.776  23.638  26.867  1.00  2.00
ATOM   1962  CE2 PHE A 265       7.723  22.663  27.900  1.00  2.00
ATOM   1963  CZ  PHE A 265       6.353  22.635  27.639  1.00  2.00
ATOM   1964  N   SER A 266      10.933  28.203  26.493  1.00  6.05
ATOM   1965  CA  SER A 266      11.859  29.113  25.823  1.00  8.35
ATOM   1966  C   SER A 266      13.235  28.449  25.686  1.00  9.64
ATOM   1967  O   SER A 266      13.567  27.513  26.430  1.00  8.47
ATOM   1968  CB  SER A 266      11.979  30.458  26.554  1.00  8.31
ATOM   1969  OG  SER A 266      12.763  30.375  27.726  1.00  8.88
ATOM   1970  N   LEU A 267      14.015  28.908  24.709  1.00  7.36
ATOM   1971  CA  LEU A 267      15.345  28.360  24.477  1.00  6.73
ATOM   1972  C   LEU A 267      16.338  29.422  24.027  1.00  7.36
ATOM   1973  O   LEU A 267      16.064  30.188  23.104  1.00  8.73
ATOM   1974  CB  LEU A 267      15.292  27.255  23.418  1.00  3.89
ATOM   1975  CG  LEU A 267      14.464  26.008  23.705  1.00  2.82
ATOM   1976  CD1 LEU A 267      13.161  26.052  22.922  1.00  2.00
ATOM   1977  CD2 LEU A 267      15.270  24.782  23.334  1.00  2.00
ATOM   1978  N   GLU A 268      17.502  29.442  24.658  1.00  6.07
ATOM   1979  CA  GLU A 268      18.547  30.389  24.302  1.00  5.50
ATOM   1980  C   GLU A 268      19.541  29.669  23.386  1.00  6.47
ATOM   1981  O   GLU A 268      20.096  28.636  23.761  1.00  7.14
ATOM   1982  CB  GLU A 268      19.247  30.879  25.567  1.00  2.00
ATOM   1983  CG  GLU A 268      20.294  31.949  25.333  1.00  2.00
ATOM   1984  CD  GLU A 268      21.685  31.403  25.054  1.00  6.26
ATOM   1985  OE1 GLU A 268      21.937  30.189  25.245  1.00  8.02
ATOM   1986  OE2 GLU A 268      22.544  32.216  24.672  1.00 11.00
ATOM   1987  N   CYS A 269      19.797  30.227  22.205  1.00  9.02
ATOM   1988  CA  CYS A 269      20.711  29.601  21.248  1.00  7.43
ATOM   1989  C   CYS A 269      21.679  30.634  20.658  1.00  6.72
ATOM   1990  O   CYS A 269      21.798  30.761  19.431  1.00  8.24
ATOM   1991  CB  CYS A 269      19.900  28.934  20.122  1.00  7.11
ATOM   1992  SG  CYS A 269      18.509  27.847  20.650  1.00  3.17
ATOM   1993  N   VAL A 270      22.379  31.343  21.539  1.00  4.29
ATOM   1994  CA  VAL A 270      23.336  32.390  21.151  1.00  7.62
ATOM   1995  C   VAL A 270      24.742  32.209  21.760  1.00  9.26
ATOM   1996  O   VAL A 270      25.756  32.336  21.074  1.00  8.40
ATOM   1997  CB  VAL A 270      22.829  33.804  21.589  1.00  5.12
ATOM   1998  CG1 VAL A 270      23.855  34.881  21.219  1.00  4.47
ATOM   1999  CG2 VAL A 270      21.486  34.122  20.969  1.00  2.00
ATOM   2000  N   GLY A 271      24.784  31.928  23.058  1.00 11.47
ATOM   2001  CA  GLY A 271      26.046  31.783  23.761  1.00 10.96
ATOM   2002  C   GLY A 271      26.374  33.064  24.518  1.00 13.07
ATOM   2003  O   GLY A 271      27.536  33.374  24.755  1.00 16.75
ATOM   2004  N   ASN A 272      25.346  33.807  24.916  1.00 11.53
ATOM   2005  CA  ASN A 272      25.531  35.062  25.643  1.00 10.33
ATOM   2006  C   ASN A 272      24.785  34.993  26.974  1.00  9.11
ATOM   2007  O   ASN A 272      23.564  34.823  26.989  1.00 10.18
ATOM   2008  CB  ASN A 272      25.010  36.234  24.805  1.00  9.24
ATOM   2009  CG  ASN A 272      25.114  37.560  25.530  1.00 12.06
ATOM   2010  OD1 ASN A 272      24.255  37.907  26.342  1.00 10.02
ATOM   2011  ND2 ASN A 272      26.179  38.300  25.259  1.00 14.78
ATOM   2012  N   VAL A 273      25.504  35.160  28.082  1.00  7.35
ATOM   2013  CA  VAL A 273      24.876  35.071  29.405  1.00  5.70
ATOM   2014  C   VAL A 273      23.729  36.048  29.646  1.00  4.05
ATOM   2015  O   VAL A 273      22.798  35.741  30.395  1.00  3.48
ATOM   2016  CB  VAL A 273      25.902  35.152  30.575  1.00  5.25
ATOM   2017  CG1 VAL A 273      26.826  33.957  30.542  1.00  2.00
ATOM   2018  CG2 VAL A 273      26.704  36.441  30.515  1.00  3.89
ATOM   2019  N   GLY A 274      23.783  37.215  29.012  1.00  2.00
ATOM   2020  CA  GLY A 274      22.718  38.190  29.178  1.00  2.00
ATOM   2021  C   GLY A 274      21.446  37.694  28.520  1.00  2.57
ATOM   2022  O   GLY A 274      20.344  37.865  29.053  1.00  2.58
ATOM   2023  N   VAL A 275      21.593  37.089  27.341  1.00  4.75
ATOM   2024  CA  VAL A 275      20.450  36.525  26.606  1.00  3.95
ATOM   2025  C   VAL A 275      19.875  35.328  27.378  1.00  2.70
ATOM   2026  O   VAL A 275      18.660  35.104  27.383  1.00  5.36
ATOM   2027  CB  VAL A 275      20.864  36.060  25.185  1.00  2.19
ATOM   2028  CG1 VAL A 275      19.666  35.476  24.433  1.00  3.13
ATOM   2029  CG2 VAL A 275      21.481  37.224  24.406  1.00  2.24
ATOM   2030  N   MET A 276      20.750  34.574  28.038  1.00  2.52
ATOM   2031  CA  MET A 276      20.328  33.410  28.812  1.00  4.31
ATOM   2032  C   MET A 276      19.381  33.806  29.940  1.00  5.90
ATOM   2033  O   MET A 276      18.394  33.115  30.209  1.00  5.95
ATOM   2034  CB  MET A 276      21.541  32.688  29.395  1.00  5.35
ATOM   2035  CG  MET A 276      22.505  32.153  28.372  1.00  5.33
ATOM   2036  SD  MET A 276      23.864  31.323  29.174  1.00  7.44
ATOM   2037  CE  MET A 276      24.954  30.960  27.755  1.00  5.43
ATOM   2038  N   ARG A 277      19.697  34.917  30.600  1.00  7.65
ATOM   2039  CA  ARG A 277      18.885  35.423  31.699  1.00  9.03
ATOM   2040  C   ARG A 277      17.527  35.878  31.182  1.00 10.46
ATOM   2041  O   ARG A 277      16.493  35.579  31.785  1.00 10.42
ATOM   2042  CB  ARG A 277      19.593  36.594  32.377  1.00 10.31
ATOM   2043  CG  ARG A 277      18.826  37.182  33.538  1.00 10.56
ATOM   2044  CD  ARG A 277      19.626  38.261  34.251  1.00  8.46
ATOM   2045  NE  ARG A 277      18.963  38.677  35.483  1.00  7.81
ATOM   2046  CZ  ARG A 277      19.594  39.085  36.584  1.00 10.43
ATOM   2047  NH1 ARG A 277      20.917  39.147  36.614  1.00  6.79
ATOM   2048  NH2 ARG A 277      18.900  39.388  37.674  1.00  3.20
ATOM   2049  N   ASN A 278      17.546  36.583  30.051  1.00 11.55
ATOM   2050  CA  ASN A 278      16.339  37.102  29.405  1.00  9.41
ATOM   2051  C   ASN A 278      15.368  36.012  28.971  1.00  7.14
ATOM   2052  O   ASN A 278      14.153  36.168  29.110  1.00  5.24
ATOM   2053  CB  ASN A 278      16.706  37.979  28.205  1.00 13.91
ATOM   2054  CG  ASN A 278      17.192  39.355  28.619  1.00 18.09
ATOM   2055  OD1 ASN A 278      17.094  39.736  29.779  1.00 21.57
ATOM   2056  ND2 ASN A 278      17.698  40.114  27.668  1.00 21.33
ATOM   2057  N   ALA A 279      15.905  34.920  28.431  1.00  5.36
ATOM   2058  CA  ALA A 279      15.094  33.778  28.000  1.00  4.40
ATOM   2059  C   ALA A 279      14.346  33.187  29.201  1.00  4.77
ATOM   2060  O   ALA A 279      13.147  32.911  29.124  1.00  4.61
ATOM   2061  CB  ALA A 279      15.982  32.714  27.363  1.00  5.58
ATOM   2062  N   LEU A 280      15.054  33.008  30.319  1.00  5.49
ATOM   2063  CA  LEU A 280      14.442  32.456  31.525  1.00  3.87
ATOM   2064  C   LEU A 280      13.297  33.330  32.007  1.00  2.12
ATOM   2065  O   LEU A 280      12.194  32.851  32.249  1.00  3.89
ATOM   2066  CB  LEU A 280      15.479  32.314  32.651  1.00  3.67
ATOM   2067  CG  LEU A 280      14.904  31.968  34.035  1.00  4.31
ATOM   2068  CD1 LEU A 280      14.438  30.523  34.092  1.00  2.00
ATOM   2069  CD2 LEU A 280      15.925  32.246  35.123  1.00  4.64
ATOM   2070  N   GLU A 281      13.564  34.624  32.107  1.00  2.64
ATOM   2071  CA  GLU A 281      12.584  35.580  32.592  1.00  3.36
ATOM   2072  C   GLU A 281      11.407  35.870  31.672  1.00  5.92
ATOM   2073  O   GLU A 281      10.409  36.453  32.111  1.00  6.85
ATOM   2074  CB  GLU A 281      13.296  36.858  33.048  1.00  4.43
ATOM   2075  CG  GLU A 281      14.270  36.579  34.208  1.00  6.71
ATOM   2076  CD  GLU A 281      15.032  37.807  34.705  1.00  7.73
ATOM   2077  OE1 GLU A 281      14.751  38.924  34.239  1.00  8.32
ATOM   2078  OE2 GLU A 281      15.915  37.649  35.574  1.00  8.83
ATOM   2079  N   SER A 282      11.505  35.467  30.408  1.00  4.55
ATOM   2080  CA  SER A 282      10.402  35.673  29.472  1.00  4.85
ATOM   2081  C   SER A 282       9.342  34.568  29.663  1.00  4.13
ATOM   2082  O   SER A 282       8.237  34.652  29.114  1.00  2.00
ATOM   2083  CB  SER A 282      10.919  35.692  28.017  1.00  7.65
ATOM   2084  OG  SER A 282      11.914  36.699  27.806  1.00  3.86
ATOM   2085  N   CYS A 283       9.692  33.540  30.442  1.00  5.57
ATOM   2086  CA  CYS A 283       8.807  32.399  30.728  1.00  5.25
ATOM   2087  C   CYS A 283       7.730  32.725  31.759  1.00  6.22
ATOM   2088  O   CYS A 283       7.922  33.581  32.625  1.00  6.52
ATOM   2089  CB  CYS A 283       9.613  31.190  31.233  1.00  4.73
ATOM   2090  SG  CYS A 283      10.492  30.241  29.965  1.00  4.36
ATOM   2091  N   LEU A 284       6.611  32.010  31.677  1.00  4.93
ATOM   2092  CA  LEU A 284       5.496  32.203  32.594  1.00  4.14
ATOM   2093  C   LEU A 284       5.787  31.570  33.952  1.00  4.77
ATOM   2094  O   LEU A 284       6.555  30.604  34.064  1.00  3.60
ATOM   2095  CB  LEU A 284       4.213  31.604  32.005  1.00  2.00
ATOM   2096  CG  LEU A 284       2.896  31.778  32.776  1.00  4.94
ATOM   2097  CD1 LEU A 284       2.509  33.245  32.888  1.00  5.34
ATOM   2098  CD2 LEU A 284       1.798  31.022  32.083  1.00  4.64
ATOM   2099  N   LYS A 285       5.160  32.119  34.983  1.00  5.35
ATOM   2100  CA  LYS A 285       5.317  31.619  36.344  1.00  6.81
ATOM   2101  C   LYS A 285       4.554  30.291  36.443  1.00  7.23
ATOM   2102  O   LYS A 285       3.747  29.967  35.561  1.00  7.19
ATOM   2103  CB  LYS A 285       4.723  32.633  37.335  1.00  7.67
ATOM   2104  CG  LYS A 285       3.216  32.812  37.202  1.00 12.86
ATOM   2105  CD  LYS A 285       2.643  33.759  38.244  1.00 15.80
ATOM   2106  CE  LYS A 285       1.156  33.967  38.014  1.00 20.27
ATOM   2107  NZ  LYS A 285       0.568  34.921  38.997  1.00 24.74
ATOM   2108  N   GLY A 286       4.832  29.504  37.481  1.00  3.53
ATOM   2109  CA  GLY A 286       4.113  28.254  37.655  1.00  2.00
ATOM   2110  C   GLY A 286       4.592  27.024  36.895  1.00  3.08
ATOM   2111  O   GLY A 286       4.764  25.975  37.515  1.00  2.00
ATOM   2112  N   TRP A 287       4.725  27.114  35.569  1.00  4.64
ATOM   2113  CA  TRP A 287       5.181  25.977  34.766  1.00  4.60
ATOM   2114  C   TRP A 287       6.160  26.307  33.632  1.00  5.89
ATOM   2115  O   TRP A 287       6.446  25.455  32.794  1.00  5.53
ATOM   2116  CB  TRP A 287       3.990  25.184  34.218  1.00  7.00
ATOM   2117  CG  TRP A 287       3.068  25.956  33.297  1.00 11.33
ATOM   2118  CD1 TRP A 287       3.371  26.472  32.065  1.00  9.30
ATOM   2119  CD2 TRP A 287       1.682  26.259  33.525  1.00 11.67
ATOM   2120  NE1 TRP A 287       2.260  27.074  31.517  1.00  9.67
ATOM   2121  CE2 TRP A 287       1.211  26.956  32.391  1.00 10.92
ATOM   2122  CE3 TRP A 287       0.793  25.999  34.580  1.00 11.68
ATOM   2123  CZ2 TRP A 287      -0.112  27.405  32.279  1.00 11.72
ATOM   2124  CZ3 TRP A 287      -0.521  26.442  34.468  1.00 12.61
ATOM   2125  CH2 TRP A 287      -0.961  27.137  33.325  1.00 12.75
ATOM   2126  N   GLY A 288       6.689  27.527  33.614  1.00  3.11
ATOM   2127  CA  GLY A 288       7.629  27.897  32.565  1.00  4.14
ATOM   2128  C   GLY A 288       8.942  27.126  32.616  1.00  3.84
ATOM   2129  O   GLY A 288       9.523  26.952  33.692  1.00  2.35
ATOM   2130  N   VAL A 289       9.418  26.677  31.457  1.00  2.24
ATOM   2131  CA  VAL A 289      10.672  25.931  31.362  1.00  2.17
ATOM   2132  C   VAL A 289      11.609  26.584  30.329  1.00  2.35
ATOM   2133  O   VAL A 289      11.226  26.771  29.175  1.00  3.33
ATOM   2134  CB  VAL A 289      10.424  24.449  30.953  1.00  4.18
ATOM   2135  CG1 VAL A 289      11.761  23.693  30.802  1.00  4.33
ATOM   2136  CG2 VAL A 289       9.542  23.754  31.990  1.00  2.00
ATOM   2137  N   SER A 290      12.815  26.953  30.760  1.00  2.85
ATOM   2138  CA  SER A 290      13.817  27.570  29.881  1.00  2.45
ATOM   2139  C   SER A 290      15.039  26.649  29.807  1.00  3.58
ATOM   2140  O   SER A 290      15.468  26.077  30.824  1.00  3.22
ATOM   2141  CB  SER A 290      14.215  28.951  30.413  1.00  3.65
ATOM   2142  OG  SER A 290      15.042  29.661  29.502  1.00  4.73
ATOM   2143  N   VAL A 291      15.610  26.537  28.610  1.00  4.66
ATOM   2144  CA  VAL A 291      16.766  25.667  28.343  1.00  3.26
ATOM   2145  C   VAL A 291      17.958  26.395  27.709  1.00  2.29
ATOM   2146  O   VAL A 291      17.792  27.145  26.739  1.00  2.18
ATOM   2147  CB  VAL A 291      16.351  24.524  27.375  1.00  2.04
ATOM   2148  CG1 VAL A 291      17.505  23.591  27.110  1.00  3.41
ATOM   2149  CG2 VAL A 291      15.162  23.765  27.932  1.00  5.59
ATOM   2150  N   LEU A 292      19.139  26.211  28.295  1.00  4.09
ATOM   2151  CA  LEU A 292      20.391  26.791  27.781  1.00  7.60
ATOM   2152  C   LEU A 292      20.943  25.893  26.668  1.00  7.17
ATOM   2153  O   LEU A 292      21.041  24.673  26.841  1.00  7.76
ATOM   2154  CB  LEU A 292      21.481  26.839  28.865  1.00  9.60
ATOM   2155  CG  LEU A 292      21.468  27.724  30.113  1.00 13.26
ATOM   2156  CD1 LEU A 292      22.803  27.562  30.813  1.00 14.49
ATOM   2157  CD2 LEU A 292      21.270  29.177  29.746  1.00 15.88
ATOM   2158  N   VAL A 293      21.376  26.502  25.568  1.00  5.74
ATOM   2159  CA  VAL A 293      21.940  25.746  24.451  1.00 10.79
ATOM   2160  C   VAL A 293      23.253  26.404  24.017  1.00 13.03
ATOM   2161  O   VAL A 293      24.226  25.712  23.708  1.00 14.18
ATOM   2162  CB  VAL A 293      20.974  25.652  23.240  1.00  9.55
ATOM   2163  CG1 VAL A 293      21.509  24.641  22.241  1.00  8.24
ATOM   2164  CG2 VAL A 293      19.576  25.258  23.694  1.00 11.94
ATOM   2165  N   GLY A 294      23.286  27.736  24.044  1.00 13.73
ATOM   2166  CA  GLY A 294      24.488  28.472  23.683  1.00 13.79
ATOM   2167  C   GLY A 294      25.658  28.128  24.591  1.00 16.05
ATOM   2168  O   GLY A 294      25.465  27.805  25.765  1.00 17.31
ATOM   2169  N   TRP A 295      26.877  28.274  24.083  1.00 16.07
ATOM   2170  CA  TRP A 295      28.058  27.924  24.864  1.00 16.38
ATOM   2171  C   TRP A 295      29.045  29.038  25.227  1.00 16.21
ATOM   2172  O   TRP A 295      29.421  29.861  24.394  1.00 16.89
ATOM   2173  CB  TRP A 295      28.824  26.780  24.172  1.00 15.29
ATOM   2174  CG  TRP A 295      30.159  26.460  24.819  1.00 16.54
ATOM   2175  CD1 TRP A 295      31.404  26.599  24.256  1.00 17.12
ATOM   2176  CD2 TRP A 295      30.383  25.981  26.158  1.00 17.48
ATOM   2177  NE1 TRP A 295      32.377  26.242  25.162  1.00 16.60
ATOM   2178  CE2 TRP A 295      31.778  25.860  26.335  1.00 18.11
ATOM   2179  CE3 TRP A 295      29.529  25.646  27.223  1.00 17.52
ATOM   2180  CZ2 TRP A 295      32.348  25.415  27.538  1.00 17.62
ATOM   2181  CZ3 TRP A 295      30.099  25.203  28.421  1.00 20.64
ATOM   2182  CH2 TRP A 295      31.495  25.092  28.566  1.00 20.66
ATOM   2183  N   THR A 296      29.474  29.019  26.486  1.00 15.35
ATOM   2184  CA  THR A 296      30.470  29.941  27.018  1.00 12.34
ATOM   2185  C   THR A 296      30.856  29.508  28.423  1.00 12.16
ATOM   2186  O   THR A 296      30.038  28.932  29.148  1.00  8.85
ATOM   2187  CB  THR A 296      30.010  31.425  27.049  1.00 13.74
ATOM   2188  OG1 THR A 296      31.066  32.226  27.609  1.00 11.91
ATOM   2189  CG2 THR A 296      28.741  31.601  27.881  1.00  8.61
ATOM   2190  N   ASP A 297      32.120  29.745  28.770  1.00 10.77
ATOM   2191  CA  ASP A 297      32.653  29.415  30.088  1.00 11.42
ATOM   2192  C   ASP A 297      33.558  30.551  30.552  1.00  9.55
ATOM   2193  O   ASP A 297      34.499  30.347  31.303  1.00  8.83
ATOM   2194  CB  ASP A 297      33.449  28.111  30.046  1.00 12.48
ATOM   2195  CG  ASP A 297      33.783  27.593  31.435  1.00 14.62
ATOM   2196  OD1 ASP A 297      32.850  27.408  32.242  1.00 14.87
ATOM   2197  OD2 ASP A 297      34.973  27.376  31.725  1.00 17.36
ATOM   2198  N   LEU A 298      33.252  31.755  30.094  1.00 11.69
ATOM   2199  CA  LEU A 298      34.028  32.930  30.436  1.00 13.75
ATOM   2200  C   LEU A 298      33.250  33.816  31.408  1.00 13.81
ATOM   2201  O   LEU A 298      33.803  34.765  31.972  1.00 15.19
ATOM   2202  CB  LEU A 298      34.360  33.708  29.156  1.00 15.45
ATOM   2203  CG  LEU A 298      35.103  32.950  28.042  1.00 17.59
ATOM   2204  CD1 LEU A 298      35.238  33.828  26.804  1.00 15.99
ATOM   2205  CD2 LEU A 298      36.474  32.499  28.527  1.00 16.39
ATOM   2206  N   HIS A 299      31.958  33.530  31.570  1.00 14.00
ATOM   2207  CA  HIS A 299      31.086  34.304  32.461  1.00 12.22
ATOM   2208  C   HIS A 299      30.030  33.410  33.112  1.00 12.35
ATOM   2209  O   HIS A 299      29.750  32.309  32.624  1.00 11.49
ATOM   2210  CB  HIS A 299      30.361  35.416  31.688  1.00 12.18
ATOM   2211  CG  HIS A 299      31.263  36.266  30.845  1.00 15.87
ATOM   2212  ND1 HIS A 299      32.025  37.291  31.363  1.00 16.95
ATOM   2213  CD2 HIS A 299      31.537  36.228  29.518  1.00 15.48
ATOM   2214  CE1 HIS A 299      32.734  37.844  30.395  1.00 17.35
ATOM   2215  NE2 HIS A 299      32.457  37.217  29.266  1.00 15.55
ATOM   2216  N   ASP A 300      29.476  33.891  34.225  1.00 11.39
ATOM   2217  CA  ASP A 300      28.426  33.199  34.973  1.00 10.63
ATOM   2218  C   ASP A 300      27.070  33.677  34.445  1.00 11.50
ATOM   2219  O   ASP A 300      26.963  34.792  33.930  1.00 12.37
ATOM   2220  CB  ASP A 300      28.467  33.588  36.465  1.00 12.45
ATOM   2221  CG  ASP A 300      29.614  32.946  37.234  1.00 13.15
ATOM   2222  OD1 ASP A 300      30.120  31.891  36.810  1.00 12.90
ATOM   2223  OD2 ASP A 300      29.982  33.488  38.301  1.00 13.51
ATOM   2224  N   VAL A 301      26.054  32.824  34.532  1.00  9.61
ATOM   2225  CA  VAL A 301      24.702  33.210  34.144  1.00  6.93
ATOM   2226  C   VAL A 301      24.032  33.423  35.512  1.00  8.73
ATOM   2227  O   VAL A 301      24.388  32.744  36.486  1.00  7.71
ATOM   2228  CB  VAL A 301      23.975  32.115  33.316  1.00  6.61
ATOM   2229  CG1 VAL A 301      23.721  30.872  34.145  1.00  7.98
ATOM   2230  CG2 VAL A 301      22.678  32.652  32.770  1.00  2.02
ATOM   2231  N   ALA A 302      23.096  34.366  35.601  1.00  9.20
ATOM   2232  CA  ALA A 302      22.450  34.662  36.874  1.00  9.55
ATOM   2233  C   ALA A 302      20.998  35.100  36.764  1.00  9.10
ATOM   2234  O   ALA A 302      20.476  35.301  35.664  1.00 11.19
ATOM   2235  CB  ALA A 302      23.253  35.735  37.607  1.00  9.60
ATOM   2236  N   THR A 303      20.347  35.230  37.917  1.00  7.42
ATOM   2237  CA  THR A 303      18.960  35.672  37.996  1.00  8.31
ATOM   2238  C   THR A 303      18.624  35.889  39.475  1.00  9.97
ATOM   2239  O   THR A 303      19.489  35.760  40.337  1.00  9.04
ATOM   2240  CB  THR A 303      17.970  34.646  37.347  1.00  9.84
ATOM   2241  OG1 THR A 303      16.661  35.228  37.235  1.00 10.12
ATOM   2242  CG2 THR A 303      17.872  33.379  38.164  1.00  6.30
ATOM   2243  N   ARG A 304      17.388  36.287  39.753  1.00 12.35
ATOM   2244  CA  ARG A 304      16.939  36.505  41.119  1.00 11.51
ATOM   2245  C   ARG A 304      16.236  35.240  41.598  1.00 11.80
ATOM   2246  O   ARG A 304      15.474  34.620  40.840  1.00 11.92
ATOM   2247  CB  ARG A 304      15.965  37.686  41.183  1.00 11.37
ATOM   2248  CG  ARG A 304      16.631  39.049  41.223  1.00 15.17
ATOM   2249  CD  ARG A 304      17.671  39.104  42.329  1.00 18.67
ATOM   2250  NE  ARG A 304      17.605  40.331  43.117  1.00 22.65
ATOM   2251  CZ  ARG A 304      18.149  41.492  42.766  1.00 23.25
ATOM   2252  NH1 ARG A 304      18.811  41.610  41.625  1.00 23.48
ATOM   2253  NH2 ARG A 304      18.034  42.537  43.570  1.00 23.94
ATOM   2254  N   PRO A 305      16.442  34.859  42.873  1.00 10.89
ATOM   2255  CA  PRO A 305      15.816  33.658  43.442  1.00  9.18
ATOM   2256  C   PRO A 305      14.307  33.543  43.184  1.00  7.92
ATOM   2257  O   PRO A 305      13.801  32.456  42.894  1.00  8.73
ATOM   2258  CB  PRO A 305      16.133  33.797  44.929  1.00 10.71
ATOM   2259  CG  PRO A 305      17.489  34.427  44.905  1.00  9.56
ATOM   2260  CD  PRO A 305      17.329  35.503  43.859  1.00  7.72
ATOM   2261  N   ILE A 306      13.603  34.671  43.244  1.00  7.44
ATOM   2262  CA  ILE A 306      12.156  34.721  43.021  1.00  7.38
ATOM   2263  C   ILE A 306      11.756  34.145  41.662  1.00  6.35
ATOM   2264  O   ILE A 306      10.720  33.493  41.547  1.00  6.12
ATOM   2265  CB  ILE A 306      11.588  36.172  43.180  1.00  7.56
ATOM   2266  CG1 ILE A 306      10.061  36.186  43.003  1.00  9.71
ATOM   2267  CG2 ILE A 306      12.236  37.122  42.181  1.00  7.86
ATOM   2268  CD1 ILE A 306       9.296  35.407  44.068  1.00 10.69
ATOM   2269  N   GLN A 307      12.590  34.343  40.645  1.00  7.25
ATOM   2270  CA  GLN A 307      12.282  33.816  39.318  1.00  6.45
ATOM   2271  C   GLN A 307      11.967  32.317  39.362  1.00  3.51
ATOM   2272  O   GLN A 307      11.000  31.862  38.752  1.00  7.44
ATOM   2273  CB  GLN A 307      13.438  34.082  38.342  1.00  8.39
ATOM   2274  CG  GLN A 307      13.610  35.539  37.937  1.00  7.44
ATOM   2275  CD  GLN A 307      12.312  36.191  37.476  1.00  8.12
ATOM   2276  OE1 GLN A 307      11.927  37.244  37.990  1.00 11.23
ATOM   2277  NE2 GLN A 307      11.633  35.572  36.519  1.00  2.00
ATOM   2278  N   LEU A 308      12.762  31.565  40.117  1.00  3.89
ATOM   2279  CA  LEU A 308      12.580  30.116  40.241  1.00  4.80
ATOM   2280  C   LEU A 308      11.555  29.735  41.295  1.00  5.28
ATOM   2281  O   LEU A 308      10.804  28.776  41.111  1.00  6.01
ATOM   2282  CB  LEU A 308      13.916  29.424  40.533  1.00  3.19
ATOM   2283  CG  LEU A 308      15.010  29.637  39.476  1.00  4.94
ATOM   2284  CD1 LEU A 308      16.312  29.024  39.955  1.00 10.54
ATOM   2285  CD2 LEU A 308      14.598  29.049  38.132  1.00  3.57
ATOM   2286  N   ILE A 309      11.516  30.484  42.397  1.00  4.77
ATOM   2287  CA  ILE A 309      10.565  30.210  43.478  1.00  5.70
ATOM   2288  C   ILE A 309       9.109  30.411  43.013  1.00  6.73
ATOM   2289  O   ILE A 309       8.174  29.793  43.539  1.00  6.80
ATOM   2290  CB  ILE A 309      10.904  31.061  44.744  1.00  4.66
ATOM   2291  CG1 ILE A 309      12.131  30.471  45.453  1.00  2.05
ATOM   2292  CG2 ILE A 309       9.726  31.110  45.707  1.00  6.86
ATOM   2293  CD1 ILE A 309      12.727  31.372  46.533  1.00  2.11
ATOM   2294  N   ALA A 310       8.930  31.249  41.996  1.00  7.09
ATOM   2295  CA  ALA A 310       7.611  31.521  41.422  1.00  4.84
ATOM   2296  C   ALA A 310       7.097  30.349  40.584  1.00  5.68
ATOM   2297  O   ALA A 310       5.949  30.367  40.127  1.00  9.56
ATOM   2298  CB  ALA A 310       7.666  32.776  40.567  1.00  5.93
ATOM   2299  N   GLY A 311       7.959  29.367  40.332  1.00  5.84
ATOM   2300  CA  GLY A 311       7.567  28.198  39.555  1.00  5.68
ATOM   2301  C   GLY A 311       8.310  27.926  38.247  1.00  4.32
ATOM   2302  O   GLY A 311       7.845  27.121  37.442  1.00  4.51
ATOM   2303  N   ARG A 312       9.426  28.604  37.998  1.00  3.40
ATOM   2304  CA  ARG A 312      10.176  28.376  36.758  1.00  3.91
ATOM   2305  C   ARG A 312      11.244  27.306  36.916  1.00  3.90
ATOM   2306  O   ARG A 312      11.760  27.091  38.017  1.00  3.33
ATOM   2307  CB  ARG A 312      10.823  29.674  36.256  1.00  2.00
ATOM   2308  CG  ARG A 312       9.819  30.698  35.762  1.00  3.61
ATOM   2309  CD  ARG A 312      10.481  32.025  35.420  1.00  2.00
ATOM   2310  NE  ARG A 312       9.483  33.025  35.040  1.00  8.68
ATOM   2311  CZ  ARG A 312       8.796  33.771  35.900  1.00  4.60
ATOM   2312  NH1 ARG A 312       8.998  33.636  37.202  1.00 10.77
ATOM   2313  NH2 ARG A 312       7.905  34.649  35.458  1.00  2.00
ATOM   2314  N   THR A 313      11.567  26.643  35.808  1.00  3.41
ATOM   2315  CA  THR A 313      12.584  25.600  35.780  1.00  3.98
ATOM   2316  C   THR A 313      13.695  25.989  34.781  1.00  3.66
ATOM   2317  O   THR A 313      13.421  26.513  33.691  1.00  2.00
ATOM   2318  CB  THR A 313      11.952  24.228  35.400  1.00  4.49
ATOM   2319  OG1 THR A 313      10.969  23.869  36.378  1.00  2.00
ATOM   2320  CG2 THR A 313      13.010  23.127  35.369  1.00  4.82
ATOM   2321  N   TRP A 314      14.946  25.777  35.181  1.00  5.47
ATOM   2322  CA  TRP A 314      16.098  26.111  34.341  1.00  5.83
ATOM   2323  C   TRP A 314      16.893  24.845  34.068  1.00  5.18
ATOM   2324  O   TRP A 314      17.306  24.147  35.007  1.00  2.02
ATOM   2325  CB  TRP A 314      17.003  27.124  35.052  1.00  5.33
ATOM   2326  CG  TRP A 314      17.621  28.140  34.145  1.00  4.47
ATOM   2327  CD1 TRP A 314      17.527  28.197  32.777  1.00  2.13
ATOM   2328  CD2 TRP A 314      18.381  29.287  34.545  1.00  2.54
ATOM   2329  NE1 TRP A 314      18.172  29.317  32.307  1.00  4.39
ATOM   2330  CE2 TRP A 314      18.705  30.004  33.365  1.00  2.00
ATOM   2331  CE3 TRP A 314      18.820  29.783  35.776  1.00  5.01
ATOM   2332  CZ2 TRP A 314      19.448  31.188  33.389  1.00  5.78
ATOM   2333  CZ3 TRP A 314      19.562  30.965  35.801  1.00  8.12
ATOM   2334  CH2 TRP A 314      19.866  31.654  34.612  1.00  6.68
ATOM   2335  N   LYS A 315      17.120  24.574  32.787  1.00  4.18
ATOM   2336  CA  LYS A 315      17.858  23.396  32.349  1.00  5.72
ATOM   2337  C   LYS A 315      18.918  23.777  31.312  1.00  5.72
ATOM   2338  O   LYS A 315      19.044  24.940  30.918  1.00  3.54
ATOM   2339  CB  LYS A 315      16.903  22.381  31.716  1.00  6.71
ATOM   2340  CG  LYS A 315      15.928  21.712  32.662  1.00 10.67
ATOM   2341  CD  LYS A 315      14.941  20.860  31.868  1.00 11.38
ATOM   2342  CE  LYS A 315      14.203  19.874  32.748  1.00 11.12
ATOM   2343  NZ  LYS A 315      15.116  18.800  33.267  1.00 14.61
ATOM   2344  N   GLY A 316      19.668  22.781  30.866  1.00  4.30
ATOM   2345  CA  GLY A 316      20.696  22.995  29.867  1.00  6.39
ATOM   2346  C   GLY A 316      20.702  21.760  28.994  1.00  7.59
ATOM   2347  O   GLY A 316      20.253  20.697  29.435  1.00  7.96
ATOM   2348  N   SER A 317      21.219  21.882  27.775  1.00  9.21
ATOM   2349  CA  SER A 317      21.241  20.765  26.841  1.00  9.79
ATOM   2350  C   SER A 317      22.585  20.621  26.140  1.00 11.04
ATOM   2351  O   SER A 317      23.252  21.615  25.837  1.00  8.04
ATOM   2352  CB  SER A 317      20.143  20.967  25.787  1.00 10.78
ATOM   2353  OG  SER A 317      19.890  19.773  25.071  1.00  5.20
ATOM   2354  N   MET A 318      22.954  19.372  25.864  1.00 12.18
ATOM   2355  CA  MET A 318      24.198  19.032  25.178  1.00 11.15
ATOM   2356  C   MET A 318      23.796  18.114  24.019  1.00  9.64
ATOM   2357  O   MET A 318      23.182  17.062  24.232  1.00  7.05
ATOM   2358  CB  MET A 318      25.144  18.297  26.130  1.00 14.57
ATOM   2359  CG  MET A 318      26.504  18.016  25.544  1.00 18.88
ATOM   2360  SD  MET A 318      27.523  17.065  26.660  1.00 22.29
ATOM   2361  CE  MET A 318      28.307  18.396  27.640  1.00 22.07
ATOM   2362  N   PHE A 319      24.086  18.542  22.796  1.00  4.40
ATOM   2363  CA  PHE A 319      23.727  17.779  21.598  1.00  3.36
ATOM   2364  C   PHE A 319      22.229  17.385  21.604  1.00  2.24
ATOM   2365  O   PHE A 319      21.860  16.262  21.281  1.00  2.00
ATOM   2366  CB  PHE A 319      24.640  16.550  21.426  1.00  4.11
ATOM   2367  CG  PHE A 319      24.580  15.923  20.035  1.00  8.03
ATOM   2368  CD1 PHE A 319      24.921  16.665  18.902  1.00  6.54
ATOM   2369  CD2 PHE A 319      24.177  14.600  19.869  1.00  7.78
ATOM   2370  CE1 PHE A 319      24.858  16.098  17.628  1.00  8.30
ATOM   2371  CE2 PHE A 319      24.112  14.019  18.594  1.00  8.99
ATOM   2372  CZ  PHE A 319      24.454  14.771  17.472  1.00  6.97
ATOM   2373  N   GLY A 320      21.376  18.326  22.000  1.00  3.22
ATOM   2374  CA  GLY A 320      19.940  18.085  22.022  1.00  2.13
ATOM   2375  C   GLY A 320      19.440  16.949  22.894  1.00  3.89
ATOM   2376  O   GLY A 320      18.309  16.491  22.727  1.00  2.00
ATOM   2377  N   GLY A 321      20.282  16.496  23.820  1.00  2.87
ATOM   2378  CA  GLY A 321      19.908  15.419  24.714  1.00  3.81
ATOM   2379  C   GLY A 321      19.812  14.064  24.039  1.00  6.47
ATOM   2380  O   GLY A 321      19.286  13.117  24.621  1.00  4.79
ATOM   2381  N   PHE A 322      20.307  13.970  22.809  1.00  6.06
ATOM   2382  CA  PHE A 322      20.292  12.715  22.055  1.00  3.48
ATOM   2383  C   PHE A 322      21.464  11.848  22.458  1.00  2.00
ATOM   2384  O   PHE A 322      22.560  12.351  22.690  1.00  2.00
ATOM   2385  CB  PHE A 322      20.465  12.973  20.548  1.00  2.08
ATOM   2386  CG  PHE A 322      19.214  13.404  19.841  1.00  2.00
ATOM   2387  CD1 PHE A 322      18.190  12.500  19.600  1.00  4.20
ATOM   2388  CD2 PHE A 322      19.076  14.710  19.382  1.00  3.86
ATOM   2389  CE1 PHE A 322      17.044  12.889  18.909  1.00  2.00
ATOM   2390  CE2 PHE A 322      17.938  15.107  18.693  1.00  2.00
ATOM   2391  CZ  PHE A 322      16.920  14.195  18.456  1.00  2.00
ATOM   2392  N   LYS A 323      21.239  10.544  22.543  1.00  3.29
ATOM   2393  CA  LYS A 323      22.326   9.622  22.811  1.00  3.00
ATOM   2394  C   LYS A 323      22.872   9.413  21.397  1.00  4.19
ATOM   2395  O   LYS A 323      22.183   8.884  20.525  1.00  4.31
ATOM   2396  CB  LYS A 323      21.810   8.323  23.442  1.00  3.34
ATOM   2397  CG  LYS A 323      21.528   8.479  24.951  1.00  4.91
ATOM   2398  CD  LYS A 323      20.542   7.455  25.458  1.00  5.45
ATOM   2399  CE  LYS A 323      21.113   6.634  26.608  1.00 10.85
ATOM   2400  NZ  LYS A 323      21.401   7.433  27.840  1.00  4.76
ATOM   2401  N   GLY A 324      24.070   9.946  21.165  1.00  5.86
ATOM   2402  CA  GLY A 324      24.728   9.888  19.871  1.00  2.33
ATOM   2403  C   GLY A 324      24.411   8.765  18.908  1.00  5.22
ATOM   2404  O   GLY A 324      23.802   8.987  17.862  1.00  5.45
ATOM   2405  N   LYS A 325      24.799   7.552  19.275  1.00  5.35
ATOM   2406  CA  LYS A 325      24.604   6.399  18.417  1.00  5.87
ATOM   2407  C   LYS A 325      23.163   5.973  18.209  1.00  5.80
ATOM   2408  O   LYS A 325      22.854   5.288  17.242  1.00  6.60
ATOM   2409  CB  LYS A 325      25.471   5.246  18.918  1.00  2.58
ATOM   2410  CG  LYS A 325      26.934   5.656  18.977  1.00  7.89
ATOM   2411  CD  LYS A 325      27.865   4.516  19.271  1.00  6.97
ATOM   2412  CE  LYS A 325      27.862   3.514  18.162  1.00 11.14
ATOM   2413  NZ  LYS A 325      29.045   2.644  18.281  1.00 13.31
ATOM   2414  N   ASP A 326      22.280   6.404  19.104  1.00  9.11
ATOM   2415  CA  ASP A 326      20.860   6.074  19.019  1.00  8.31
ATOM   2416  C   ASP A 326      20.083   7.109  18.216  1.00  8.96
ATOM   2417  O   ASP A 326      19.310   6.765  17.320  1.00 11.68
ATOM   2418  CB  ASP A 326      20.226   6.021  20.419  1.00  8.70
ATOM   2419  CG  ASP A 326      20.716   4.854  21.266  1.00 13.10
ATOM   2420  OD1 ASP A 326      21.575   4.067  20.815  1.00 14.93
ATOM   2421  OD2 ASP A 326      20.224   4.724  22.406  1.00 11.65
ATOM   2422  N   GLY A 327      20.248   8.374  18.592  1.00  5.84
ATOM   2423  CA  GLY A 327      19.524   9.462  17.953  1.00  4.61
ATOM   2424  C   GLY A 327      19.829   9.838  16.514  1.00  5.10
ATOM   2425  O   GLY A 327      18.907   9.980  15.714  1.00  2.90
ATOM   2426  N   VAL A 328      21.104   9.991  16.176  1.00  5.48
ATOM   2427  CA  VAL A 328      21.510  10.379  14.818  1.00  6.22
ATOM   2428  C   VAL A 328      20.962   9.489  13.694  1.00  5.53
ATOM   2429  O   VAL A 328      20.415   9.994  12.711  1.00  7.37
ATOM   2430  CB  VAL A 328      23.063  10.515  14.711  1.00  3.23
ATOM   2431  CG1 VAL A 328      23.473  10.975  13.316  1.00  4.66
ATOM   2432  CG2 VAL A 328      23.572  11.503  15.742  1.00  2.00
ATOM   2433  N   PRO A 329      21.074   8.156  13.823  1.00  8.39
ATOM   2434  CA  PRO A 329      20.557   7.279  12.760  1.00  7.39
ATOM   2435  C   PRO A 329      19.045   7.463  12.547  1.00 10.29
ATOM   2436  O   PRO A 329      18.535   7.381  11.416  1.00 10.54
ATOM   2437  CB  PRO A 329      20.890   5.876  13.282  1.00 12.24
ATOM   2438  CG  PRO A 329      22.135   6.120  14.147  1.00  6.65
ATOM   2439  CD  PRO A 329      21.751   7.372  14.874  1.00  7.47
ATOM   2440  N   LYS A 330      18.328   7.683  13.643  1.00  8.89
ATOM   2441  CA  LYS A 330      16.895   7.901  13.589  1.00  6.67
ATOM   2442  C   LYS A 330      16.552   9.231  12.896  1.00  7.00
ATOM   2443  O   LYS A 330      15.558   9.315  12.166  1.00  6.34
ATOM   2444  CB  LYS A 330      16.321   7.858  15.006  1.00 12.75
ATOM   2445  CG  LYS A 330      16.327   6.456  15.620  1.00 18.36
ATOM   2446  CD  LYS A 330      16.225   6.524  17.136  1.00 21.22
ATOM   2447  CE  LYS A 330      15.856   5.184  17.782  1.00 22.42
ATOM   2448  NZ  LYS A 330      16.630   4.000  17.317  1.00 24.75
ATOM   2449  N   MET A 331      17.364  10.264  13.123  1.00  5.97
ATOM   2450  CA  MET A 331      17.154  11.580  12.496  1.00  5.53
ATOM   2451  C   MET A 331      17.397  11.495  10.988  1.00  5.60
ATOM   2452  O   MET A 331      16.767  12.216  10.212  1.00  7.32
ATOM   2453  CB  MET A 331      18.045  12.666  13.123  1.00  4.69
ATOM   2454  CG  MET A 331      17.604  13.153  14.509  1.00  2.02
ATOM   2455  SD  MET A 331      15.971  13.944  14.541  1.00  5.67
ATOM   2456  CE  MET A 331      16.387  15.592  13.927  1.00  5.12
ATOM   2457  N   VAL A 332      18.321  10.628  10.574  1.00  5.33
ATOM   2458  CA  VAL A 332      18.591  10.433   9.151  1.00  6.23
ATOM   2459  C   VAL A 332      17.363   9.798   8.488  1.00  5.50
ATOM   2460  O   VAL A 332      16.882  10.285   7.462  1.00  6.09
ATOM   2461  CB  VAL A 332      19.825   9.536   8.919  1.00  5.08
ATOM   2462  CG1 VAL A 332      19.955   9.191   7.434  1.00  2.54
ATOM   2463  CG2 VAL A 332      21.082  10.253   9.395  1.00  4.73
ATOM   2464  N   LYS A 333      16.840   8.742   9.109  1.00  7.30
ATOM   2465  CA  LYS A 333      15.655   8.050   8.608  1.00  9.12
ATOM   2466  C   LYS A 333      14.485   9.029   8.499  1.00 10.65
ATOM   2467  O   LYS A 333      13.725   8.987   7.527  1.00 11.16
ATOM   2468  CB  LYS A 333      15.267   6.903   9.543  1.00 14.33
ATOM   2469  CG  LYS A 333      16.260   5.750   9.579  1.00 24.29
ATOM   2470  CD  LYS A 333      15.972   4.730   8.482  1.00 29.34
ATOM   2471  CE  LYS A 333      16.993   3.600   8.479  1.00 32.45
ATOM   2472  NZ  LYS A 333      16.709   2.587   7.409  1.00 37.13
ATOM   2473  N   ALA A 334      14.361   9.925   9.480  1.00  9.97
ATOM   2474  CA  ALA A 334      13.292  10.929   9.499  1.00  8.42
ATOM   2475  C   ALA A 334      13.398  11.904   8.324  1.00  9.59
ATOM   2476  O   ALA A 334      12.384  12.272   7.718  1.00  8.51
ATOM   2477  CB  ALA A 334      13.299  11.687  10.813  1.00  6.90
ATOM   2478  N   TYR A 335      14.622  12.328   8.016  1.00  9.59
ATOM   2479  CA  TYR A 335      14.868  13.243   6.902  1.00  8.35
ATOM   2480  C   TYR A 335      14.491  12.533   5.603  1.00  6.72
ATOM   2481  O   TYR A 335      13.776  13.078   4.759  1.00  7.47
ATOM   2482  CB  TYR A 335      16.349  13.659   6.878  1.00  7.39
ATOM   2483  CG  TYR A 335      16.817  14.262   5.562  1.00  7.96
ATOM   2484  CD1 TYR A 335      16.378  15.528   5.153  1.00  7.02
ATOM   2485  CD2 TYR A 335      17.700  13.570   4.728  1.00  6.69
ATOM   2486  CE1 TYR A 335      16.808  16.093   3.953  1.00  2.00
ATOM   2487  CE2 TYR A 335      18.137  14.124   3.511  1.00  5.92
ATOM   2488  CZ  TYR A 335      17.685  15.390   3.134  1.00  7.61
ATOM   2489  OH  TYR A 335      18.111  15.956   1.946  1.00  3.02
ATOM   2490  N   LEU A 336      14.950  11.294   5.467  1.00  9.05
ATOM   2491  CA  LEU A 336      14.658  10.498   4.280  1.00  7.17
ATOM   2492  C   LEU A 336      13.149  10.244   4.112  1.00  8.79
ATOM   2493  O   LEU A 336      12.637  10.211   2.993  1.00  9.38
ATOM   2494  CB  LEU A 336      15.441   9.185   4.326  1.00  5.64
ATOM   2495  CG  LEU A 336      16.977   9.291   4.301  1.00  5.35
ATOM   2496  CD1 LEU A 336      17.581   7.915   4.420  1.00  2.83
ATOM   2497  CD2 LEU A 336      17.463   9.983   3.025  1.00  4.46
ATOM   2498  N   ASP A 337      12.439  10.100   5.226  1.00  8.84
ATOM   2499  CA  ASP A 337      10.995   9.875   5.201  1.00  8.90
ATOM   2500  C   ASP A 337      10.208  11.180   5.101  1.00 10.26
ATOM   2501  O   ASP A 337       8.999  11.193   5.318  1.00  9.19
ATOM   2502  CB  ASP A 337      10.546   9.110   6.453  1.00 14.04
ATOM   2503  CG  ASP A 337      10.982   7.644   6.449  1.00 16.57
ATOM   2504  OD1 ASP A 337      11.570   7.169   5.449  1.00 17.62
ATOM   2505  OD2 ASP A 337      10.727   6.958   7.464  1.00 22.69
ATOM   2506  N   LYS A 338      10.900  12.278   4.796  1.00  8.39
ATOM   2507  CA  LYS A 338      10.266  13.586   4.666  1.00  9.89
ATOM   2508  C   LYS A 338       9.623  14.114   5.950  1.00  8.91
ATOM   2509  O   LYS A 338       8.643  14.848   5.888  1.00  8.70
ATOM   2510  CB  LYS A 338       9.199  13.561   3.564  1.00 13.38
ATOM   2511  CG  LYS A 338       9.702  13.448   2.139  1.00 19.25
ATOM   2512  CD  LYS A 338       8.506  13.408   1.195  1.00 27.16
ATOM   2513  CE  LYS A 338       8.916  13.357  -0.274  1.00 33.83
ATOM   2514  NZ  LYS A 338       7.710  13.248  -1.160  1.00 36.23
ATOM   2515  N   LYS A 339      10.158  13.761   7.114  1.00 10.45
ATOM   2516  CA  LYS A 339       9.578  14.243   8.372  1.00 10.42
ATOM   2517  C   LYS A 339      10.322  15.444   8.963  1.00  8.42
ATOM   2518  O   LYS A 339       9.773  16.180   9.788  1.00  8.97
ATOM   2519  CB  LYS A 339       9.508  13.115   9.403  1.00 10.58
ATOM   2520  CG  LYS A 339       8.592  11.960   9.039  1.00 11.12
ATOM   2521  CD  LYS A 339       8.852  10.776   9.979  1.00 15.76
ATOM   2522  CE  LYS A 339       8.063   9.526   9.567  1.00 19.79
ATOM   2523  NZ  LYS A 339       8.475   8.317  10.342  1.00 21.63
ATOM   2524  N   VAL A 340      11.570  15.634   8.547  1.00  7.26
ATOM   2525  CA  VAL A 340      12.400  16.738   9.027  1.00  9.83
ATOM   2526  C   VAL A 340      13.140  17.386   7.847  1.00  9.40
ATOM   2527  O   VAL A 340      13.435  16.715   6.859  1.00  9.04
ATOM   2528  CB  VAL A 340      13.427  16.236  10.104  1.00  9.66
ATOM   2529  CG1 VAL A 340      14.481  17.293  10.401  1.00 12.89
ATOM   2530  CG2 VAL A 340      12.708  15.888  11.393  1.00  8.44
ATOM   2531  N   LYS A 341      13.401  18.690   7.949  1.00  8.02
ATOM   2532  CA  LYS A 341      14.118  19.441   6.913  1.00  7.41
ATOM   2533  C   LYS A 341      15.605  19.579   7.248  1.00  4.90
ATOM   2534  O   LYS A 341      15.972  19.763   8.408  1.00  5.10
ATOM   2535  CB  LYS A 341      13.571  20.865   6.773  1.00  3.46
ATOM   2536  CG  LYS A 341      12.123  21.028   6.391  1.00  4.83
ATOM   2537  CD  LYS A 341      11.813  22.531   6.390  1.00  9.90
ATOM   2538  CE  LYS A 341      10.366  22.832   6.078  1.00 12.12
ATOM   2539  NZ  LYS A 341      10.106  22.791   4.627  1.00 16.93
ATOM   2540  N   LEU A 342      16.441  19.578   6.215  1.00  5.07
ATOM   2541  CA  LEU A 342      17.885  19.732   6.371  1.00  3.16
ATOM   2542  C   LEU A 342      18.476  20.640   5.292  1.00  4.68
ATOM   2543  O   LEU A 342      19.266  21.541   5.582  1.00  6.92
ATOM   2544  CB  LEU A 342      18.597  18.378   6.337  1.00  2.21
ATOM   2545  CG  LEU A 342      18.484  17.412   7.522  1.00  3.45
ATOM   2546  CD1 LEU A 342      19.375  16.215   7.273  1.00  6.68
ATOM   2547  CD2 LEU A 342      18.900  18.088   8.806  1.00  4.76
ATOM   2548  N   ASP A 343      18.051  20.446   4.051  1.00  6.21
ATOM   2549  CA  ASP A 343      18.576  21.240   2.943  1.00  7.71
ATOM   2550  C   ASP A 343      18.417  22.750   3.123  1.00  6.92
ATOM   2551  O   ASP A 343      19.315  23.513   2.779  1.00  2.37
ATOM   2552  CB  ASP A 343      17.934  20.789   1.629  1.00 11.92
ATOM   2553  CG  ASP A 343      18.093  19.302   1.392  1.00 14.26
ATOM   2554  OD1 ASP A 343      19.222  18.864   1.099  1.00 20.00
ATOM   2555  OD2 ASP A 343      17.096  18.566   1.519  1.00 17.51
ATOM   2556  N   GLU A 344      17.318  23.158   3.757  1.00  7.13
ATOM   2557  CA  GLU A 344      17.009  24.569   3.980  1.00  4.08
ATOM   2558  C   GLU A 344      17.970  25.263   4.934  1.00  3.76
ATOM   2559  O   GLU A 344      17.920  26.476   5.091  1.00  4.10
ATOM   2560  CB  GLU A 344      15.576  24.728   4.489  1.00  7.00
ATOM   2561  CG  GLU A 344      14.505  24.390   3.462  1.00  4.37
ATOM   2562  CD  GLU A 344      14.099  22.920   3.422  1.00  4.58
ATOM   2563  OE1 GLU A 344      14.853  22.027   3.864  1.00  5.90
ATOM   2564  OE2 GLU A 344      12.990  22.662   2.932  1.00  6.18
ATOM   2565  N   PHE A 345      18.802  24.481   5.609  1.00  3.65
ATOM   2566  CA  PHE A 345      19.798  25.013   6.533  1.00  4.06
ATOM   2567  C   PHE A 345      21.071  25.445   5.786  1.00  4.44
ATOM   2568  O   PHE A 345      21.841  26.276   6.282  1.00  2.00
ATOM   2569  CB  PHE A 345      20.202  23.934   7.555  1.00  2.00
ATOM   2570  CG  PHE A 345      19.193  23.698   8.644  1.00  4.03
ATOM   2571  CD1 PHE A 345      19.152  24.525   9.763  1.00  2.99
ATOM   2572  CD2 PHE A 345      18.295  22.642   8.563  1.00  3.42
ATOM   2573  CE1 PHE A 345      18.228  24.297  10.783  1.00  2.74
ATOM   2574  CE2 PHE A 345      17.370  22.408   9.575  1.00  6.90
ATOM   2575  CZ  PHE A 345      17.336  23.239  10.689  1.00  3.96
ATOM   2576  N   ILE A 346      21.305  24.841   4.620  1.00  3.74
ATOM   2577  CA  ILE A 346      22.515  25.086   3.824  1.00  2.92
ATOM   2578  C   ILE A 346      22.370  26.246   2.850  1.00  4.31
ATOM   2579  O   ILE A 346      21.707  26.126   1.822  1.00  5.82
ATOM   2580  CB  ILE A 346      22.919  23.794   3.061  1.00  4.46
ATOM   2581  CG1 ILE A 346      23.113  22.653   4.069  1.00  2.03
ATOM   2582  CG2 ILE A 346      24.206  24.014   2.242  1.00  2.14
ATOM   2583  CD1 ILE A 346      23.044  21.267   3.483  1.00  2.00
ATOM   2584  N   THR A 347      22.983  27.376   3.183  1.00  4.52
ATOM   2585  CA  THR A 347      22.902  28.553   2.329  1.00  4.47
ATOM   2586  C   THR A 347      24.125  28.717   1.419  1.00  5.38
ATOM   2587  O   THR A 347      24.024  29.311   0.343  1.00  2.00
ATOM   2588  CB  THR A 347      22.686  29.823   3.162  1.00  3.82
ATOM   2589  OG1 THR A 347      23.723  29.941   4.145  1.00  5.33
ATOM   2590  CG2 THR A 347      21.343  29.771   3.860  1.00  2.00
ATOM   2591  N   HIS A 348      25.278  28.228   1.880  1.00  5.84
ATOM   2592  CA  HIS A 348      26.531  28.301   1.124  1.00  5.17
ATOM   2593  C   HIS A 348      27.249  26.936   1.055  1.00  6.43
ATOM   2594  O   HIS A 348      27.171  26.123   1.993  1.00  3.69
ATOM   2595  CB  HIS A 348      27.510  29.296   1.772  1.00  5.57
ATOM   2596  CG  HIS A 348      27.029  30.717   1.811  1.00  6.94
ATOM   2597  ND1 HIS A 348      25.945  31.125   2.559  1.00  7.43
ATOM   2598  CD2 HIS A 348      27.534  31.841   1.244  1.00  2.00
ATOM   2599  CE1 HIS A 348      25.802  32.434   2.456  1.00  2.36
ATOM   2600  NE2 HIS A 348      26.755  32.893   1.662  1.00  2.00
ATOM   2601  N   ARG A 349      27.978  26.720  -0.041  1.00  4.21
ATOM   2602  CA  ARG A 349      28.781  25.510  -0.263  1.00  2.52
ATOM   2603  C   ARG A 349      30.082  25.997  -0.915  1.00  5.20
ATOM   2604  O   ARG A 349      30.052  26.877  -1.787  1.00  2.00
ATOM   2605  CB  ARG A 349      28.064  24.507  -1.181  1.00  4.49
ATOM   2606  CG  ARG A 349      26.850  23.791  -0.563  1.00  2.00
ATOM   2607  CD  ARG A 349      26.443  22.575  -1.400  1.00  4.89
ATOM   2608  NE  ARG A 349      25.327  21.799  -0.839  1.00  6.23
ATOM   2609  CZ  ARG A 349      25.429  20.882   0.127  1.00  7.45
ATOM   2610  NH1 ARG A 349      26.605  20.594   0.680  1.00  2.60
ATOM   2611  NH2 ARG A 349      24.341  20.228   0.534  1.00  3.36
ATOM   2612  N   MET A 350      31.219  25.497  -0.440  1.00  2.00
ATOM   2613  CA  MET A 350      32.509  25.904  -0.983  1.00  4.80
ATOM   2614  C   MET A 350      33.598  24.917  -0.578  1.00  6.10
ATOM   2615  O   MET A 350      33.409  24.125   0.349  1.00  6.72
ATOM   2616  CB  MET A 350      32.866  27.335  -0.542  1.00  5.04
ATOM   2617  CG  MET A 350      33.040  27.545   0.965  1.00  5.75
ATOM   2618  SD  MET A 350      33.154  29.307   1.377  1.00  2.04
ATOM   2619  CE  MET A 350      31.435  29.800   1.252  1.00  2.00
ATOM   2620  N   PRO A 351      34.719  24.891  -1.323  1.00  5.62
ATOM   2621  CA  PRO A 351      35.829  23.978  -1.021  1.00  3.57
ATOM   2622  C   PRO A 351      36.517  24.261   0.316  1.00  2.78
ATOM   2623  O   PRO A 351      36.427  25.364   0.856  1.00  3.35
ATOM   2624  CB  PRO A 351      36.802  24.224  -2.187  1.00  4.96
ATOM   2625  CG  PRO A 351      35.907  24.659  -3.301  1.00  2.36
ATOM   2626  CD  PRO A 351      34.950  25.584  -2.602  1.00  2.11
ATOM   2627  N   LEU A 352      37.259  23.272   0.804  1.00  3.44
ATOM   2628  CA  LEU A 352      38.004  23.386   2.053  1.00  4.21
ATOM   2629  C   LEU A 352      38.979  24.564   2.020  1.00  5.78
ATOM   2630  O   LEU A 352      39.201  25.227   3.034  1.00  6.68
ATOM   2631  CB  LEU A 352      38.778  22.092   2.313  1.00  6.01
ATOM   2632  CG  LEU A 352      39.628  22.036   3.583  1.00 10.67
ATOM   2633  CD1 LEU A 352      38.713  22.009   4.820  1.00  7.11
ATOM   2634  CD2 LEU A 352      40.532  20.810   3.537  1.00  7.31
ATOM   2635  N   GLU A 353      39.582  24.809   0.860  1.00  3.56
ATOM   2636  CA  GLU A 353      40.533  25.919   0.715  1.00  3.32
ATOM   2637  C   GLU A 353      39.937  27.271   1.086  1.00  2.02
ATOM   2638  O   GLU A 353      40.674  28.188   1.457  1.00  2.94
ATOM   2639  CB  GLU A 353      41.090  25.988  -0.714  1.00  3.41
ATOM   2640  CG  GLU A 353      42.159  24.940  -1.035  1.00  5.98
ATOM   2641  CD  GLU A 353      41.627  23.514  -1.185  1.00  7.60
ATOM   2642  OE1 GLU A 353      40.425  23.321  -1.477  1.00  5.39
ATOM   2643  OE2 GLU A 353      42.439  22.574  -1.034  1.00  8.85
ATOM   2644  N   SER A 354      38.608  27.376   1.022  1.00  5.51
ATOM   2645  CA  SER A 354      37.891  28.612   1.344  1.00  7.35
ATOM   2646  C   SER A 354      37.404  28.659   2.795  1.00  8.97
ATOM   2647  O   SER A 354      36.531  29.463   3.132  1.00 11.28
ATOM   2648  CB  SER A 354      36.686  28.773   0.408  1.00  9.99
ATOM   2649  OG  SER A 354      37.073  28.828  -0.960  1.00 13.44
ATOM   2650  N   VAL A 355      37.981  27.824   3.656  1.00  9.15
ATOM   2651  CA  VAL A 355      37.585  27.769   5.059  1.00  8.53
ATOM   2652  C   VAL A 355      37.502  29.129   5.764  1.00  8.10
ATOM   2653  O   VAL A 355      36.504  29.425   6.420  1.00 10.48
ATOM   2654  CB  VAL A 355      38.475  26.776   5.878  1.00  8.27
ATOM   2655  CG1 VAL A 355      39.913  27.278   5.998  1.00 12.34
ATOM   2656  CG2 VAL A 355      37.862  26.533   7.253  1.00  7.81
ATOM   2657  N   ASN A 356      38.512  29.970   5.582  1.00 10.67
ATOM   2658  CA  ASN A 356      38.549  31.296   6.210  1.00  8.93
ATOM   2659  C   ASN A 356      37.414  32.210   5.723  1.00  7.62
ATOM   2660  O   ASN A 356      37.001  33.137   6.430  1.00 10.02
ATOM   2661  CB  ASN A 356      39.922  31.963   6.008  1.00  7.86
ATOM   2662  CG  ASN A 356      41.054  31.252   6.765  1.00  8.89
ATOM   2663  OD1 ASN A 356      41.007  31.095   7.987  1.00  6.75
ATOM   2664  ND2 ASN A 356      42.090  30.852   6.040  1.00  5.31
ATOM   2665  N   ASP A 357      36.890  31.940   4.533  1.00  8.08
ATOM   2666  CA  ASP A 357      35.779  32.730   4.002  1.00  6.22
ATOM   2667  C   ASP A 357      34.481  32.338   4.696  1.00  6.29
ATOM   2668  O   ASP A 357      33.640  33.194   4.977  1.00  7.85
ATOM   2669  CB  ASP A 357      35.617  32.530   2.497  1.00  8.32
ATOM   2670  CG  ASP A 357      36.791  33.081   1.700  1.00 13.17
ATOM   2671  OD1 ASP A 357      37.233  34.218   1.966  1.00 12.42
ATOM   2672  OD2 ASP A 357      37.274  32.370   0.801  1.00 16.22
ATOM   2673  N   ALA A 358      34.315  31.041   4.947  1.00  6.40
ATOM   2674  CA  ALA A 358      33.126  30.515   5.619  1.00  6.53
ATOM   2675  C   ALA A 358      33.091  31.021   7.052  1.00  6.39
ATOM   2676  O   ALA A 358      32.029  31.389   7.574  1.00  6.48
ATOM   2677  CB  ALA A 358      33.142  28.988   5.611  1.00  6.70
ATOM   2678  N   ILE A 359      34.257  31.002   7.690  1.00  3.89
ATOM   2679  CA  ILE A 359      34.395  31.466   9.061  1.00  4.84
ATOM   2680  C   ILE A 359      34.025  32.945   9.130  1.00  5.78
ATOM   2681  O   ILE A 359      33.258  33.355   9.992  1.00  9.55
ATOM   2682  CB  ILE A 359      35.834  31.236   9.584  1.00  4.27
ATOM   2683  CG1 ILE A 359      36.030  29.751   9.923  1.00  2.26
ATOM   2684  CG2 ILE A 359      36.123  32.125  10.809  1.00  2.00
ATOM   2685  CD1 ILE A 359      37.442  29.390  10.356  1.00  3.41
ATOM   2686  N   ASP A 360      34.500  33.718   8.160  1.00  7.27
ATOM   2687  CA  ASP A 360      34.219  35.146   8.097  1.00  8.68
ATOM   2688  C   ASP A 360      32.720  35.407   7.934  1.00 11.29
ATOM   2689  O   ASP A 360      32.176  36.338   8.547  1.00  9.53
ATOM   2690  CB  ASP A 360      35.002  35.782   6.946  1.00 13.10
ATOM   2691  CG  ASP A 360      35.244  37.260   7.156  1.00 15.35
ATOM   2692  OD1 ASP A 360      36.156  37.612   7.941  1.00 16.94
ATOM   2693  OD2 ASP A 360      34.516  38.068   6.541  1.00 19.28
ATOM   2694  N   LEU A 361      32.053  34.590   7.117  1.00  9.15
ATOM   2695  CA  LEU A 361      30.612  34.734   6.912  1.00  7.90
ATOM   2696  C   LEU A 361      29.903  34.549   8.247  1.00  9.37
ATOM   2697  O   LEU A 361      29.059  35.364   8.624  1.00  9.27
ATOM   2698  CB  LEU A 361      30.080  33.699   5.924  1.00  3.25
ATOM   2699  CG  LEU A 361      30.404  33.839   4.440  1.00  5.97
ATOM   2700  CD1 LEU A 361      29.747  32.686   3.714  1.00  3.66
ATOM   2701  CD2 LEU A 361      29.874  35.177   3.894  1.00  4.70
ATOM   2702  N   MET A 362      30.255  33.477   8.955  1.00  9.91
ATOM   2703  CA  MET A 362      29.666  33.176  10.258  1.00 12.38
ATOM   2704  C   MET A 362      29.915  34.320  11.245  1.00 13.55
ATOM   2705  O   MET A 362      29.010  34.740  11.970  1.00 13.67
ATOM   2706  CB  MET A 362      30.260  31.879  10.810  1.00 11.91
ATOM   2707  CG  MET A 362      29.688  30.604  10.201  1.00  8.62
ATOM   2708  SD  MET A 362      28.097  30.165  10.943  1.00  8.25
ATOM   2709  CE  MET A 362      28.650  29.613  12.555  1.00  7.12
ATOM   2710  N   LYS A 363      31.136  34.851  11.213  1.00 15.05
ATOM   2711  CA  LYS A 363      31.565  35.941  12.084  1.00 14.80
ATOM   2712  C   LYS A 363      30.665  37.161  11.924  1.00 14.65
ATOM   2713  O   LYS A 363      30.468  37.933  12.867  1.00 14.62
ATOM   2714  CB  LYS A 363      33.012  36.310  11.747  1.00 17.87
ATOM   2715  CG  LYS A 363      33.688  37.267  12.705  1.00 21.67
ATOM   2716  CD  LYS A 363      34.877  36.592  13.386  1.00 25.84
ATOM   2717  CE  LYS A 363      35.772  37.609  14.084  1.00 27.18
ATOM   2718  NZ  LYS A 363      36.848  36.969  14.895  1.00 30.28
ATOM   2719  N   HIS A 364      30.100  37.322  10.732  1.00 13.39
ATOM   2720  CA  HIS A 364      29.233  38.460  10.452  1.00 13.47
ATOM   2721  C   HIS A 364      27.761  38.108  10.243  1.00 13.19
ATOM   2722  O   HIS A 364      27.001  38.905   9.694  1.00 12.32
ATOM   2723  CB  HIS A 364      29.789  39.250   9.268  1.00 11.04
ATOM   2724  CG  HIS A 364      31.152  39.810   9.521  1.00 10.67
ATOM   2725  ND1 HIS A 364      31.415  40.678  10.564  1.00 10.95
ATOM   2726  CD2 HIS A 364      32.343  39.580   8.923  1.00  9.51
ATOM   2727  CE1 HIS A 364      32.704  40.947  10.598  1.00  7.68
ATOM   2728  NE2 HIS A 364      33.293  40.293   9.613  1.00  5.21
ATOM   2729  N   GLY A 365      27.363  36.929  10.718  1.00 13.29
ATOM   2730  CA  GLY A 365      25.988  36.478  10.589  1.00 12.11
ATOM   2731  C   GLY A 365      25.458  36.548   9.171  1.00 12.84
ATOM   2732  O   GLY A 365      24.263  36.783   8.956  1.00 13.30
ATOM   2733  N   LYS A 366      26.343  36.325   8.205  1.00 10.19
ATOM   2734  CA  LYS A 366      25.984  36.379   6.793  1.00 10.98
ATOM   2735  C   LYS A 366      25.665  35.012   6.187  1.00  9.72
ATOM   2736  O   LYS A 366      25.800  34.822   4.979  1.00 11.44
ATOM   2737  CB  LYS A 366      27.110  37.063   6.012  1.00  9.58
ATOM   2738  CG  LYS A 366      27.267  38.544   6.337  1.00 13.86
ATOM   2739  CD  LYS A 366      26.298  39.399   5.530  1.00 16.37
ATOM   2740  CE  LYS A 366      26.046  40.743   6.197  1.00 20.59
ATOM   2741  NZ  LYS A 366      25.003  40.648   7.271  1.00 25.46
ATOM   2742  N   CYS A 367      25.196  34.077   7.012  1.00 10.82
ATOM   2743  CA  CYS A 367      24.867  32.733   6.543  1.00 10.15
ATOM   2744  C   CYS A 367      24.203  31.912   7.640  1.00 11.35
ATOM   2745  O   CYS A 367      24.320  32.250   8.812  1.00 11.85
ATOM   2746  CB  CYS A 367      26.149  31.997   6.141  1.00 10.47
ATOM   2747  SG  CYS A 367      27.096  31.280   7.535  1.00 10.60
ATOM   2748  N   ILE A 368      23.467  30.869   7.254  1.00  8.84
ATOM   2749  CA  ILE A 368      22.885  29.959   8.234  1.00  7.39
ATOM   2750  C   ILE A 368      24.038  28.948   8.362  1.00  7.48
ATOM   2751  O   ILE A 368      24.888  29.092   9.238  1.00  7.30
ATOM   2752  CB  ILE A 368      21.571  29.303   7.736  1.00  6.28
ATOM   2753  CG1 ILE A 368      20.504  30.378   7.507  1.00  7.03
ATOM   2754  CG2 ILE A 368      21.050  28.303   8.756  1.00  4.87
ATOM   2755  CD1 ILE A 368      20.334  31.327   8.667  1.00 10.81
ATOM   2756  N   ARG A 369      24.124  27.984   7.448  1.00  7.44
ATOM   2757  CA  ARG A 369      25.239  27.035   7.463  1.00  6.63
ATOM   2758  C   ARG A 369      25.973  26.990   6.124  1.00  6.20
ATOM   2759  O   ARG A 369      25.352  27.021   5.056  1.00  5.96
ATOM   2760  CB  ARG A 369      24.778  25.613   7.798  1.00  5.20
ATOM   2761  CG  ARG A 369      24.622  25.295   9.272  1.00  5.02
ATOM   2762  CD  ARG A 369      25.900  25.510  10.061  1.00  6.37
ATOM   2763  NE  ARG A 369      25.891  24.753  11.316  1.00  6.01
ATOM   2764  CZ  ARG A 369      25.813  25.286  12.538  1.00  6.40
ATOM   2765  NH1 ARG A 369      25.719  26.598  12.711  1.00  2.31
ATOM   2766  NH2 ARG A 369      25.916  24.500  13.603  1.00  6.90
ATOM   2767  N   THR A 370      27.299  26.964   6.195  1.00  5.84
ATOM   2768  CA  THR A 370      28.165  26.844   5.021  1.00  3.69
ATOM   2769  C   THR A 370      28.679  25.405   5.148  1.00  4.90
ATOM   2770  O   THR A 370      29.100  24.981   6.243  1.00  2.86
ATOM   2771  CB  THR A 370      29.381  27.830   5.064  1.00  4.04
ATOM   2772  OG1 THR A 370      28.950  29.166   4.760  1.00  4.16
ATOM   2773  CG2 THR A 370      30.436  27.426   4.052  1.00  4.87
ATOM   2774  N   VAL A 371      28.569  24.637   4.068  1.00  2.00
ATOM   2775  CA  VAL A 371      29.025  23.248   4.057  1.00  2.42
ATOM   2776  C   VAL A 371      30.173  23.091   3.053  1.00  5.35
ATOM   2777  O   VAL A 371      30.023  23.410   1.861  1.00  2.00
ATOM   2778  CB  VAL A 371      27.869  22.270   3.711  1.00  3.84
ATOM   2779  CG1 VAL A 371      28.402  20.865   3.560  1.00  2.00
ATOM   2780  CG2 VAL A 371      26.810  22.296   4.815  1.00  4.95
ATOM   2781  N   LEU A 372      31.307  22.599   3.560  1.00  3.34
ATOM   2782  CA  LEU A 372      32.540  22.401   2.796  1.00  3.34
ATOM   2783  C   LEU A 372      32.712  21.042   2.121  1.00  4.76
ATOM   2784  O   LEU A 372      32.314  20.007   2.675  1.00  5.01
ATOM   2785  CB  LEU A 372      33.746  22.593   3.734  1.00  4.51
ATOM   2786  CG  LEU A 372      34.341  23.952   4.094  1.00  5.22
ATOM   2787  CD1 LEU A 372      33.332  25.048   3.951  1.00  2.00
ATOM   2788  CD2 LEU A 372      34.928  23.915   5.507  1.00  2.00
ATOM   2789  N   SER A 373      33.315  21.056   0.929  1.00  3.99
ATOM   2790  CA  SER A 373      33.634  19.833   0.202  1.00  3.44
ATOM   2791  C   SER A 373      35.135  19.611   0.476  1.00  2.29
ATOM   2792  O   SER A 373      35.840  20.554   0.852  1.00  2.00
ATOM   2793  CB  SER A 373      33.348  19.999  -1.295  1.00  3.88
ATOM   2794  OG  SER A 373      33.985  21.153  -1.831  1.00  5.83
ATOM   2795  N   LEU A 374      35.629  18.384   0.319  1.00  3.77
ATOM   2796  CA  LEU A 374      37.037  18.090   0.592  1.00  7.41
ATOM   2797  C   LEU A 374      37.684  17.233  -0.509  1.00 10.40
ATOM   2798  O   LEU A 374      38.589  16.430  -0.192  1.00  8.12
ATOM   2799  CB  LEU A 374      37.189  17.396   1.965  1.00  8.16
ATOM   2800  CG  LEU A 374      36.591  18.002   3.250  1.00  8.01
ATOM   2801  CD1 LEU A 374      35.079  17.753   3.347  1.00  4.19
ATOM   2802  CD2 LEU A 374      37.274  17.382   4.446  1.00  9.26
ATOM   2803  OXT LEU A 374      37.297  17.388  -1.689  1.00 10.53
HETATM 2805 AP   NAD A 375      25.237  31.644  14.920  1.00  7.45
HETATM 2806 AO1  NAD A 375      26.309  32.603  15.279  1.00  2.79
HETATM 2807 AO2  NAD A 375      25.105  31.097  13.552  1.00  6.63
HETATM 2808 AO5* NAD A 375      23.814  32.286  15.358  1.00  7.53
HETATM 2809 AC5* NAD A 375      23.748  33.158  16.493  1.00  2.00
HETATM 2810 AC4* NAD A 375      22.506  33.964  16.257  1.00  4.49
HETATM 2811 AO4* NAD A 375      22.199  34.587  17.508  1.00  7.98
HETATM 2812 AC3* NAD A 375      22.730  35.064  15.221  1.00  4.80
HETATM 2813 AO3* NAD A 375      21.710  35.135  14.207  1.00  3.85
HETATM 2814 AC2* NAD A 375      22.761  36.335  16.062  1.00  7.57
HETATM 2815 AO2* NAD A 375      22.300  37.461  15.287  1.00  5.93
HETATM 2816 AC1* NAD A 375      21.857  35.942  17.211  1.00  7.24
HETATM 2817 AN9  NAD A 375      21.943  36.877  18.354  1.00  8.72
HETATM 2818 AC8  NAD A 375      23.050  37.446  18.873  1.00  6.93
HETATM 2819 AN7  NAD A 375      22.728  38.227  19.910  1.00  7.10
HETATM 2820 AC5  NAD A 375      21.409  38.110  19.991  1.00  6.40
HETATM 2821 AC6  NAD A 375      20.615  38.757  20.917  1.00  7.20
HETATM 2822 AN6  NAD A 375      21.154  39.562  21.831  1.00  9.33
HETATM 2823 AN1  NAD A 375      19.291  38.518  20.826  1.00  8.59
HETATM 2824 AC2  NAD A 375      18.769  37.705  19.908  1.00  4.71
HETATM 2825 AN3  NAD A 375      19.543  37.083  19.016  1.00  7.23
HETATM 2826 AC4  NAD A 375      20.881  37.277  19.042  1.00  6.17
HETATM 2827  O3  NAD A 375      25.432  30.420  15.955  1.00  7.31
HETATM 2828 NP   NAD A 375      25.166  28.845  15.960  1.00  9.71
HETATM 2829 NO1  NAD A 375      26.267  28.230  15.177  1.00  6.53
HETATM 2830 NO2  NAD A 375      23.730  28.631  15.609  1.00  8.65
HETATM 2831 NO5* NAD A 375      25.355  28.454  17.502  1.00  9.29
HETATM 2832 NC5* NAD A 375      24.807  29.306  18.511  1.00  4.17
HETATM 2833 NC4* NAD A 375      25.352  28.943  19.885  1.00  3.29
HETATM 2834 NO4* NAD A 375      25.251  27.519  20.060  1.00  3.46
HETATM 2835 NC3* NAD A 375      26.811  29.198  20.089  1.00  4.54
HETATM 2836 NO3* NAD A 375      27.083  29.803  21.361  1.00  4.01
HETATM 2837 NC2* NAD A 375      27.433  27.805  20.004  1.00  5.83
HETATM 2838 NO2* NAD A 375      28.720  27.873  20.615  1.00  7.50
HETATM 2839 NC1* NAD A 375      26.419  26.967  20.722  1.00  3.32
HETATM 2840 NN1  NAD A 375      26.316  25.498  20.496  1.00  6.94
HETATM 2841 NC2  NAD A 375      26.123  24.604  21.593  1.00  5.33
HETATM 2842 NC3  NAD A 375      25.904  23.234  21.394  1.00  4.48
HETATM 2843 NC7  NAD A 375      25.505  22.253  22.528  1.00  6.87
HETATM 2844 NO7  NAD A 375      25.664  21.038  22.392  1.00  2.32
HETATM 2845 NN7  NAD A 375      24.956  22.784  23.633  1.00  4.40
HETATM 2846 NC4  NAD A 375      25.906  22.762  20.064  1.00  8.43
HETATM 2847 NC5  NAD A 375      26.102  23.616  18.967  1.00  7.34
HETATM 2848 NC6  NAD A 375      26.303  24.987  19.174  1.00  3.47
HETATM 2849 ZN    ZN A 376      28.662  22.734  17.156  1.00  9.10
HETATM 2850 ZN    ZN A 377      29.097   5.720  28.841  1.00  9.91
CONECT  345  344 2849
CONECT  526  524  525 2849
CONECT  789  788 2850
CONECT  850  849 2850
CONECT 1328 1327 2849
CONECT 2805 2806 2807 2808 2827
CONECT 2806 2805
CONECT 2807 2805
CONECT 2808 2805 2809
CONECT 2809 2808 2810
CONECT 2810 2809 2811 2812
CONECT 2811 2810 2816
CONECT 2812 2810 2813 2814
CONECT 2813 2812
CONECT 2814 2812 2815 2816
CONECT 2815 2814
CONECT 2816 2811 2814 2817
CONECT 2817 2816 2818 2826
CONECT 2818 2817 2819
CONECT 2819 2818 2820
CONECT 2820 2819 2821 2826
CONECT 2821 2820 2822 2823
CONECT 2822 2821
CONECT 2823 2821 2824
CONECT 2824 2823 2825
CONECT 2825 2824 2826
CONECT 2826 2817 2820 2825
CONECT 2827 2805 2828
CONECT 2828 2827 2829 2830 2831
CONECT 2829 2828
CONECT 2830 2828
CONECT 2831 2828 2832
CONECT 2832 2831 2833
CONECT 2833 2832 2834 2835
CONECT 2834 2833 2839
CONECT 2835 2833 2836 2837
CONECT 2836 2835
CONECT 2837 2835 2838 2839
CONECT 2838 2837
CONECT 2839 2834 2837 2840
CONECT 2840 2839 2841 2848
CONECT 2841 2840 2842
CONECT 2842 2841 2843 2846
CONECT 2843 2842 2844 2845
CONECT 2844 2843
CONECT 2845 2843
CONECT 2846 2842 2847
CONECT 2847 2846 2848
CONECT 2848 2840 2847
CONECT 2849  345  526 1328
CONECT 2850  789  850
CONECT 3376 3374 3375 5699
CONECT 3639 3638 5700
CONECT 3700 3699 5700
CONECT 4178 4177 5699
CONECT 5655 5656 5657 5658 5677
CONECT 5656 5655
CONECT 5657 5655
CONECT 5658 5655 5659
CONECT 5659 5658 5660
CONECT 5660 5659 5661 5662
CONECT 5661 5660 5666
CONECT 5662 5660 5663 5664
CONECT 5663 5662
CONECT 5664 5662 5665 5666
CONECT 5665 5664
CONECT 5666 5661 5664 5667
CONECT 5667 5666 5668 5676
CONECT 5668 5667 5669
CONECT 5669 5668 5670
CONECT 5670 5669 5671 5676
CONECT 5671 5670 5672 5673
CONECT 5672 5671
CONECT 5673 5671 5674
CONECT 5674 5673 5675
CONECT 5675 5674 5676
CONECT 5676 5667 5670 5675
CONECT 5677 5655 5678
CONECT 5678 5677 5679 5680 5681
CONECT 5679 5678
CONECT 5680 5678
CONECT 5681 5678 5682
CONECT 5682 5681 5683
CONECT 5683 5682 5684 5685
CONECT 5684 5683 5689
CONECT 5685 5683 5686 5687
CONECT 5686 5685
CONECT 5687 5685 5688 5689
CONECT 5688 5687
CONECT 5689 5684 5687 5690
CONECT 5690 5689 5691 5698
CONECT 5691 5690 5692
CONECT 5692 5691 5693 5696
CONECT 5693 5692 5694 5695
CONECT 5694 5693
CONECT 5695 5693
CONECT 5696 5692 5697
CONECT 5697 5696 5698
CONECT 5698 5690 5697
CONECT 5699 3376 4178
CONECT 5700 3639 3700
END
