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PDBsum entry 4ai6

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Top Page protein ligands metals links
Motor protein PDB id
4ai6
Jmol
Contents
Protein chains
2650 a.a.
Ligands
ATP ×2
ADP ×4
SO4 ×2
Metals
_MG ×2
HEADER    MOTOR PROTEIN                           08-FEB-12   4AI6
TITLE     DYNEIN MOTOR DOMAIN - ADP COMPLEX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE CLASS-MU 26 KDA ISOZYME, DYNEIN
COMPND   3  HEAVY CHAIN CYTOPLASMIC;
COMPND   4 CHAIN: A, B;
COMPND   5 FRAGMENT: RESIDUES 1-218,1364-3038,3292-4092;
COMPND   6 SYNONYM: GST 26, SJ26 ANTIGEN, SJGST, DYHC;
COMPND   7 EC: 2.5.1.18;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SCHISTOSOMA JAPONICUM, SACCHAROMYCES
SOURCE   3  CEREVISIAE;
SOURCE   4 ORGANISM_TAXID: 6182, 4932;
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS    MOTOR PROTEIN, AAA+ PROTEIN, ASCE PROTEIN, P-LOOP NTPASE,
KEYWDS   2 CYTOSKELETAL MOTOR, ATPASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.SCHMIDT,E.S.GLEAVE,A.P.CARTER
REVDAT   2   16-MAY-12 4AI6    1       JRNL
REVDAT   1   14-MAR-12 4AI6    0
JRNL        AUTH   H.SCHMIDT,E.S.GLEAVE,A.P.CARTER
JRNL        TITL   INSIGHTS INTO DYNEIN MOTOR DOMAIN FUNCTION FROM A 3.3
JRNL        TITL 2 ANGSTROM CRYSTAL STRUCTURE
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19   492 2012
JRNL        REFN                   ISSN 1545-9993
JRNL        PMID   22426545
JRNL        DOI    10.1038/NSMB.2272
REMARK   2
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.7.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.29
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 104357
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.24453
REMARK   3   R VALUE            (WORKING SET) : 0.24138
REMARK   3   FREE R VALUE                     : 0.30300
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.00
REMARK   3   FREE R VALUE TEST SET COUNT      : 5512
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.400
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.488
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7616
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3980
REMARK   3   BIN FREE R VALUE SET COUNT          : 407
REMARK   3   BIN FREE R VALUE                    : 0.4250
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 41496
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 182
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 184.69
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.46000
REMARK   3    B22 (A**2) : -6.32000
REMARK   3    B33 (A**2) : 6.78000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.87000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.663
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.608
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.967
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 42482 ; 0.010 ; 0.019
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 57532 ; 1.557 ; 1.965
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  5290 ; 6.067 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1874 ;44.278 ;24.674
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  7448 ;19.424 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   196 ;18.918 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  6580 ; 0.103 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 31524 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK   3  THE INPUT
REMARK   4
REMARK   4 4AI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-12.
REMARK 100 THE PDBE ID CODE IS EBI-51218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 4
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97925
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 109899
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.4
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.2
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 21.8
REMARK 200  R MERGE                    (I) : 0.120
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.70
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 21.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       59.58750
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     LYS A   217
REMARK 465     SER A   218
REMARK 465     ASP A   219
REMARK 465     GLU A  1364
REMARK 465     ILE A  2944
REMARK 465     VAL A  2945
REMARK 465     PRO A  2946
REMARK 465     GLU A  2947
REMARK 465     VAL A  2948
REMARK 465     ASN A  2949
REMARK 465     LYS A  2950
REMARK 465     GLU A  2951
REMARK 465     LEU A  2952
REMARK 465     VAL A  2953
REMARK 465     PHE A  2954
REMARK 465     THR A  2955
REMARK 465     GLU A  2956
REMARK 465     PRO A  2957
REMARK 465     ILE A  2958
REMARK 465     GLN A  2959
REMARK 465     LEU A  3029
REMARK 465     LYS A  3030
REMARK 465     VAL A  3031
REMARK 465     ASN A  3032
REMARK 465     GLU A  3033
REMARK 465     LEU A  3034
REMARK 465     ASN A  3035
REMARK 465     LYS A  3036
REMARK 465     THR A  3037
REMARK 465     LEU A  3038
REMARK 465     SER A  3292
REMARK 465     ILE A  3293
REMARK 465     SER A  3294
REMARK 465     LEU A  3295
REMARK 465     VAL A  3296
REMARK 465     LYS A  3659
REMARK 465     LYS A  3660
REMARK 465     SER A  3661
REMARK 465     ARG A  3662
REMARK 465     GLU A  3663
REMARK 465     THR A  3664
REMARK 465     ARG A  3665
REMARK 465     ALA A  3666
REMARK 465     ALA A  3667
REMARK 465     ARG A  3668
REMARK 465     LYS B   217
REMARK 465     SER B   218
REMARK 465     ASP B   219
REMARK 465     GLU B  1364
REMARK 465     ILE B  2944
REMARK 465     VAL B  2945
REMARK 465     PRO B  2946
REMARK 465     GLU B  2947
REMARK 465     VAL B  2948
REMARK 465     ASN B  2949
REMARK 465     LYS B  2950
REMARK 465     GLU B  2951
REMARK 465     LEU B  2952
REMARK 465     VAL B  2953
REMARK 465     PHE B  2954
REMARK 465     THR B  2955
REMARK 465     GLU B  2956
REMARK 465     PRO B  2957
REMARK 465     ILE B  2958
REMARK 465     GLN B  2959
REMARK 465     LEU B  3029
REMARK 465     LYS B  3030
REMARK 465     VAL B  3031
REMARK 465     ASN B  3032
REMARK 465     GLU B  3033
REMARK 465     LEU B  3034
REMARK 465     ASN B  3035
REMARK 465     LYS B  3036
REMARK 465     THR B  3037
REMARK 465     LEU B  3038
REMARK 465     SER B  3292
REMARK 465     ILE B  3293
REMARK 465     SER B  3294
REMARK 465     LEU B  3295
REMARK 465     VAL B  3296
REMARK 465     LYS B  3659
REMARK 465     LYS B  3660
REMARK 465     SER B  3661
REMARK 465     ARG B  3662
REMARK 465     GLU B  3663
REMARK 465     THR B  3664
REMARK 465     ARG B  3665
REMARK 465     ALA B  3666
REMARK 465     ALA B  3667
REMARK 465     ARG B  3668
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     SER A   1    OG
REMARK 470     PRO A   2    CG   CD
REMARK 470     ILE A   3    CG1  CG2  CD1
REMARK 470     LEU A   4    CG   CD1  CD2
REMARK 470     TYR A   6    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     TRP A   7    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP A   7    CH2
REMARK 470     LYS A   8    CG   CD   CE   NZ
REMARK 470     ILE A   9    CG1  CG2  CD1
REMARK 470     LYS A  10    CG   CD   CE   NZ
REMARK 470     LEU A  12    CG   CD1  CD2
REMARK 470     VAL A  13    CG1  CG2
REMARK 470     GLN A  14    CG   CD   OE1  NE2
REMARK 470     PRO A  15    CG   CD
REMARK 470     THR A  16    OG1  CG2
REMARK 470     ARG A  17    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A  18    CG   CD1  CD2
REMARK 470     LEU A  19    CG   CD1  CD2
REMARK 470     LEU A  20    CG   CD1  CD2
REMARK 470     GLU A  21    CG   CD   OE1  OE2
REMARK 470     TYR A  22    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LEU A  23    CG   CD1  CD2
REMARK 470     GLU A  24    CG   CD   OE1  OE2
REMARK 470     GLU A  25    CG   CD   OE1  OE2
REMARK 470     LYS A  26    CG   CD   CE   NZ
REMARK 470     TYR A  27    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU A  28    CG   CD   OE1  OE2
REMARK 470     GLU A  29    CG   CD   OE1  OE2
REMARK 470     HIS A  30    CG   ND1  CD2  CE1  NE2
REMARK 470     LEU A  31    CG   CD1  CD2
REMARK 470     TYR A  32    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU A  33    CG   CD   OE1  OE2
REMARK 470     ARG A  34    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A  35    CG   OD1  OD2
REMARK 470     GLU A  36    CG   CD   OE1  OE2
REMARK 470     ASP A  38    CG   OD1  OD2
REMARK 470     LYS A  39    CG   CD   CE   NZ
REMARK 470     TRP A  40    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP A  40    CH2
REMARK 470     ARG A  41    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASN A  42    CG   OD1  ND2
REMARK 470     LYS A  43    CG   CD   CE   NZ
REMARK 470     LYS A  44    CG   CD   CE   NZ
REMARK 470     PHE A  45    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU A  46    CG   CD   OE1  OE2
REMARK 470     LEU A  47    CG   CD1  CD2
REMARK 470     LEU A  49    CG   CD1  CD2
REMARK 470     GLU A  50    CG   CD   OE1  OE2
REMARK 470     PHE A  51    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     PRO A  52    CG   CD
REMARK 470     ASN A  53    CG   OD1  ND2
REMARK 470     LEU A  54    CG   CD1  CD2
REMARK 470     PRO A  55    CG   CD
REMARK 470     TYR A  56    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     TYR A  57    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ILE A  58    CG1  CG2  CD1
REMARK 470     ASP A  59    CG   OD1  OD2
REMARK 470     ASP A  61    CG   OD1  OD2
REMARK 470     VAL A  62    CG1  CG2
REMARK 470     LYS A  63    CG   CD   CE   NZ
REMARK 470     LEU A  64    CG   CD1  CD2
REMARK 470     THR A  65    OG1  CG2
REMARK 470     GLN A  66    CG   CD   OE1  NE2
REMARK 470     SER A  67    OG
REMARK 470     MET A  68    CG   SD   CE
REMARK 470     ILE A  70    CG1  CG2  CD1
REMARK 470     ILE A  71    CG1  CG2  CD1
REMARK 470     ARG A  72    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TYR A  73    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ILE A  74    CG1  CG2  CD1
REMARK 470     ASP A  76    CG   OD1  OD2
REMARK 470     LYS A  77    CG   CD   CE   NZ
REMARK 470     HIS A  78    CG   ND1  CD2  CE1  NE2
REMARK 470     ASN A  79    CG   OD1  ND2
REMARK 470     MET A  80    CG   SD   CE
REMARK 470     LEU A  81    CG   CD1  CD2
REMARK 470     CYS A  84    SG
REMARK 470     PRO A  85    CG   CD
REMARK 470     LYS A  86    CG   CD   CE   NZ
REMARK 470     GLU A  87    CG   CD   OE1  OE2
REMARK 470     ARG A  88    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A  90    CG   CD   OE1  OE2
REMARK 470     ILE A  91    CG1  CG2  CD1
REMARK 470     SER A  92    OG
REMARK 470     MET A  93    CG   SD   CE
REMARK 470     LEU A  94    CG   CD1  CD2
REMARK 470     GLU A  95    CG   CD   OE1  OE2
REMARK 470     VAL A  98    CG1  CG2
REMARK 470     LEU A  99    CG   CD1  CD2
REMARK 470     ASP A 100    CG   OD1  OD2
REMARK 470     ILE A 101    CG1  CG2  CD1
REMARK 470     ARG A 102    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TYR A 103    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     VAL A 105    CG1  CG2
REMARK 470     SER A 106    OG
REMARK 470     ARG A 107    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE A 108    CG1  CG2  CD1
REMARK 470     TYR A 110    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     SER A 111    OG
REMARK 470     LYS A 112    CG   CD   CE   NZ
REMARK 470     ASP A 113    CG   OD1  OD2
REMARK 470     PHE A 114    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU A 115    CG   CD   OE1  OE2
REMARK 470     THR A 116    OG1  CG2
REMARK 470     LEU A 117    CG   CD1  CD2
REMARK 470     LYS A 118    CG   CD   CE   NZ
REMARK 470     VAL A 119    CG1  CG2
REMARK 470     ASP A 120    CG   OD1  OD2
REMARK 470     PHE A 121    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LEU A 122    CG   CD1  CD2
REMARK 470     SER A 123    OG
REMARK 470     LYS A 124    CG   CD   CE   NZ
REMARK 470     LEU A 125    CG   CD1  CD2
REMARK 470     PRO A 126    CG   CD
REMARK 470     GLU A 127    CG   CD   OE1  OE2
REMARK 470     MET A 128    CG   SD   CE
REMARK 470     LEU A 129    CG   CD1  CD2
REMARK 470     LYS A 130    CG   CD   CE   NZ
REMARK 470     MET A 131    CG   SD   CE
REMARK 470     PHE A 132    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU A 133    CG   CD   OE1  OE2
REMARK 470     ASP A 134    CG   OD1  OD2
REMARK 470     ARG A 135    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A 136    CG   CD1  CD2
REMARK 470     CYS A 137    SG
REMARK 470     HIS A 138    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS A 139    CG   CD   CE   NZ
REMARK 470     THR A 140    OG1  CG2
REMARK 470     TYR A 141    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LEU A 142    CG   CD1  CD2
REMARK 470     ASN A 143    CG   OD1  ND2
REMARK 470     ASP A 145    CG   OD1  OD2
REMARK 470     HIS A 146    CG   ND1  CD2  CE1  NE2
REMARK 470     VAL A 147    CG1  CG2
REMARK 470     THR A 148    OG1  CG2
REMARK 470     HIS A 149    CG   ND1  CD2  CE1  NE2
REMARK 470     PRO A 150    CG   CD
REMARK 470     ASP A 151    CG   OD1  OD2
REMARK 470     PHE A 152    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     MET A 153    CG   SD   CE
REMARK 470     LEU A 154    CG   CD1  CD2
REMARK 470     TYR A 155    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ASP A 156    CG   OD1  OD2
REMARK 470     LEU A 158    CG   CD1  CD2
REMARK 470     ASP A 159    CG   OD1  OD2
REMARK 470     VAL A 160    CG1  CG2
REMARK 470     VAL A 161    CG1  CG2
REMARK 470     LEU A 162    CG   CD1  CD2
REMARK 470     TYR A 163    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     MET A 164    CG   SD   CE
REMARK 470     ASP A 165    CG   OD1  OD2
REMARK 470     PRO A 166    CG   CD
REMARK 470     MET A 167    CG   SD   CE
REMARK 470     CYS A 168    SG
REMARK 470     LEU A 169    CG   CD1  CD2
REMARK 470     ASP A 170    CG   OD1  OD2
REMARK 470     PHE A 172    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     PRO A 173    CG   CD
REMARK 470     LYS A 174    CG   CD   CE   NZ
REMARK 470     LEU A 175    CG   CD1  CD2
REMARK 470     VAL A 176    CG1  CG2
REMARK 470     CYS A 177    SG
REMARK 470     PHE A 178    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 179    CG   CD   CE   NZ
REMARK 470     LYS A 180    CG   CD   CE   NZ
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE A 182    CG1  CG2  CD1
REMARK 470     GLU A 183    CG   CD   OE1  OE2
REMARK 470     ILE A 185    CG1  CG2  CD1
REMARK 470     PRO A 186    CG   CD
REMARK 470     GLN A 187    CG   CD   OE1  NE2
REMARK 470     ILE A 188    CG1  CG2  CD1
REMARK 470     ASP A 189    CG   OD1  OD2
REMARK 470     LYS A 190    CG   CD   CE   NZ
REMARK 470     TYR A 191    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LEU A 192    CG   CD1  CD2
REMARK 470     LYS A 193    CG   CD   CE   NZ
REMARK 470     SER A 194    OG
REMARK 470     SER A 195    OG
REMARK 470     LYS A 196    CG   CD   CE   NZ
REMARK 470     TYR A 197    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ILE A 198    CG1  CG2  CD1
REMARK 470     TRP A 200    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP A 200    CH2
REMARK 470     PRO A 201    CG   CD
REMARK 470     LEU A 202    CG   CD1  CD2
REMARK 470     GLN A 203    CG   CD   OE1  NE2
REMARK 470     TRP A 205    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP A 205    CH2
REMARK 470     GLN A 206    CG   CD   OE1  NE2
REMARK 470     THR A 208    OG1  CG2
REMARK 470     PHE A 209    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ASP A 213    CG   OD1  OD2
REMARK 470     HIS A 214    CG   ND1  CD2  CE1  NE2
REMARK 470     PRO A 215    CG   CD
REMARK 470     PRO A 216    CG   CD
REMARK 470     SER B   1    OG
REMARK 470     PRO B   2    CG   CD
REMARK 470     ILE B   3    CG1  CG2  CD1
REMARK 470     LEU B   4    CG   CD1  CD2
REMARK 470     TYR B   6    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     TRP B   7    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP B   7    CH2
REMARK 470     LYS B   8    CG   CD   CE   NZ
REMARK 470     ILE B   9    CG1  CG2  CD1
REMARK 470     LYS B  10    CG   CD   CE   NZ
REMARK 470     LEU B  12    CG   CD1  CD2
REMARK 470     VAL B  13    CG1  CG2
REMARK 470     GLN B  14    CG   CD   OE1  NE2
REMARK 470     PRO B  15    CG   CD
REMARK 470     THR B  16    OG1  CG2
REMARK 470     ARG B  17    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU B  18    CG   CD1  CD2
REMARK 470     LEU B  19    CG   CD1  CD2
REMARK 470     LEU B  20    CG   CD1  CD2
REMARK 470     GLU B  21    CG   CD   OE1  OE2
REMARK 470     TYR B  22    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LEU B  23    CG   CD1  CD2
REMARK 470     GLU B  24    CG   CD   OE1  OE2
REMARK 470     GLU B  25    CG   CD   OE1  OE2
REMARK 470     LYS B  26    CG   CD   CE   NZ
REMARK 470     TYR B  27    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU B  28    CG   CD   OE1  OE2
REMARK 470     GLU B  29    CG   CD   OE1  OE2
REMARK 470     HIS B  30    CG   ND1  CD2  CE1  NE2
REMARK 470     LEU B  31    CG   CD1  CD2
REMARK 470     TYR B  32    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU B  33    CG   CD   OE1  OE2
REMARK 470     ARG B  34    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B  35    CG   OD1  OD2
REMARK 470     GLU B  36    CG   CD   OE1  OE2
REMARK 470     ASP B  38    CG   OD1  OD2
REMARK 470     LYS B  39    CG   CD   CE   NZ
REMARK 470     TRP B  40    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP B  40    CH2
REMARK 470     ARG B  41    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASN B  42    CG   OD1  ND2
REMARK 470     LYS B  43    CG   CD   CE   NZ
REMARK 470     LYS B  44    CG   CD   CE   NZ
REMARK 470     PHE B  45    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU B  46    CG   CD   OE1  OE2
REMARK 470     LEU B  47    CG   CD1  CD2
REMARK 470     LEU B  49    CG   CD1  CD2
REMARK 470     GLU B  50    CG   CD   OE1  OE2
REMARK 470     PHE B  51    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     PRO B  52    CG   CD
REMARK 470     ASN B  53    CG   OD1  ND2
REMARK 470     LEU B  54    CG   CD1  CD2
REMARK 470     PRO B  55    CG   CD
REMARK 470     TYR B  56    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     TYR B  57    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ILE B  58    CG1  CG2  CD1
REMARK 470     ASP B  59    CG   OD1  OD2
REMARK 470     ASP B  61    CG   OD1  OD2
REMARK 470     VAL B  62    CG1  CG2
REMARK 470     LYS B  63    CG   CD   CE   NZ
REMARK 470     LEU B  64    CG   CD1  CD2
REMARK 470     THR B  65    OG1  CG2
REMARK 470     GLN B  66    CG   CD   OE1  NE2
REMARK 470     SER B  67    OG
REMARK 470     MET B  68    CG   SD   CE
REMARK 470     ILE B  70    CG1  CG2  CD1
REMARK 470     ILE B  71    CG1  CG2  CD1
REMARK 470     ARG B  72    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TYR B  73    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ILE B  74    CG1  CG2  CD1
REMARK 470     ASP B  76    CG   OD1  OD2
REMARK 470     LYS B  77    CG   CD   CE   NZ
REMARK 470     HIS B  78    CG   ND1  CD2  CE1  NE2
REMARK 470     ASN B  79    CG   OD1  ND2
REMARK 470     MET B  80    CG   SD   CE
REMARK 470     LEU B  81    CG   CD1  CD2
REMARK 470     CYS B  84    SG
REMARK 470     PRO B  85    CG   CD
REMARK 470     LYS B  86    CG   CD   CE   NZ
REMARK 470     GLU B  87    CG   CD   OE1  OE2
REMARK 470     ARG B  88    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B  90    CG   CD   OE1  OE2
REMARK 470     ILE B  91    CG1  CG2  CD1
REMARK 470     SER B  92    OG
REMARK 470     MET B  93    CG   SD   CE
REMARK 470     LEU B  94    CG   CD1  CD2
REMARK 470     GLU B  95    CG   CD   OE1  OE2
REMARK 470     VAL B  98    CG1  CG2
REMARK 470     LEU B  99    CG   CD1  CD2
REMARK 470     ASP B 100    CG   OD1  OD2
REMARK 470     ILE B 101    CG1  CG2  CD1
REMARK 470     ARG B 102    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TYR B 103    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     VAL B 105    CG1  CG2
REMARK 470     SER B 106    OG
REMARK 470     ARG B 107    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE B 108    CG1  CG2  CD1
REMARK 470     TYR B 110    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     SER B 111    OG
REMARK 470     LYS B 112    CG   CD   CE   NZ
REMARK 470     ASP B 113    CG   OD1  OD2
REMARK 470     PHE B 114    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU B 115    CG   CD   OE1  OE2
REMARK 470     THR B 116    OG1  CG2
REMARK 470     LEU B 117    CG   CD1  CD2
REMARK 470     LYS B 118    CG   CD   CE   NZ
REMARK 470     VAL B 119    CG1  CG2
REMARK 470     ASP B 120    CG   OD1  OD2
REMARK 470     PHE B 121    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LEU B 122    CG   CD1  CD2
REMARK 470     SER B 123    OG
REMARK 470     LYS B 124    CG   CD   CE   NZ
REMARK 470     LEU B 125    CG   CD1  CD2
REMARK 470     PRO B 126    CG   CD
REMARK 470     GLU B 127    CG   CD   OE1  OE2
REMARK 470     MET B 128    CG   SD   CE
REMARK 470     LEU B 129    CG   CD1  CD2
REMARK 470     LYS B 130    CG   CD   CE   NZ
REMARK 470     MET B 131    CG   SD   CE
REMARK 470     PHE B 132    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU B 133    CG   CD   OE1  OE2
REMARK 470     ASP B 134    CG   OD1  OD2
REMARK 470     ARG B 135    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU B 136    CG   CD1  CD2
REMARK 470     CYS B 137    SG
REMARK 470     HIS B 138    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS B 139    CG   CD   CE   NZ
REMARK 470     THR B 140    OG1  CG2
REMARK 470     TYR B 141    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LEU B 142    CG   CD1  CD2
REMARK 470     ASN B 143    CG   OD1  ND2
REMARK 470     ASP B 145    CG   OD1  OD2
REMARK 470     HIS B 146    CG   ND1  CD2  CE1  NE2
REMARK 470     VAL B 147    CG1  CG2
REMARK 470     THR B 148    OG1  CG2
REMARK 470     HIS B 149    CG   ND1  CD2  CE1  NE2
REMARK 470     PRO B 150    CG   CD
REMARK 470     ASP B 151    CG   OD1  OD2
REMARK 470     PHE B 152    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     MET B 153    CG   SD   CE
REMARK 470     LEU B 154    CG   CD1  CD2
REMARK 470     TYR B 155    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ASP B 156    CG   OD1  OD2
REMARK 470     LEU B 158    CG   CD1  CD2
REMARK 470     ASP B 159    CG   OD1  OD2
REMARK 470     VAL B 160    CG1  CG2
REMARK 470     VAL B 161    CG1  CG2
REMARK 470     LEU B 162    CG   CD1  CD2
REMARK 470     TYR B 163    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     MET B 164    CG   SD   CE
REMARK 470     ASP B 165    CG   OD1  OD2
REMARK 470     PRO B 166    CG   CD
REMARK 470     MET B 167    CG   SD   CE
REMARK 470     CYS B 168    SG
REMARK 470     LEU B 169    CG   CD1  CD2
REMARK 470     ASP B 170    CG   OD1  OD2
REMARK 470     PHE B 172    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     PRO B 173    CG   CD
REMARK 470     LYS B 174    CG   CD   CE   NZ
REMARK 470     LEU B 175    CG   CD1  CD2
REMARK 470     VAL B 176    CG1  CG2
REMARK 470     CYS B 177    SG
REMARK 470     PHE B 178    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS B 179    CG   CD   CE   NZ
REMARK 470     LYS B 180    CG   CD   CE   NZ
REMARK 470     ARG B 181    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE B 182    CG1  CG2  CD1
REMARK 470     GLU B 183    CG   CD   OE1  OE2
REMARK 470     ILE B 185    CG1  CG2  CD1
REMARK 470     PRO B 186    CG   CD
REMARK 470     GLN B 187    CG   CD   OE1  NE2
REMARK 470     ILE B 188    CG1  CG2  CD1
REMARK 470     ASP B 189    CG   OD1  OD2
REMARK 470     LYS B 190    CG   CD   CE   NZ
REMARK 470     TYR B 191    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LEU B 192    CG   CD1  CD2
REMARK 470     LYS B 193    CG   CD   CE   NZ
REMARK 470     SER B 194    OG
REMARK 470     SER B 195    OG
REMARK 470     LYS B 196    CG   CD   CE   NZ
REMARK 470     TYR B 197    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ILE B 198    CG1  CG2  CD1
REMARK 470     TRP B 200    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP B 200    CH2
REMARK 470     PRO B 201    CG   CD
REMARK 470     LEU B 202    CG   CD1  CD2
REMARK 470     GLN B 203    CG   CD   OE1  NE2
REMARK 470     TRP B 205    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP B 205    CH2
REMARK 470     GLN B 206    CG   CD   OE1  NE2
REMARK 470     THR B 208    OG1  CG2
REMARK 470     PHE B 209    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ASP B 213    CG   OD1  OD2
REMARK 470     HIS B 214    CG   ND1  CD2  CE1  NE2
REMARK 470     PRO B 215    CG   CD
REMARK 470     PRO B 216    CG   CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    PRO A   2   C   -  N   -  CA  ANGL. DEV. =  14.2 DEGREES
REMARK 500    PRO A 201   C   -  N   -  CA  ANGL. DEV. =  19.2 DEGREES
REMARK 500    PRO A 216   C   -  N   -  CA  ANGL. DEV. =  12.9 DEGREES
REMARK 500    LEU A1463   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES
REMARK 500    LEU A1882   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES
REMARK 500    PRO A2028   C   -  N   -  CD  ANGL. DEV. = -13.6 DEGREES
REMARK 500    LEU A3650   CB  -  CG  -  CD1 ANGL. DEV. = -12.0 DEGREES
REMARK 500    LEU A3945   CB  -  CG  -  CD2 ANGL. DEV. = -11.0 DEGREES
REMARK 500    PRO B   2   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES
REMARK 500    PRO B 201   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES
REMARK 500    PRO B2028   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES
REMARK 500    LEU B2455   CB  -  CG  -  CD1 ANGL. DEV. = -13.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A  24       17.05     41.38
REMARK 500    GLU A  33     -177.42    -64.71
REMARK 500    ASN A  53      168.73    175.81
REMARK 500    ASP A  59     -105.92   -139.49
REMARK 500    GLN A  66      107.53     88.40
REMARK 500    ASN A  79       70.45     42.64
REMARK 500    GLU A 115       -8.25    -49.45
REMARK 500    PHE A 178      -35.21    -38.53
REMARK 500    PRO A 201      173.71    -46.72
REMARK 500    PRO A 215      174.12    -58.98
REMARK 500    PRO A1535        2.75    -60.77
REMARK 500    HIS A1555      -52.92     71.74
REMARK 500    PHE A1566      -50.37   -120.60
REMARK 500    GLU A1576      -58.77     78.96
REMARK 500    ASN A1738       37.24    -99.77
REMARK 500    ASP A1739      -31.95   -132.96
REMARK 500    LEU A1741     -162.92   -103.52
REMARK 500    ASP A1742       45.90     73.14
REMARK 500    ASP A1823        1.56     85.31
REMARK 500    GLU A1849       60.75     63.64
REMARK 500    GLU A1940     -126.54     58.86
REMARK 500    PHE A1987     -103.08   -113.14
REMARK 500    LEU A2123       62.03     32.69
REMARK 500    TYR A2298       34.43    -95.99
REMARK 500    SER A2369      156.66    146.94
REMARK 500    SER A2373       54.24     72.62
REMARK 500    PRO A2388       -5.90    -57.09
REMARK 500    LYS A2411        6.53     84.50
REMARK 500    LYS A2447      -39.20    -39.03
REMARK 500    LEU A2471     -136.12     60.13
REMARK 500    ASN A2481      145.24    -38.60
REMARK 500    GLN A2513      -23.00     97.59
REMARK 500    GLU A2548      -18.23    -46.86
REMARK 500    SER A2563      -56.85     75.17
REMARK 500    ARG A2638      129.11    -38.07
REMARK 500    GLU A2727     -149.11   -102.18
REMARK 500    ALA A2761     -121.47     56.64
REMARK 500    ARG A2763       -8.32     94.60
REMARK 500    HIS A2789       40.02   -104.44
REMARK 500    PHE A2940      143.43    -38.11
REMARK 500    THR A3309      -38.77      2.19
REMARK 500    THR A3332      -63.45    -93.96
REMARK 500    ILE A3462      -17.57    -49.10
REMARK 500    ASP A3483      -56.44   -138.66
REMARK 500    ASP A3739      -13.92     70.69
REMARK 500    LYS A3808        4.12     80.65
REMARK 500    GLU A3809     -131.31     31.71
REMARK 500    SER A3818     -162.34   -114.78
REMARK 500    ILE A3980        1.27    -59.36
REMARK 500    PRO A3981       -4.95    -55.92
REMARK 500
REMARK 500 THIS ENTRY HAS     102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASN A 3308     THR A 3309                  140.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A1794        19.1      L          L   OUTSIDE RANGE
REMARK 500    PHE A2257        24.1      L          L   OUTSIDE RANGE
REMARK 500    ILE A3980        22.6      L          L   OUTSIDE RANGE
REMARK 500    LYS B1422        23.2      L          L   OUTSIDE RANGE
REMARK 500    PHE B1794        19.3      L          L   OUTSIDE RANGE
REMARK 500    PHE B2257        22.0      L          L   OUTSIDE RANGE
REMARK 500    ILE B2479        22.1      L          L   OUTSIDE RANGE
REMARK 500    ASN B2521        24.4      L          L   OUTSIDE RANGE
REMARK 500    LYS B2522        23.6      L          L   OUTSIDE RANGE
REMARK 500    ILE B3980        23.6      L          L   OUTSIDE RANGE
REMARK 500    PHE B4015        22.1      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A5400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A5401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A5402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A5403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A5404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B5400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B5401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B5402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B5403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B5404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B8X   RELATED DB: PDB
REMARK 900  GLUTATHIONE S-TRANSFERASE FUSED WITH THE NUCLEAR MATRIX
REMARK 900   TARGETING SIGNAL OF THE TRANSCRIPTION FACTOR AML-1
REMARK 900 RELATED ID: 1DUG   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING
REMARK 900  ANDFACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH
REMARK 900  CARRIERPROTEIN DRIVEN CRYSTALLIZATION
REMARK 900 RELATED ID: 1GNE   RELATED DB: PDB
REMARK 900  GLUTATHIONE S-TRANSFERASE FUSED WITH A CONSERVED
REMARK 900  NEUTRALIZING EPITOPE ON GP41 OF HUMAN IMMUNODEFICIENCY
REMARK 900  VIRUS TYPE 1, COMPLEXED WITH GLUTATHIONE
REMARK 900 RELATED ID: 1GTA   RELATED DB: PDB
REMARK 900  GLUTATHIONE S-TRANSFERASE (26 KDA)
REMARK 900 RELATED ID: 1GTB   RELATED DB: PDB
REMARK 900 RELATED ID: 1M99   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S-
REMARK 900  TRANSFERASEFROM SCHISTOSOMA JAPONICUM COMPLEXED WITH
REMARK 900  GLUTATHIONESULFONIC ACID
REMARK 900 RELATED ID: 1M9A   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S-
REMARK 900  TRANSFERASEFROM SCHISTOSOMA JAPONICUM COMPLEXED WITH S-
REMARK 900  HEXYLGLUTATHIONE
REMARK 900 RELATED ID: 1M9B   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S-
REMARK 900  TRANSFERASEFROM SCHISTOSOMA JAPONICUM COMPLEXED WITH GAMMA-
REMARK 900  GLUTAMYL[S-(2-IODOBENZYL)CYSTEINYL]GLYCINE
REMARK 900 RELATED ID: 1U87   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S-
REMARK 900  TRANSFERASEY7F MUTANT FROM SCHISTOSOMA JAPONICUM COMPLEXED
REMARK 900  WITHGLUTATHIONE
REMARK 900 RELATED ID: 1U88   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE 26 KDA GLUTATHIONE S-
REMARK 900  TRANSFERASEY7F MUTANT FROM SCHISTOSOMA JAPONICUM COMPLEXED
REMARK 900  WITH S-OCTYL GLUTATHIONE
REMARK 900 RELATED ID: 1UA5   RELATED DB: PDB
REMARK 900  NON-FUSION GST FROM S. JAPONICUM IN COMPLEX WITH
REMARK 900  GLUTATHIONE
REMARK 900 RELATED ID: 1Y6E   RELATED DB: PDB
REMARK 900  ORTHORHOMBIC GLUTATHIONE S-TRANSFERASE OF
REMARK 900  SCHISTOSOMAJAPONICUM
REMARK 900 RELATED ID: 4AKG   RELATED DB: PDB
REMARK 900  DYNEIN MOTOR DOMAIN - ATP COMPLEX
REMARK 900 RELATED ID: 4AKH   RELATED DB: PDB
REMARK 900  DYNEIN MOTOR DOMAIN - AMPPNP COMPLEX
REMARK 900 RELATED ID: 4AKI   RELATED DB: PDB
REMARK 900  DYNEIN MOTOR DOMAIN - LUAC DERIVATIVE
DBREF  4AI6 A    1   217  UNP    P08515   GST26_SCHJA      2    218
DBREF  4AI6 A  218   219  PDB    4AI6     4AI6           218    219
DBREF  4AI6 A 1364  3038  UNP    P36022   DYHC_YEAST    1364   3038
DBREF  4AI6 A 3292  4092  UNP    P36022   DYHC_YEAST    3292   4092
DBREF  4AI6 B    1   217  UNP    P08515   GST26_SCHJA      2    218
DBREF  4AI6 B  218   219  PDB    4AI6     4AI6           218    219
DBREF  4AI6 B 1364  3038  UNP    P36022   DYHC_YEAST    1364   3038
DBREF  4AI6 B 3292  4092  UNP    P36022   DYHC_YEAST    3292   4092
SEQADV 4AI6 ILE A 1630  UNP  P36022    LEU  1630 CONFLICT
SEQADV 4AI6 ASP A 3782  UNP  P36022    GLU  3782 CONFLICT
SEQADV 4AI6 ILE B 1630  UNP  P36022    LEU  1630 CONFLICT
SEQADV 4AI6 ASP B 3782  UNP  P36022    GLU  3782 CONFLICT
SEQRES   1 A 2695  SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU VAL
SEQRES   2 A 2695  GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU LYS
SEQRES   3 A 2695  TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP LYS
SEQRES   4 A 2695  TRP ARG ASN LYS LYS PHE GLU LEU GLY LEU GLU PHE PRO
SEQRES   5 A 2695  ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU THR
SEQRES   6 A 2695  GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS HIS
SEQRES   7 A 2695  ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU ILE
SEQRES   8 A 2695  SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR GLY
SEQRES   9 A 2695  VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR LEU
SEQRES  10 A 2695  LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU LYS
SEQRES  11 A 2695  MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU ASN
SEQRES  12 A 2695  GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR ASP
SEQRES  13 A 2695  ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS LEU
SEQRES  14 A 2695  ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG ILE
SEQRES  15 A 2695  GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER SER
SEQRES  16 A 2695  LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA THR
SEQRES  17 A 2695  PHE GLY GLY GLY ASP HIS PRO PRO LYS SER ASP GLU PHE
SEQRES  18 A 2695  VAL ILE GLU LYS SER LEU ASN ARG ILE LYS LYS PHE TRP
SEQRES  19 A 2695  LYS GLU ALA GLN TYR GLU VAL ILE GLU HIS SER SER GLY
SEQRES  20 A 2695  LEU LYS LEU VAL ARG GLU TRP ASP VAL LEU GLU GLN ALA
SEQRES  21 A 2695  CYS LYS GLU ASP LEU GLU GLU LEU VAL SER MET LYS ALA
SEQRES  22 A 2695  SER ASN TYR TYR LYS ILE PHE GLU GLN ASP CYS LEU ASP
SEQRES  23 A 2695  LEU GLU SER LYS LEU THR LYS LEU SER GLU ILE GLN VAL
SEQRES  24 A 2695  ASN TRP VAL GLU VAL GLN PHE TYR TRP LEU ASP LEU TYR
SEQRES  25 A 2695  GLY ILE LEU GLY GLU ASN LEU ASP ILE GLN ASN PHE LEU
SEQRES  26 A 2695  PRO LEU GLU THR SER LYS PHE LYS SER LEU THR SER GLU
SEQRES  27 A 2695  TYR LYS MET ILE THR THR ARG ALA PHE GLN LEU ASP THR
SEQRES  28 A 2695  THR ILE GLU VAL ILE HIS ILE PRO ASN PHE ASP THR THR
SEQRES  29 A 2695  LEU LYS LEU THR ILE ASP SER LEU LYS MET ILE LYS SER
SEQRES  30 A 2695  SER LEU SER THR PHE LEU GLU ARG GLN ARG ARG GLN PHE
SEQRES  31 A 2695  PRO ARG PHE TYR PHE LEU GLY ASN ASP ASP LEU LEU LYS
SEQRES  32 A 2695  ILE ILE GLY SER GLY LYS HIS HIS ASP GLN VAL SER LYS
SEQRES  33 A 2695  PHE MET LYS LYS MET PHE GLY SER ILE GLU SER ILE ILE
SEQRES  34 A 2695  PHE LEU GLU ASP PHE ILE THR GLY VAL ARG SER VAL GLU
SEQRES  35 A 2695  GLY GLU VAL LEU ASN LEU ASN GLU LYS ILE GLU LEU LYS
SEQRES  36 A 2695  ASP SER ILE GLN ALA GLN GLU TRP LEU ASN ILE LEU ASP
SEQRES  37 A 2695  THR GLU ILE LYS LEU SER VAL PHE THR GLN PHE ARG ASP
SEQRES  38 A 2695  CYS LEU GLY GLN ILE LYS ASP GLY THR ASP ILE GLU VAL
SEQRES  39 A 2695  VAL VAL SER LYS TYR ILE PHE GLN ALA ILE LEU LEU SER
SEQRES  40 A 2695  ALA GLN VAL MET TRP THR GLU LEU VAL GLU LYS CYS LEU
SEQRES  41 A 2695  GLN THR ASN GLN PHE SER LYS TYR TRP LYS GLU VAL ASP
SEQRES  42 A 2695  MET LYS ILE LYS GLY LEU LEU ASP LYS LEU ASN LYS SER
SEQRES  43 A 2695  SER ASP ASN VAL LYS LYS LYS ILE GLU ALA LEU LEU VAL
SEQRES  44 A 2695  GLU TYR LEU HIS PHE ASN ASN VAL ILE GLY GLN LEU LYS
SEQRES  45 A 2695  ASN CYS SER THR LYS GLU GLU ALA ARG LEU LEU TRP ALA
SEQRES  46 A 2695  LYS VAL GLN LYS PHE TYR GLN LYS ASN ASP THR LEU ASP
SEQRES  47 A 2695  ASP LEU ASN SER VAL PHE ILE SER GLN SER GLY TYR LEU
SEQRES  48 A 2695  LEU GLN TYR LYS PHE GLU TYR ILE GLY ILE PRO GLU ARG
SEQRES  49 A 2695  LEU ILE TYR THR PRO LEU LEU LEU ILE GLY PHE ALA THR
SEQRES  50 A 2695  LEU THR ASP SER LEU HIS GLN LYS TYR GLY GLY CYS PHE
SEQRES  51 A 2695  PHE GLY PRO ALA GLY THR GLY LYS THR GLU THR VAL LYS
SEQRES  52 A 2695  ALA PHE GLY GLN ASN LEU GLY ARG VAL VAL VAL VAL PHE
SEQRES  53 A 2695  ASN CYS ASP ASP SER PHE ASP TYR GLN VAL LEU SER ARG
SEQRES  54 A 2695  LEU LEU VAL GLY ILE THR GLN ILE GLY ALA TRP GLY CYS
SEQRES  55 A 2695  PHE ASP GLU PHE ASN ARG LEU ASP GLU LYS VAL LEU SER
SEQRES  56 A 2695  ALA VAL SER ALA ASN ILE GLN GLN ILE GLN ASN GLY LEU
SEQRES  57 A 2695  GLN VAL GLY LYS SER HIS ILE THR LEU LEU GLU GLU GLU
SEQRES  58 A 2695  THR PRO LEU SER PRO HIS THR ALA VAL PHE ILE THR LEU
SEQRES  59 A 2695  ASN PRO GLY TYR ASN GLY ARG SER GLU LEU PRO GLU ASN
SEQRES  60 A 2695  LEU LYS LYS SER PHE ARG GLU PHE SER MET LYS SER PRO
SEQRES  61 A 2695  GLN SER GLY THR ILE ALA GLU MET ILE LEU GLN ILE MET
SEQRES  62 A 2695  GLY PHE GLU ASP SER LYS SER LEU ALA SER LYS ILE VAL
SEQRES  63 A 2695  HIS PHE LEU GLU LEU LEU SER SER LYS CYS SER SER MET
SEQRES  64 A 2695  ASN HIS TYR HIS PHE GLY LEU ARG THR LEU LYS GLY VAL
SEQRES  65 A 2695  LEU ARG ASN CYS SER PRO LEU ILE SER GLU PHE GLY GLU
SEQRES  66 A 2695  GLY GLU LYS THR VAL VAL GLU SER LEU LYS ARG VAL ILE
SEQRES  67 A 2695  LEU PRO SER LEU GLY ASP THR ASP GLU LEU VAL PHE LYS
SEQRES  68 A 2695  ASP GLU LEU SER LYS ILE PHE ASP SER ALA GLY THR PRO
SEQRES  69 A 2695  LEU ASN SER LYS ALA ILE VAL GLN CYS LEU LYS ASP ALA
SEQRES  70 A 2695  GLY GLN ARG SER GLY PHE SER MET SER GLU GLU PHE LEU
SEQRES  71 A 2695  LYS LYS CYS MET GLN PHE TYR TYR MET GLN LYS THR GLN
SEQRES  72 A 2695  GLN ALA LEU ILE LEU VAL GLY LYS ALA GLY CYS GLY LYS
SEQRES  73 A 2695  THR ALA THR TRP LYS THR VAL ILE ASP ALA MET ALA ILE
SEQRES  74 A 2695  PHE ASP GLY HIS ALA ASN VAL VAL TYR VAL ILE ASP THR
SEQRES  75 A 2695  LYS VAL LEU THR LYS GLU SER LEU TYR GLY SER MET LEU
SEQRES  76 A 2695  LYS ALA THR LEU GLU TRP ARG ASP GLY LEU PHE THR SER
SEQRES  77 A 2695  ILE LEU ARG ARG VAL ASN ASP ASP ILE THR GLY THR PHE
SEQRES  78 A 2695  LYS ASN SER ARG ILE TRP VAL VAL PHE ASP SER ASP LEU
SEQRES  79 A 2695  ASP PRO GLU TYR VAL GLU ALA MET ASN SER VAL LEU ASP
SEQRES  80 A 2695  ASP ASN LYS ILE LEU THR LEU PRO ASN GLY GLU ARG LEU
SEQRES  81 A 2695  PRO ILE PRO PRO ASN PHE ARG ILE LEU PHE GLU THR ASP
SEQRES  82 A 2695  ASN LEU ASP HIS THR THR PRO ALA THR ILE THR ARG CYS
SEQRES  83 A 2695  GLY LEU LEU TRP PHE SER THR ASP VAL CYS SER ILE SER
SEQRES  84 A 2695  SER LYS ILE ASP HIS LEU LEU ASN LYS SER TYR GLU ALA
SEQRES  85 A 2695  LEU ASP ASN LYS LEU SER MET PHE GLU LEU ASP LYS LEU
SEQRES  86 A 2695  LYS ASP LEU ILE SER ASP SER PHE ASP MET ALA SER LEU
SEQRES  87 A 2695  THR ASN ILE PHE THR CYS SER ASN ASP LEU VAL HIS ILE
SEQRES  88 A 2695  LEU GLY VAL ARG THR PHE ASN LYS LEU GLU THR ALA VAL
SEQRES  89 A 2695  GLN LEU ALA VAL HIS LEU ILE SER SER TYR ARG GLN TRP
SEQRES  90 A 2695  PHE GLN ASN LEU ASP ASP LYS SER LEU LYS ASP VAL ILE
SEQRES  91 A 2695  THR LEU LEU ILE LYS ARG SER LEU LEU TYR ALA LEU ALA
SEQRES  92 A 2695  GLY ASP SER THR GLY GLU SER GLN ARG ALA PHE ILE GLN
SEQRES  93 A 2695  THR ILE ASN THR TYR PHE GLY HIS ASP SER GLN GLU LEU
SEQRES  94 A 2695  SER ASP TYR SER THR ILE VAL ILE ALA ASN ASP LYS LEU
SEQRES  95 A 2695  SER PHE SER SER PHE CYS SER GLU ILE PRO SER VAL SER
SEQRES  96 A 2695  LEU GLU ALA HIS GLU VAL MET ARG PRO ASP ILE VAL ILE
SEQRES  97 A 2695  PRO THR ILE ASP THR ILE LYS HIS GLU LYS ILE PHE TYR
SEQRES  98 A 2695  ASP LEU LEU ASN SER LYS ARG GLY ILE ILE LEU CYS GLY
SEQRES  99 A 2695  PRO PRO GLY SER GLY LYS THR MET ILE MET ASN ASN ALA
SEQRES 100 A 2695  LEU ARG ASN SER SER LEU TYR ASP VAL VAL GLY ILE ASN
SEQRES 101 A 2695  PHE SER LYS ASP THR THR THR GLU HIS ILE LEU SER ALA
SEQRES 102 A 2695  LEU HIS ARG HIS THR ASN TYR VAL THR THR SER LYS GLY
SEQRES 103 A 2695  LEU THR LEU LEU PRO LYS SER ASP ILE LYS ASN LEU VAL
SEQRES 104 A 2695  LEU PHE CYS ASP GLU ILE ASN LEU PRO LYS LEU ASP LYS
SEQRES 105 A 2695  TYR GLY SER GLN ASN VAL VAL LEU PHE LEU ARG GLN LEU
SEQRES 106 A 2695  MET GLU LYS GLN GLY PHE TRP LYS THR PRO GLU ASN LYS
SEQRES 107 A 2695  TRP VAL THR ILE GLU ARG ILE HIS ILE VAL GLY ALA CYS
SEQRES 108 A 2695  ASN PRO PRO THR ASP PRO GLY ARG ILE PRO MET SER GLU
SEQRES 109 A 2695  ARG PHE THR ARG HIS ALA ALA ILE LEU TYR LEU GLY TYR
SEQRES 110 A 2695  PRO SER GLY LYS SER LEU SER GLN ILE TYR GLU ILE TYR
SEQRES 111 A 2695  TYR LYS ALA ILE PHE LYS LEU VAL PRO GLU PHE ARG SER
SEQRES 112 A 2695  TYR THR GLU PRO PHE ALA ARG ALA SER VAL HIS LEU TYR
SEQRES 113 A 2695  ASN GLU CYS LYS ALA ARG TYR SER THR GLY LEU GLN SER
SEQRES 114 A 2695  HIS TYR LEU PHE SER PRO ARG GLU LEU THR ARG LEU VAL
SEQRES 115 A 2695  ARG GLY VAL TYR THR ALA ILE ASN THR GLY PRO ARG GLN
SEQRES 116 A 2695  THR LEU ARG SER LEU ILE ARG LEU TRP ALA TYR GLU ALA
SEQRES 117 A 2695  TRP ARG ILE PHE ALA ASP ARG LEU VAL GLY VAL LYS GLU
SEQRES 118 A 2695  LYS ASN SER PHE GLU GLN LEU LEU TYR GLU THR VAL ASP
SEQRES 119 A 2695  LYS TYR LEU PRO ASN GLN ASP LEU GLY ASN ILE SER SER
SEQRES 120 A 2695  THR SER LEU LEU PHE SER GLY LEU LEU SER LEU ASP PHE
SEQRES 121 A 2695  LYS GLU VAL ASN LYS THR ASP LEU VAL ASN PHE ILE GLU
SEQRES 122 A 2695  GLU ARG PHE LYS THR PHE CYS ASP GLU GLU LEU GLU VAL
SEQRES 123 A 2695  PRO MET VAL ILE HIS GLU SER MET VAL ASP HIS ILE LEU
SEQRES 124 A 2695  ARG ILE ASP ARG ALA LEU LYS GLN VAL GLN GLY HIS MET
SEQRES 125 A 2695  MET LEU ILE GLY ALA SER ARG THR GLY LYS THR ILE LEU
SEQRES 126 A 2695  THR ARG PHE VAL ALA TRP LEU ASN GLY LEU LYS ILE VAL
SEQRES 127 A 2695  GLN PRO LYS ILE HIS ARG HIS SER ASN LEU SER ASP PHE
SEQRES 128 A 2695  ASP MET ILE LEU LYS LYS ALA ILE SER ASP CYS SER LEU
SEQRES 129 A 2695  LYS GLU SER ARG THR CYS LEU ILE ILE ASP GLU SER ASN
SEQRES 130 A 2695  ILE LEU GLU THR ALA PHE LEU GLU ARG MET ASN THR LEU
SEQRES 131 A 2695  LEU ALA ASN ALA ASP ILE PRO ASP LEU PHE GLN GLY GLU
SEQRES 132 A 2695  GLU TYR ASP LYS LEU LEU ASN ASN LEU ARG ASN LYS THR
SEQRES 133 A 2695  ARG SER LEU GLY LEU LEU LEU ASP THR GLU GLN GLU LEU
SEQRES 134 A 2695  TYR ASP TRP PHE VAL GLY GLU ILE ALA LYS ASN LEU HIS
SEQRES 135 A 2695  VAL VAL PHE THR ILE CYS ASP PRO THR ASN ASN LYS SER
SEQRES 136 A 2695  SER ALA MET ILE SER SER PRO ALA LEU PHE ASN ARG CYS
SEQRES 137 A 2695  ILE ILE ASN TRP MET GLY ASP TRP ASP THR LYS THR MET
SEQRES 138 A 2695  SER GLN VAL ALA ASN ASN MET VAL ASP VAL ILE PRO MET
SEQRES 139 A 2695  GLU PHE THR ASP PHE ILE VAL PRO GLU VAL ASN LYS GLU
SEQRES 140 A 2695  LEU VAL PHE THR GLU PRO ILE GLN THR ILE ARG ASP ALA
SEQRES 141 A 2695  VAL VAL ASN ILE LEU ILE HIS PHE ASP ARG ASN PHE TYR
SEQRES 142 A 2695  GLN LYS MET LYS VAL GLY VAL ASN PRO ARG SER PRO GLY
SEQRES 143 A 2695  TYR PHE ILE ASP GLY LEU ARG ALA LEU VAL LYS LEU VAL
SEQRES 144 A 2695  THR ALA LYS TYR GLN ASP LEU GLN GLU ASN GLN ARG PHE
SEQRES 145 A 2695  VAL ASN VAL GLY LEU GLU LYS LEU ASN GLU SER VAL LEU
SEQRES 146 A 2695  LYS VAL ASN GLU LEU ASN LYS THR LEU SER ILE SER LEU
SEQRES 147 A 2695  VAL LYS SER LEU THR PHE GLU LYS GLU ARG TRP LEU ASN
SEQRES 148 A 2695  THR THR LYS GLN PHE SER LYS THR SER GLN GLU LEU ILE
SEQRES 149 A 2695  GLY ASN CYS ILE ILE SER SER ILE TYR GLU THR TYR PHE
SEQRES 150 A 2695  GLY HIS LEU ASN GLU ARG GLU ARG ALA ASP MET LEU VAL
SEQRES 151 A 2695  ILE LEU LYS ARG LEU LEU GLY LYS PHE ALA VAL LYS TYR
SEQRES 152 A 2695  ASP VAL ASN TYR ARG PHE ILE ASP TYR LEU VAL THR LEU
SEQRES 153 A 2695  ASP GLU LYS MET LYS TRP LEU GLU CYS GLY LEU ASP LYS
SEQRES 154 A 2695  ASN ASP TYR PHE LEU GLU ASN MET SER ILE VAL MET ASN
SEQRES 155 A 2695  SER GLN ASP ALA VAL PRO PHE LEU LEU ASP PRO SER SER
SEQRES 156 A 2695  HIS MET ILE THR VAL ILE SER ASN TYR TYR GLY ASN LYS
SEQRES 157 A 2695  THR VAL LEU LEU SER PHE LEU GLU GLU GLY PHE VAL LYS
SEQRES 158 A 2695  ARG LEU GLU ASN ALA ILE ARG PHE GLY SER VAL VAL ILE
SEQRES 159 A 2695  ILE GLN ASP GLY GLU PHE PHE ASP PRO ILE ILE SER ARG
SEQRES 160 A 2695  LEU ILE SER ARG GLU PHE ASN HIS ALA GLY ASN ARG VAL
SEQRES 161 A 2695  THR VAL GLU ILE GLY ASP HIS GLU VAL ASP VAL SER GLY
SEQRES 162 A 2695  ASP PHE LYS LEU PHE ILE HIS SER CYS ASP PRO SER GLY
SEQRES 163 A 2695  ASP ILE PRO ILE PHE LEU ARG SER ARG VAL ARG LEU VAL
SEQRES 164 A 2695  HIS PHE VAL THR ASN LYS GLU SER ILE GLU THR ARG ILE
SEQRES 165 A 2695  PHE ASP ILE THR LEU THR GLU GLU ASN ALA GLU MET GLN
SEQRES 166 A 2695  ARG LYS ARG GLU ASP LEU ILE LYS LEU ASN THR GLU TYR
SEQRES 167 A 2695  LYS LEU LYS LEU LYS ASN LEU GLU LYS ARG LEU LEU GLU
SEQRES 168 A 2695  GLU LEU ASN ASN SER GLN GLY ASN MET LEU GLU ASN ASP
SEQRES 169 A 2695  GLU LEU MET VAL THR LEU ASN ASN LEU LYS LYS GLU ALA
SEQRES 170 A 2695  MET ASN ILE GLU LYS LYS LEU SER GLU SER GLU GLU PHE
SEQRES 171 A 2695  PHE PRO GLN PHE ASP ASN LEU VAL GLU GLU TYR SER ILE
SEQRES 172 A 2695  ILE GLY LYS HIS SER VAL LYS ILE PHE SER MET LEU GLU
SEQRES 173 A 2695  LYS PHE GLY GLN PHE HIS TRP PHE TYR GLY ILE SER ILE
SEQRES 174 A 2695  GLY GLN PHE LEU SER CYS PHE LYS ARG VAL PHE ILE LYS
SEQRES 175 A 2695  LYS SER ARG GLU THR ARG ALA ALA ARG THR ARG VAL ASP
SEQRES 176 A 2695  GLU ILE LEU TRP LEU LEU TYR GLN GLU VAL TYR CYS GLN
SEQRES 177 A 2695  PHE SER THR ALA LEU ASP LYS LYS PHE LYS MET ILE MET
SEQRES 178 A 2695  ALA MET THR MET PHE CYS LEU TYR LYS PHE ASP ILE GLU
SEQRES 179 A 2695  SER GLU GLN TYR LYS GLU ALA VAL LEU THR MET ILE GLY
SEQRES 180 A 2695  VAL LEU SER GLU SER SER ASP GLY VAL PRO LYS LEU THR
SEQRES 181 A 2695  VAL ASP THR ASN ASN ASP LEU ARG TYR LEU TRP ASP TYR
SEQRES 182 A 2695  VAL THR THR LYS SER TYR ILE SER ALA LEU ASN TRP PHE
SEQRES 183 A 2695  LYS ASN GLU PHE PHE VAL ASP GLU TRP ASN ILE ALA ASP
SEQRES 184 A 2695  VAL VAL ALA ASN SER ASP ASN ASN TYR PHE THR MET ALA
SEQRES 185 A 2695  SER GLU ARG ASP VAL ASP GLY THR PHE LYS LEU ILE GLU
SEQRES 186 A 2695  LEU ALA LYS ALA SER LYS GLU SER LEU LYS ILE ILE PRO
SEQRES 187 A 2695  LEU GLY SER ILE GLU ASN LEU ASN TYR ALA GLN GLU GLU
SEQRES 188 A 2695  ILE SER LYS SER LYS ILE GLU GLY GLY TRP ILE LEU LEU
SEQRES 189 A 2695  GLN ASN ILE GLN MET SER LEU SER TRP VAL LYS THR TYR
SEQRES 190 A 2695  LEU HIS LYS HIS VAL GLU GLU THR LYS ALA ALA GLU GLU
SEQRES 191 A 2695  HIS GLU LYS PHE LYS MET PHE MET THR CYS HIS LEU THR
SEQRES 192 A 2695  GLY ASP LYS LEU PRO ALA PRO LEU LEU GLN ARG THR ASP
SEQRES 193 A 2695  ARG PHE VAL TYR GLU ASP ILE PRO GLY ILE LEU ASP THR
SEQRES 194 A 2695  VAL LYS ASP LEU TRP GLY SER GLN PHE PHE THR GLY LYS
SEQRES 195 A 2695  ILE SER GLY VAL TRP SER VAL TYR CYS THR PHE LEU LEU
SEQRES 196 A 2695  SER TRP PHE HIS ALA LEU ILE THR ALA ARG THR ARG LEU
SEQRES 197 A 2695  VAL PRO HIS GLY PHE SER LYS LYS TYR TYR PHE ASN ASP
SEQRES 198 A 2695  CYS ASP PHE GLN PHE ALA SER VAL TYR LEU GLU ASN VAL
SEQRES 199 A 2695  LEU ALA THR ASN SER THR ASN ASN ILE PRO TRP ALA GLN
SEQRES 200 A 2695  VAL ARG ASP HIS ILE ALA THR ILE VAL TYR GLY GLY LYS
SEQRES 201 A 2695  ILE ASP GLU GLU LYS ASP LEU GLU VAL VAL ALA LYS LEU
SEQRES 202 A 2695  CYS ALA HIS VAL PHE CYS GLY SER ASP ASN LEU GLN ILE
SEQRES 203 A 2695  VAL PRO GLY VAL ARG ILE PRO GLN PRO LEU LEU GLN GLN
SEQRES 204 A 2695  SER GLU GLU GLU GLU ARG ALA ARG LEU THR ALA ILE LEU
SEQRES 205 A 2695  SER ASN THR ILE GLU PRO ALA ASP SER LEU SER SER TRP
SEQRES 206 A 2695  LEU GLN LEU PRO ARG GLU SER ILE LEU ASN TYR GLU ARG
SEQRES 207 A 2695  LEU GLN ALA LYS GLU VAL ALA SER SER THR GLU GLN LEU
SEQRES 208 A 2695  LEU GLN GLU MET
SEQRES   1 B 2695  SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU VAL
SEQRES   2 B 2695  GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU LYS
SEQRES   3 B 2695  TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP LYS
SEQRES   4 B 2695  TRP ARG ASN LYS LYS PHE GLU LEU GLY LEU GLU PHE PRO
SEQRES   5 B 2695  ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU THR
SEQRES   6 B 2695  GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS HIS
SEQRES   7 B 2695  ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU ILE
SEQRES   8 B 2695  SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR GLY
SEQRES   9 B 2695  VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR LEU
SEQRES  10 B 2695  LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU LYS
SEQRES  11 B 2695  MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU ASN
SEQRES  12 B 2695  GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR ASP
SEQRES  13 B 2695  ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS LEU
SEQRES  14 B 2695  ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG ILE
SEQRES  15 B 2695  GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER SER
SEQRES  16 B 2695  LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA THR
SEQRES  17 B 2695  PHE GLY GLY GLY ASP HIS PRO PRO LYS SER ASP GLU PHE
SEQRES  18 B 2695  VAL ILE GLU LYS SER LEU ASN ARG ILE LYS LYS PHE TRP
SEQRES  19 B 2695  LYS GLU ALA GLN TYR GLU VAL ILE GLU HIS SER SER GLY
SEQRES  20 B 2695  LEU LYS LEU VAL ARG GLU TRP ASP VAL LEU GLU GLN ALA
SEQRES  21 B 2695  CYS LYS GLU ASP LEU GLU GLU LEU VAL SER MET LYS ALA
SEQRES  22 B 2695  SER ASN TYR TYR LYS ILE PHE GLU GLN ASP CYS LEU ASP
SEQRES  23 B 2695  LEU GLU SER LYS LEU THR LYS LEU SER GLU ILE GLN VAL
SEQRES  24 B 2695  ASN TRP VAL GLU VAL GLN PHE TYR TRP LEU ASP LEU TYR
SEQRES  25 B 2695  GLY ILE LEU GLY GLU ASN LEU ASP ILE GLN ASN PHE LEU
SEQRES  26 B 2695  PRO LEU GLU THR SER LYS PHE LYS SER LEU THR SER GLU
SEQRES  27 B 2695  TYR LYS MET ILE THR THR ARG ALA PHE GLN LEU ASP THR
SEQRES  28 B 2695  THR ILE GLU VAL ILE HIS ILE PRO ASN PHE ASP THR THR
SEQRES  29 B 2695  LEU LYS LEU THR ILE ASP SER LEU LYS MET ILE LYS SER
SEQRES  30 B 2695  SER LEU SER THR PHE LEU GLU ARG GLN ARG ARG GLN PHE
SEQRES  31 B 2695  PRO ARG PHE TYR PHE LEU GLY ASN ASP ASP LEU LEU LYS
SEQRES  32 B 2695  ILE ILE GLY SER GLY LYS HIS HIS ASP GLN VAL SER LYS
SEQRES  33 B 2695  PHE MET LYS LYS MET PHE GLY SER ILE GLU SER ILE ILE
SEQRES  34 B 2695  PHE LEU GLU ASP PHE ILE THR GLY VAL ARG SER VAL GLU
SEQRES  35 B 2695  GLY GLU VAL LEU ASN LEU ASN GLU LYS ILE GLU LEU LYS
SEQRES  36 B 2695  ASP SER ILE GLN ALA GLN GLU TRP LEU ASN ILE LEU ASP
SEQRES  37 B 2695  THR GLU ILE LYS LEU SER VAL PHE THR GLN PHE ARG ASP
SEQRES  38 B 2695  CYS LEU GLY GLN ILE LYS ASP GLY THR ASP ILE GLU VAL
SEQRES  39 B 2695  VAL VAL SER LYS TYR ILE PHE GLN ALA ILE LEU LEU SER
SEQRES  40 B 2695  ALA GLN VAL MET TRP THR GLU LEU VAL GLU LYS CYS LEU
SEQRES  41 B 2695  GLN THR ASN GLN PHE SER LYS TYR TRP LYS GLU VAL ASP
SEQRES  42 B 2695  MET LYS ILE LYS GLY LEU LEU ASP LYS LEU ASN LYS SER
SEQRES  43 B 2695  SER ASP ASN VAL LYS LYS LYS ILE GLU ALA LEU LEU VAL
SEQRES  44 B 2695  GLU TYR LEU HIS PHE ASN ASN VAL ILE GLY GLN LEU LYS
SEQRES  45 B 2695  ASN CYS SER THR LYS GLU GLU ALA ARG LEU LEU TRP ALA
SEQRES  46 B 2695  LYS VAL GLN LYS PHE TYR GLN LYS ASN ASP THR LEU ASP
SEQRES  47 B 2695  ASP LEU ASN SER VAL PHE ILE SER GLN SER GLY TYR LEU
SEQRES  48 B 2695  LEU GLN TYR LYS PHE GLU TYR ILE GLY ILE PRO GLU ARG
SEQRES  49 B 2695  LEU ILE TYR THR PRO LEU LEU LEU ILE GLY PHE ALA THR
SEQRES  50 B 2695  LEU THR ASP SER LEU HIS GLN LYS TYR GLY GLY CYS PHE
SEQRES  51 B 2695  PHE GLY PRO ALA GLY THR GLY LYS THR GLU THR VAL LYS
SEQRES  52 B 2695  ALA PHE GLY GLN ASN LEU GLY ARG VAL VAL VAL VAL PHE
SEQRES  53 B 2695  ASN CYS ASP ASP SER PHE ASP TYR GLN VAL LEU SER ARG
SEQRES  54 B 2695  LEU LEU VAL GLY ILE THR GLN ILE GLY ALA TRP GLY CYS
SEQRES  55 B 2695  PHE ASP GLU PHE ASN ARG LEU ASP GLU LYS VAL LEU SER
SEQRES  56 B 2695  ALA VAL SER ALA ASN ILE GLN GLN ILE GLN ASN GLY LEU
SEQRES  57 B 2695  GLN VAL GLY LYS SER HIS ILE THR LEU LEU GLU GLU GLU
SEQRES  58 B 2695  THR PRO LEU SER PRO HIS THR ALA VAL PHE ILE THR LEU
SEQRES  59 B 2695  ASN PRO GLY TYR ASN GLY ARG SER GLU LEU PRO GLU ASN
SEQRES  60 B 2695  LEU LYS LYS SER PHE ARG GLU PHE SER MET LYS SER PRO
SEQRES  61 B 2695  GLN SER GLY THR ILE ALA GLU MET ILE LEU GLN ILE MET
SEQRES  62 B 2695  GLY PHE GLU ASP SER LYS SER LEU ALA SER LYS ILE VAL
SEQRES  63 B 2695  HIS PHE LEU GLU LEU LEU SER SER LYS CYS SER SER MET
SEQRES  64 B 2695  ASN HIS TYR HIS PHE GLY LEU ARG THR LEU LYS GLY VAL
SEQRES  65 B 2695  LEU ARG ASN CYS SER PRO LEU ILE SER GLU PHE GLY GLU
SEQRES  66 B 2695  GLY GLU LYS THR VAL VAL GLU SER LEU LYS ARG VAL ILE
SEQRES  67 B 2695  LEU PRO SER LEU GLY ASP THR ASP GLU LEU VAL PHE LYS
SEQRES  68 B 2695  ASP GLU LEU SER LYS ILE PHE ASP SER ALA GLY THR PRO
SEQRES  69 B 2695  LEU ASN SER LYS ALA ILE VAL GLN CYS LEU LYS ASP ALA
SEQRES  70 B 2695  GLY GLN ARG SER GLY PHE SER MET SER GLU GLU PHE LEU
SEQRES  71 B 2695  LYS LYS CYS MET GLN PHE TYR TYR MET GLN LYS THR GLN
SEQRES  72 B 2695  GLN ALA LEU ILE LEU VAL GLY LYS ALA GLY CYS GLY LYS
SEQRES  73 B 2695  THR ALA THR TRP LYS THR VAL ILE ASP ALA MET ALA ILE
SEQRES  74 B 2695  PHE ASP GLY HIS ALA ASN VAL VAL TYR VAL ILE ASP THR
SEQRES  75 B 2695  LYS VAL LEU THR LYS GLU SER LEU TYR GLY SER MET LEU
SEQRES  76 B 2695  LYS ALA THR LEU GLU TRP ARG ASP GLY LEU PHE THR SER
SEQRES  77 B 2695  ILE LEU ARG ARG VAL ASN ASP ASP ILE THR GLY THR PHE
SEQRES  78 B 2695  LYS ASN SER ARG ILE TRP VAL VAL PHE ASP SER ASP LEU
SEQRES  79 B 2695  ASP PRO GLU TYR VAL GLU ALA MET ASN SER VAL LEU ASP
SEQRES  80 B 2695  ASP ASN LYS ILE LEU THR LEU PRO ASN GLY GLU ARG LEU
SEQRES  81 B 2695  PRO ILE PRO PRO ASN PHE ARG ILE LEU PHE GLU THR ASP
SEQRES  82 B 2695  ASN LEU ASP HIS THR THR PRO ALA THR ILE THR ARG CYS
SEQRES  83 B 2695  GLY LEU LEU TRP PHE SER THR ASP VAL CYS SER ILE SER
SEQRES  84 B 2695  SER LYS ILE ASP HIS LEU LEU ASN LYS SER TYR GLU ALA
SEQRES  85 B 2695  LEU ASP ASN LYS LEU SER MET PHE GLU LEU ASP LYS LEU
SEQRES  86 B 2695  LYS ASP LEU ILE SER ASP SER PHE ASP MET ALA SER LEU
SEQRES  87 B 2695  THR ASN ILE PHE THR CYS SER ASN ASP LEU VAL HIS ILE
SEQRES  88 B 2695  LEU GLY VAL ARG THR PHE ASN LYS LEU GLU THR ALA VAL
SEQRES  89 B 2695  GLN LEU ALA VAL HIS LEU ILE SER SER TYR ARG GLN TRP
SEQRES  90 B 2695  PHE GLN ASN LEU ASP ASP LYS SER LEU LYS ASP VAL ILE
SEQRES  91 B 2695  THR LEU LEU ILE LYS ARG SER LEU LEU TYR ALA LEU ALA
SEQRES  92 B 2695  GLY ASP SER THR GLY GLU SER GLN ARG ALA PHE ILE GLN
SEQRES  93 B 2695  THR ILE ASN THR TYR PHE GLY HIS ASP SER GLN GLU LEU
SEQRES  94 B 2695  SER ASP TYR SER THR ILE VAL ILE ALA ASN ASP LYS LEU
SEQRES  95 B 2695  SER PHE SER SER PHE CYS SER GLU ILE PRO SER VAL SER
SEQRES  96 B 2695  LEU GLU ALA HIS GLU VAL MET ARG PRO ASP ILE VAL ILE
SEQRES  97 B 2695  PRO THR ILE ASP THR ILE LYS HIS GLU LYS ILE PHE TYR
SEQRES  98 B 2695  ASP LEU LEU ASN SER LYS ARG GLY ILE ILE LEU CYS GLY
SEQRES  99 B 2695  PRO PRO GLY SER GLY LYS THR MET ILE MET ASN ASN ALA
SEQRES 100 B 2695  LEU ARG ASN SER SER LEU TYR ASP VAL VAL GLY ILE ASN
SEQRES 101 B 2695  PHE SER LYS ASP THR THR THR GLU HIS ILE LEU SER ALA
SEQRES 102 B 2695  LEU HIS ARG HIS THR ASN TYR VAL THR THR SER LYS GLY
SEQRES 103 B 2695  LEU THR LEU LEU PRO LYS SER ASP ILE LYS ASN LEU VAL
SEQRES 104 B 2695  LEU PHE CYS ASP GLU ILE ASN LEU PRO LYS LEU ASP LYS
SEQRES 105 B 2695  TYR GLY SER GLN ASN VAL VAL LEU PHE LEU ARG GLN LEU
SEQRES 106 B 2695  MET GLU LYS GLN GLY PHE TRP LYS THR PRO GLU ASN LYS
SEQRES 107 B 2695  TRP VAL THR ILE GLU ARG ILE HIS ILE VAL GLY ALA CYS
SEQRES 108 B 2695  ASN PRO PRO THR ASP PRO GLY ARG ILE PRO MET SER GLU
SEQRES 109 B 2695  ARG PHE THR ARG HIS ALA ALA ILE LEU TYR LEU GLY TYR
SEQRES 110 B 2695  PRO SER GLY LYS SER LEU SER GLN ILE TYR GLU ILE TYR
SEQRES 111 B 2695  TYR LYS ALA ILE PHE LYS LEU VAL PRO GLU PHE ARG SER
SEQRES 112 B 2695  TYR THR GLU PRO PHE ALA ARG ALA SER VAL HIS LEU TYR
SEQRES 113 B 2695  ASN GLU CYS LYS ALA ARG TYR SER THR GLY LEU GLN SER
SEQRES 114 B 2695  HIS TYR LEU PHE SER PRO ARG GLU LEU THR ARG LEU VAL
SEQRES 115 B 2695  ARG GLY VAL TYR THR ALA ILE ASN THR GLY PRO ARG GLN
SEQRES 116 B 2695  THR LEU ARG SER LEU ILE ARG LEU TRP ALA TYR GLU ALA
SEQRES 117 B 2695  TRP ARG ILE PHE ALA ASP ARG LEU VAL GLY VAL LYS GLU
SEQRES 118 B 2695  LYS ASN SER PHE GLU GLN LEU LEU TYR GLU THR VAL ASP
SEQRES 119 B 2695  LYS TYR LEU PRO ASN GLN ASP LEU GLY ASN ILE SER SER
SEQRES 120 B 2695  THR SER LEU LEU PHE SER GLY LEU LEU SER LEU ASP PHE
SEQRES 121 B 2695  LYS GLU VAL ASN LYS THR ASP LEU VAL ASN PHE ILE GLU
SEQRES 122 B 2695  GLU ARG PHE LYS THR PHE CYS ASP GLU GLU LEU GLU VAL
SEQRES 123 B 2695  PRO MET VAL ILE HIS GLU SER MET VAL ASP HIS ILE LEU
SEQRES 124 B 2695  ARG ILE ASP ARG ALA LEU LYS GLN VAL GLN GLY HIS MET
SEQRES 125 B 2695  MET LEU ILE GLY ALA SER ARG THR GLY LYS THR ILE LEU
SEQRES 126 B 2695  THR ARG PHE VAL ALA TRP LEU ASN GLY LEU LYS ILE VAL
SEQRES 127 B 2695  GLN PRO LYS ILE HIS ARG HIS SER ASN LEU SER ASP PHE
SEQRES 128 B 2695  ASP MET ILE LEU LYS LYS ALA ILE SER ASP CYS SER LEU
SEQRES 129 B 2695  LYS GLU SER ARG THR CYS LEU ILE ILE ASP GLU SER ASN
SEQRES 130 B 2695  ILE LEU GLU THR ALA PHE LEU GLU ARG MET ASN THR LEU
SEQRES 131 B 2695  LEU ALA ASN ALA ASP ILE PRO ASP LEU PHE GLN GLY GLU
SEQRES 132 B 2695  GLU TYR ASP LYS LEU LEU ASN ASN LEU ARG ASN LYS THR
SEQRES 133 B 2695  ARG SER LEU GLY LEU LEU LEU ASP THR GLU GLN GLU LEU
SEQRES 134 B 2695  TYR ASP TRP PHE VAL GLY GLU ILE ALA LYS ASN LEU HIS
SEQRES 135 B 2695  VAL VAL PHE THR ILE CYS ASP PRO THR ASN ASN LYS SER
SEQRES 136 B 2695  SER ALA MET ILE SER SER PRO ALA LEU PHE ASN ARG CYS
SEQRES 137 B 2695  ILE ILE ASN TRP MET GLY ASP TRP ASP THR LYS THR MET
SEQRES 138 B 2695  SER GLN VAL ALA ASN ASN MET VAL ASP VAL ILE PRO MET
SEQRES 139 B 2695  GLU PHE THR ASP PHE ILE VAL PRO GLU VAL ASN LYS GLU
SEQRES 140 B 2695  LEU VAL PHE THR GLU PRO ILE GLN THR ILE ARG ASP ALA
SEQRES 141 B 2695  VAL VAL ASN ILE LEU ILE HIS PHE ASP ARG ASN PHE TYR
SEQRES 142 B 2695  GLN LYS MET LYS VAL GLY VAL ASN PRO ARG SER PRO GLY
SEQRES 143 B 2695  TYR PHE ILE ASP GLY LEU ARG ALA LEU VAL LYS LEU VAL
SEQRES 144 B 2695  THR ALA LYS TYR GLN ASP LEU GLN GLU ASN GLN ARG PHE
SEQRES 145 B 2695  VAL ASN VAL GLY LEU GLU LYS LEU ASN GLU SER VAL LEU
SEQRES 146 B 2695  LYS VAL ASN GLU LEU ASN LYS THR LEU SER ILE SER LEU
SEQRES 147 B 2695  VAL LYS SER LEU THR PHE GLU LYS GLU ARG TRP LEU ASN
SEQRES 148 B 2695  THR THR LYS GLN PHE SER LYS THR SER GLN GLU LEU ILE
SEQRES 149 B 2695  GLY ASN CYS ILE ILE SER SER ILE TYR GLU THR TYR PHE
SEQRES 150 B 2695  GLY HIS LEU ASN GLU ARG GLU ARG ALA ASP MET LEU VAL
SEQRES 151 B 2695  ILE LEU LYS ARG LEU LEU GLY LYS PHE ALA VAL LYS TYR
SEQRES 152 B 2695  ASP VAL ASN TYR ARG PHE ILE ASP TYR LEU VAL THR LEU
SEQRES 153 B 2695  ASP GLU LYS MET LYS TRP LEU GLU CYS GLY LEU ASP LYS
SEQRES 154 B 2695  ASN ASP TYR PHE LEU GLU ASN MET SER ILE VAL MET ASN
SEQRES 155 B 2695  SER GLN ASP ALA VAL PRO PHE LEU LEU ASP PRO SER SER
SEQRES 156 B 2695  HIS MET ILE THR VAL ILE SER ASN TYR TYR GLY ASN LYS
SEQRES 157 B 2695  THR VAL LEU LEU SER PHE LEU GLU GLU GLY PHE VAL LYS
SEQRES 158 B 2695  ARG LEU GLU ASN ALA ILE ARG PHE GLY SER VAL VAL ILE
SEQRES 159 B 2695  ILE GLN ASP GLY GLU PHE PHE ASP PRO ILE ILE SER ARG
SEQRES 160 B 2695  LEU ILE SER ARG GLU PHE ASN HIS ALA GLY ASN ARG VAL
SEQRES 161 B 2695  THR VAL GLU ILE GLY ASP HIS GLU VAL ASP VAL SER GLY
SEQRES 162 B 2695  ASP PHE LYS LEU PHE ILE HIS SER CYS ASP PRO SER GLY
SEQRES 163 B 2695  ASP ILE PRO ILE PHE LEU ARG SER ARG VAL ARG LEU VAL
SEQRES 164 B 2695  HIS PHE VAL THR ASN LYS GLU SER ILE GLU THR ARG ILE
SEQRES 165 B 2695  PHE ASP ILE THR LEU THR GLU GLU ASN ALA GLU MET GLN
SEQRES 166 B 2695  ARG LYS ARG GLU ASP LEU ILE LYS LEU ASN THR GLU TYR
SEQRES 167 B 2695  LYS LEU LYS LEU LYS ASN LEU GLU LYS ARG LEU LEU GLU
SEQRES 168 B 2695  GLU LEU ASN ASN SER GLN GLY ASN MET LEU GLU ASN ASP
SEQRES 169 B 2695  GLU LEU MET VAL THR LEU ASN ASN LEU LYS LYS GLU ALA
SEQRES 170 B 2695  MET ASN ILE GLU LYS LYS LEU SER GLU SER GLU GLU PHE
SEQRES 171 B 2695  PHE PRO GLN PHE ASP ASN LEU VAL GLU GLU TYR SER ILE
SEQRES 172 B 2695  ILE GLY LYS HIS SER VAL LYS ILE PHE SER MET LEU GLU
SEQRES 173 B 2695  LYS PHE GLY GLN PHE HIS TRP PHE TYR GLY ILE SER ILE
SEQRES 174 B 2695  GLY GLN PHE LEU SER CYS PHE LYS ARG VAL PHE ILE LYS
SEQRES 175 B 2695  LYS SER ARG GLU THR ARG ALA ALA ARG THR ARG VAL ASP
SEQRES 176 B 2695  GLU ILE LEU TRP LEU LEU TYR GLN GLU VAL TYR CYS GLN
SEQRES 177 B 2695  PHE SER THR ALA LEU ASP LYS LYS PHE LYS MET ILE MET
SEQRES 178 B 2695  ALA MET THR MET PHE CYS LEU TYR LYS PHE ASP ILE GLU
SEQRES 179 B 2695  SER GLU GLN TYR LYS GLU ALA VAL LEU THR MET ILE GLY
SEQRES 180 B 2695  VAL LEU SER GLU SER SER ASP GLY VAL PRO LYS LEU THR
SEQRES 181 B 2695  VAL ASP THR ASN ASN ASP LEU ARG TYR LEU TRP ASP TYR
SEQRES 182 B 2695  VAL THR THR LYS SER TYR ILE SER ALA LEU ASN TRP PHE
SEQRES 183 B 2695  LYS ASN GLU PHE PHE VAL ASP GLU TRP ASN ILE ALA ASP
SEQRES 184 B 2695  VAL VAL ALA ASN SER ASP ASN ASN TYR PHE THR MET ALA
SEQRES 185 B 2695  SER GLU ARG ASP VAL ASP GLY THR PHE LYS LEU ILE GLU
SEQRES 186 B 2695  LEU ALA LYS ALA SER LYS GLU SER LEU LYS ILE ILE PRO
SEQRES 187 B 2695  LEU GLY SER ILE GLU ASN LEU ASN TYR ALA GLN GLU GLU
SEQRES 188 B 2695  ILE SER LYS SER LYS ILE GLU GLY GLY TRP ILE LEU LEU
SEQRES 189 B 2695  GLN ASN ILE GLN MET SER LEU SER TRP VAL LYS THR TYR
SEQRES 190 B 2695  LEU HIS LYS HIS VAL GLU GLU THR LYS ALA ALA GLU GLU
SEQRES 191 B 2695  HIS GLU LYS PHE LYS MET PHE MET THR CYS HIS LEU THR
SEQRES 192 B 2695  GLY ASP LYS LEU PRO ALA PRO LEU LEU GLN ARG THR ASP
SEQRES 193 B 2695  ARG PHE VAL TYR GLU ASP ILE PRO GLY ILE LEU ASP THR
SEQRES 194 B 2695  VAL LYS ASP LEU TRP GLY SER GLN PHE PHE THR GLY LYS
SEQRES 195 B 2695  ILE SER GLY VAL TRP SER VAL TYR CYS THR PHE LEU LEU
SEQRES 196 B 2695  SER TRP PHE HIS ALA LEU ILE THR ALA ARG THR ARG LEU
SEQRES 197 B 2695  VAL PRO HIS GLY PHE SER LYS LYS TYR TYR PHE ASN ASP
SEQRES 198 B 2695  CYS ASP PHE GLN PHE ALA SER VAL TYR LEU GLU ASN VAL
SEQRES 199 B 2695  LEU ALA THR ASN SER THR ASN ASN ILE PRO TRP ALA GLN
SEQRES 200 B 2695  VAL ARG ASP HIS ILE ALA THR ILE VAL TYR GLY GLY LYS
SEQRES 201 B 2695  ILE ASP GLU GLU LYS ASP LEU GLU VAL VAL ALA LYS LEU
SEQRES 202 B 2695  CYS ALA HIS VAL PHE CYS GLY SER ASP ASN LEU GLN ILE
SEQRES 203 B 2695  VAL PRO GLY VAL ARG ILE PRO GLN PRO LEU LEU GLN GLN
SEQRES 204 B 2695  SER GLU GLU GLU GLU ARG ALA ARG LEU THR ALA ILE LEU
SEQRES 205 B 2695  SER ASN THR ILE GLU PRO ALA ASP SER LEU SER SER TRP
SEQRES 206 B 2695  LEU GLN LEU PRO ARG GLU SER ILE LEU ASN TYR GLU ARG
SEQRES 207 B 2695  LEU GLN ALA LYS GLU VAL ALA SER SER THR GLU GLN LEU
SEQRES 208 B 2695  LEU GLN GLU MET
HET    ATP  A5400      31
HET    ADP  A5401      27
HET    ADP  A5402      27
HET    SO4  A5403       5
HET     MG  A5404       1
HET    ATP  B5400      31
HET    ADP  B5401      27
HET    ADP  B5402      27
HET    SO4  B5403       5
HET     MG  B5404       1
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM     SO4 SULFATE ION
HETNAM      MG MAGNESIUM ION
FORMUL   3  ATP    2(C10 H16 N5 O13 P3)
FORMUL   4  ADP    4(C10 H15 N5 O10 P2)
FORMUL   5  SO4    2(O4 S 2-)
FORMUL   6   MG    2(MG 2+)
HELIX    1   1 GLN A   14  TYR A   22  1                                   9
HELIX    2   2 GLY A   37  LYS A   43  1                                   7
HELIX    3   3 SER A   67  ASP A   76  1                                  10
HELIX    4   4 PRO A   85  ARG A  107  1                                  23
HELIX    5   5 PHE A  114  ARG A  135  1                                  22
HELIX    6   6 HIS A  149  MET A  164  1                                  16
HELIX    7   7 PRO A  173  ALA A  184  1                                  12
HELIX    8   8 PRO A  186  LEU A  192  1                                   7
HELIX    9   9 VAL A 1366  TRP A 1378  1                                  13
HELIX   10  10 TRP A 1398  ALA A 1417  1                                  20
HELIX   11  11 GLU A 1425  ILE A 1458  1                                  34
HELIX   12  12 ASP A 1464  PHE A 1468  1                                   5
HELIX   13  13 PRO A 1470  PHE A 1491  1                                  22
HELIX   14  14 PHE A 1505  GLN A 1533  1                                  29
HELIX   15  15 PHE A 1537  LEU A 1540  1                                   4
HELIX   16  16 ASN A 1542  GLY A 1550  1                                   9
HELIX   17  17 VAL A 1558  PHE A 1566  1                                   9
HELIX   18  18 ALA A 1604  LYS A 1631  1                                  28
HELIX   19  19 ILE A 1636  VAL A 1640  1                                   5
HELIX   20  20 PHE A 1645  THR A 1666  1                                  22
HELIX   21  21 PHE A 1669  ASN A 1688  1                                  20
HELIX   22  22 ASP A 1692  ASN A 1717  1                                  26
HELIX   23  23 LYS A 1721  LYS A 1730  1                                  10
HELIX   24  24 PRO A 1773  HIS A 1787  1                                  15
HELIX   25  25 LYS A 1802  GLN A 1811  1                                  10
HELIX   26  26 TYR A 1828  ILE A 1841  1                                  14
HELIX   27  27 GLU A 1855  VAL A 1874  1                                  20
HELIX   28  28 GLU A 1910  LYS A 1913  1                                   4
HELIX   29  29 SER A 1926  GLY A 1938  1                                  13
HELIX   30  30 SER A 1942  LYS A 1959  1                                  18
HELIX   31  31 LEU A 1970  GLU A 1986  1                                  17
HELIX   32  32 GLU A 1991  SER A 2005  1                                  15
HELIX   33  33 ASP A 2008  ILE A 2021  1                                  14
HELIX   34  34 ALA A 2033  SER A 2045  1                                  13
HELIX   35  35 GLU A 2051  THR A 2066  1                                  16
HELIX   36  36 LYS A 2080  PHE A 2094  1                                  15
HELIX   37  37 LYS A 2111  LEU A 2114  1                                   4
HELIX   38  38 LEU A 2129  ASP A 2140  1                                  12
HELIX   39  39 PRO A 2160  GLU A 2164  1                                   5
HELIX   40  40 MET A 2166  LEU A 2170  1                                   5
HELIX   41  41 PRO A 2204  ARG A 2209  1                                   6
HELIX   42  42 ILE A 2222  ASP A 2238  1                                  17
HELIX   43  43 MET A 2243  SER A 2256  1                                  14
HELIX   44  44 MET A 2259  ASN A 2270  1                                  12
HELIX   45  45 THR A 2280  SER A 2297  1                                  18
HELIX   46  46 ASP A 2307  ALA A 2327  1                                  21
HELIX   47  47 GLU A 2333  TYR A 2345  1                                  13
HELIX   48  48 ILE A 2395  SER A 2410  1                                  16
HELIX   49  49 LYS A 2424  ARG A 2433  1                                  10
HELIX   50  50 THR A 2451  HIS A 2459  1                                   9
HELIX   51  51 ASN A 2501  GLU A 2511  1                                  11
HELIX   52  52 GLU A 2548  THR A 2551  1                                   4
HELIX   53  53 SER A 2566  ILE A 2578  1                                  13
HELIX   54  54 THR A 2589  ARG A 2606  1                                  18
HELIX   55  55 PRO A 2619  ASN A 2634  1                                  16
HELIX   56  56 LEU A 2641  PHE A 2656  1                                  16
HELIX   57  57 LYS A 2664  TYR A 2680  1                                  17
HELIX   58  58 LYS A 2709  GLU A 2726  1                                  18
HELIX   59  59 GLU A 2736  LYS A 2750  1                                  15
HELIX   60  60 LYS A 2766  LEU A 2776  1                                  11
HELIX   61  61 LEU A 2792  SER A 2807  1                                  16
HELIX   62  62 THR A 2825  ALA A 2836  1                                  12
HELIX   63  63 GLU A 2847  LEU A 2863  1                                  17
HELIX   64  64 GLU A 2870  ASN A 2884  1                                  15
HELIX   65  65 ASN A 2897  SER A 2904  1                                   8
HELIX   66  66 PRO A 2906  ARG A 2911  1                                   6
HELIX   67  67 THR A 2922  MET A 2932  1                                  11
HELIX   68  68 ILE A 2961  MET A 2980  1                                  20
HELIX   69  69 TYR A 2991  SER A 3027  1                                  37
HELIX   70  70 THR A 3300  TRP A 3306  1                                   7
HELIX   71  71 THR A 3309  TYR A 3333  1                                  25
HELIX   72  72 GLU A 3339  LYS A 3355  1                                  17
HELIX   73  73 PHE A 3366  LEU A 3370  1                                   5
HELIX   74  74 LEU A 3373  CYS A 3382  1                                  10
HELIX   75  75 ASP A 3388  ASN A 3399  1                                  12
HELIX   76  76 MET A 3414  TYR A 3422  1                                   9
HELIX   77  77 PHE A 3436  ARG A 3445  1                                  10
HELIX   78  78 SER A 3463  ILE A 3466  1                                   4
HELIX   79  79 ILE A 3507  ARG A 3512  1                                   6
HELIX   80  80 GLU A 3523  THR A 3535  1                                  13
HELIX   81  81 ALA A 3539  ASN A 3572  1                                  34
HELIX   82  82 ASN A 3580  PHE A 3638  1                                  59
HELIX   83  83 ILE A 3646  ARG A 3655  1                                  10
HELIX   84  84 ARG A 3670  PHE A 3686  1                                  17
HELIX   85  85 LYS A 3692  ILE A 3710  1                                  19
HELIX   86  86 GLU A 3713  LEU A 3726  1                                  14
HELIX   87  87 ASP A 3743  THR A 3752  1                                  10
HELIX   88  88 TYR A 3756  ASN A 3765  1                                  10
HELIX   89  89 ILE A 3774  ASN A 3780  1                                   7
HELIX   90  90 THR A 3797  LYS A 3805  1                                   9
HELIX   91  91 ILE A 3819  GLU A 3835  1                                  17
HELIX   92  92 LEU A 3848  GLU A 3861  1                                  14
HELIX   93  93 ALA A 3886  ARG A 3891  1                                   6
HELIX   94  94 ILE A 3903  SER A 3913  1                                  11
HELIX   95  95 VAL A 3923  ARG A 3944  1                                  22
HELIX   96  96 ASP A 3958  THR A 3974  1                                  17
HELIX   97  97 TRP A 3982  THR A 3991  1                                  10
HELIX   98  98 GLU A 4001  VAL A 4014  1                                  14
HELIX   99  99 GLU A 4038  ASN A 4051  1                                  14
HELIX  100 100 SER A 4058  SER A 4061  1                                   4
HELIX  101 101 ARG A 4067  GLN A 4090  1                                  24
HELIX  102 102 GLN B   14  LEU B   23  1                                  10
HELIX  103 103 GLY B   37  LYS B   43  1                                   7
HELIX  104 104 SER B   67  ASP B   76  1                                  10
HELIX  105 105 PRO B   85  ALA B  109  1                                  25
HELIX  106 106 PHE B  114  ARG B  135  1                                  22
HELIX  107 107 PRO B  150  MET B  164  1                                  15
HELIX  108 108 PRO B  173  ALA B  184  1                                  12
HELIX  109 109 PRO B  186  LEU B  192  1                                   7
HELIX  110 110 VAL B 1366  TRP B 1378  1                                  13
HELIX  111 111 TRP B 1398  SER B 1414  1                                  17
HELIX  112 112 PHE B 1424  ILE B 1458  1                                  35
HELIX  113 113 ASP B 1464  PHE B 1468  1                                   5
HELIX  114 114 PRO B 1470  PHE B 1491  1                                  22
HELIX  115 115 PHE B 1505  GLN B 1533  1                                  29
HELIX  116 116 PHE B 1537  LEU B 1540  1                                   4
HELIX  117 117 ASN B 1542  GLY B 1550  1                                   9
HELIX  118 118 VAL B 1558  PHE B 1566  1                                   9
HELIX  119 119 ALA B 1604  LYS B 1631  1                                  28
HELIX  120 120 ILE B 1636  VAL B 1640  1                                   5
HELIX  121 121 PHE B 1645  THR B 1666  1                                  22
HELIX  122 122 PHE B 1669  ASN B 1688  1                                  20
HELIX  123 123 ASP B 1692  ASN B 1717  1                                  26
HELIX  124 124 LYS B 1721  LYS B 1730  1                                  10
HELIX  125 125 PRO B 1773  HIS B 1787  1                                  15
HELIX  126 126 LYS B 1802  GLN B 1811  1                                  10
HELIX  127 127 TYR B 1828  ILE B 1841  1                                  14
HELIX  128 128 GLU B 1855  VAL B 1874  1                                  20
HELIX  129 129 GLU B 1910  LYS B 1913  1                                   4
HELIX  130 130 SER B 1926  GLY B 1938  1                                  13
HELIX  131 131 SER B 1942  LYS B 1959  1                                  18
HELIX  132 132 LEU B 1970  GLU B 1986  1                                  17
HELIX  133 133 GLU B 1991  VAL B 2001  1                                  11
HELIX  134 134 ASP B 2008  ILE B 2021  1                                  14
HELIX  135 135 ALA B 2033  SER B 2045  1                                  13
HELIX  136 136 GLU B 2051  THR B 2066  1                                  16
HELIX  137 137 LYS B 2080  PHE B 2094  1                                  15
HELIX  138 138 LYS B 2111  LEU B 2114  1                                   4
HELIX  139 139 LEU B 2129  ASP B 2140  1                                  12
HELIX  140 140 PRO B 2160  GLU B 2164  1                                   5
HELIX  141 141 MET B 2166  LEU B 2170  1                                   5
HELIX  142 142 PRO B 2204  ARG B 2209  1                                   6
HELIX  143 143 ILE B 2222  ASP B 2238  1                                  17
HELIX  144 144 MET B 2243  SER B 2256  1                                  14
HELIX  145 145 MET B 2259  ASN B 2270  1                                  12
HELIX  146 146 THR B 2280  SER B 2297  1                                  18
HELIX  147 147 ASP B 2307  ALA B 2327  1                                  21
HELIX  148 148 GLU B 2333  TYR B 2345  1                                  13
HELIX  149 149 ILE B 2395  SER B 2410  1                                  16
HELIX  150 150 LYS B 2424  ASN B 2434  1                                  11
HELIX  151 151 THR B 2451  HIS B 2459  1                                   9
HELIX  152 152 ASN B 2501  GLU B 2511  1                                  11
HELIX  153 153 GLU B 2548  THR B 2551  1                                   4
HELIX  154 154 SER B 2566  ILE B 2578  1                                  13
HELIX  155 155 THR B 2589  ARG B 2606  1                                  18
HELIX  156 156 PRO B 2619  ASN B 2634  1                                  16
HELIX  157 157 LEU B 2641  PHE B 2656  1                                  16
HELIX  158 158 LYS B 2664  TYR B 2680  1                                  17
HELIX  159 159 LYS B 2709  GLU B 2726  1                                  18
HELIX  160 160 GLU B 2736  LYS B 2750  1                                  15
HELIX  161 161 LYS B 2766  LEU B 2776  1                                  11
HELIX  162 162 LEU B 2792  LEU B 2808  1                                  17
HELIX  163 163 THR B 2825  ALA B 2836  1                                  12
HELIX  164 164 GLU B 2847  LEU B 2863  1                                  17
HELIX  165 165 GLU B 2870  ASN B 2884  1                                  15
HELIX  166 166 ASN B 2897  SER B 2904  1                                   8
HELIX  167 167 PRO B 2906  ARG B 2911  1                                   6
HELIX  168 168 THR B 2922  MET B 2932  1                                  11
HELIX  169 169 ILE B 2961  MET B 2980  1                                  20
HELIX  170 170 TYR B 2991  SER B 3027  1                                  37
HELIX  171 171 THR B 3300  ARG B 3305  1                                   6
HELIX  172 172 LEU B 3307  TYR B 3333  1                                  27
HELIX  173 173 GLU B 3339  LYS B 3355  1                                  17
HELIX  174 174 PHE B 3366  LEU B 3370  1                                   5
HELIX  175 175 LEU B 3373  CYS B 3382  1                                  10
HELIX  176 176 ASP B 3388  ASN B 3399  1                                  12
HELIX  177 177 MET B 3414  TYR B 3422  1                                   9
HELIX  178 178 PHE B 3436  ARG B 3445  1                                  10
HELIX  179 179 SER B 3463  ILE B 3466  1                                   4
HELIX  180 180 ILE B 3507  ARG B 3512  1                                   6
HELIX  181 181 GLU B 3523  GLU B 3537  1                                  15
HELIX  182 182 ALA B 3539  ASN B 3572  1                                  34
HELIX  183 183 ASN B 3580  PHE B 3638  1                                  59
HELIX  184 184 ILE B 3646  LYS B 3654  1                                   9
HELIX  185 185 ARG B 3670  PHE B 3686  1                                  17
HELIX  186 186 LYS B 3692  ILE B 3710  1                                  19
HELIX  187 187 GLU B 3713  LEU B 3726  1                                  14
HELIX  188 188 ASP B 3743  THR B 3752  1                                  10
HELIX  189 189 TYR B 3756  ASN B 3765  1                                  10
HELIX  190 190 ILE B 3774  ASN B 3780  1                                   7
HELIX  191 191 THR B 3797  LYS B 3805  1                                   9
HELIX  192 192 ILE B 3819  GLU B 3835  1                                  17
HELIX  193 193 SER B 3849  THR B 3853  1                                   5
HELIX  194 194 TYR B 3854  GLU B 3861  1                                   8
HELIX  195 195 ALA B 3886  ARG B 3891  1                                   6
HELIX  196 196 ILE B 3903  SER B 3913  1                                  11
HELIX  197 197 VAL B 3923  ARG B 3944  1                                  22
HELIX  198 198 ASP B 3958  THR B 3974  1                                  17
HELIX  199 199 TRP B 3982  THR B 3991  1                                  10
HELIX  200 200 GLU B 4001  VAL B 4014  1                                  14
HELIX  201 201 GLU B 4038  ASN B 4051  1                                  14
HELIX  202 202 SER B 4058  SER B 4061  1                                   4
HELIX  203 203 ARG B 4067  GLN B 4090  1                                  24
SHEET    1   1 1 ILE A   3  TRP A   7  0
SHEET    2   2 1 GLU A  28  TYR A  32  0
SHEET    3   3 1 TYR A  56  ILE A  58  0
SHEET    4   4 1 LYS A  63  THR A  65  0
SHEET    5   5 1 GLU A1384  GLU A1387  0
SHEET    6   6 1 LYS A1393  ARG A1396  0
SHEET    7   7 1 ILE A1569  PHE A1574  0
SHEET    8   8 1 PHE A1578  SER A1584  0
SHEET    9   9 1 VAL A1589  GLU A1597  0
SHEET   10  10 1 LYS A1733  GLN A1736  0
SHEET   11  11 1 VAL A1747  GLN A1751  0
SHEET   12  12 1 TYR A1754  GLN A1757  0
SHEET   13  13 1 GLY A1791  PHE A1795  0
SHEET   14  14 1 VAL A1818  ASN A1821  0
SHEET   15  15 1 TRP A1844  ASP A1848  0
SHEET   16  16 1 HIS A1878  LEU A1881  0
SHEET   17  17 1 GLU A1884  PRO A1887  0
SHEET   18  18 1 ALA A1893  LEU A1898  0
SHEET   19  19 1 PHE A1916  SER A1920  0
SHEET   20  20 1 ALA A2069  GLY A2074  0
SHEET   21  21 1 ASN A2099  ILE A2104  0
SHEET   22  22 1 SER A2117  LEU A2119  0
SHEET   23  23 1 LEU A2123  ARG A2126  0
SHEET   24  24 1 ARG A2149  PHE A2154  0
SHEET   25  25 1 LYS A2174  LEU A2178  0
SHEET   26  26 1 GLU A2182  ILE A2186  0
SHEET   27  27 1 ARG A2191  THR A2196  0
SHEET   28  28 1 GLY A2211  PHE A2215  0
SHEET   29  29 1 GLY A2413  CYS A2417  0
SHEET   30  30 1 ASP A2439  ASN A2444  0
SHEET   31  31 1 VAL A2465  THR A2467  0
SHEET   32  32 1 LEU A2471  LEU A2474  0
SHEET   33  33 1 LEU A2482  ASP A2487  0
SHEET   34  34 1 GLY A2514  TRP A2516  0
SHEET   35  35 1 TRP A2523  ILE A2526  0
SHEET   36  36 1 ILE A2529  CYS A2535  0
SHEET   37  37 1 ALA A2554  TYR A2558  0
SHEET   38  38 1 PHE A2696  SER A2697  0
SHEET   39  39 1 LYS A2705  GLU A2706  0
SHEET   40  40 1 GLY A2754  ILE A2759  0
SHEET   41  41 1 LYS A2780  GLN A2783  0
SHEET   42  42 1 THR A2813  ASP A2818  0
SHEET   43  43 1 HIS A2886  ILE A2891  0
SHEET   44  44 1 ILE A2913  TRP A2916  0
SHEET   45  45 1 PRO A3405  LEU A3408  0
SHEET   46  46 1 THR A3426  LEU A3429  0
SHEET   47  47 1 VAL A3449  ILE A3452  0
SHEET   48  48 1 PHE A3470  ALA A3473  0
SHEET   49  49 1 ARG A3476  ILE A3481  0
SHEET   50  50 1 HIS A3484  VAL A3488  0
SHEET   51  51 1 LYS A3493  SER A3498  0
SHEET   52  52 1 ARG A3514  HIS A3517  0
SHEET   53  53 1 TYR A3785  SER A3790  0
SHEET   54  54 1 LYS A3812  PRO A3815  0
SHEET   55  55 1 ILE A3839  GLN A3842  0
SHEET   56  56 1 MET A3873  HIS A3878  0
SHEET   57  57 1 ASP A3893  TYR A3897  0
SHEET   58  58 1 ILE B   3  TRP B   7  0
SHEET   59  59 1 GLU B  28  TYR B  32  0
SHEET   60  60 1 TYR B  56  ILE B  58  0
SHEET   61  61 1 LYS B  63  THR B  65  0
SHEET   62  62 1 GLU B1384  GLU B1387  0
SHEET   63  63 1 LYS B1393  ARG B1396  0
SHEET   64  64 1 ILE B1569  PHE B1574  0
SHEET   65  65 1 PHE B1578  SER B1584  0
SHEET   66  66 1 VAL B1589  GLU B1597  0
SHEET   67  67 1 LYS B1733  GLN B1736  0
SHEET   68  68 1 VAL B1747  GLN B1751  0
SHEET   69  69 1 TYR B1754  GLN B1757  0
SHEET   70  70 1 GLY B1791  PHE B1795  0
SHEET   71  71 1 VAL B1818  ASN B1821  0
SHEET   72  72 1 TRP B1844  ASP B1848  0
SHEET   73  73 1 HIS B1878  LEU B1881  0
SHEET   74  74 1 GLU B1884  PRO B1887  0
SHEET   75  75 1 ALA B1893  LEU B1898  0
SHEET   76  76 1 PHE B1916  SER B1920  0
SHEET   77  77 1 ALA B2069  GLY B2074  0
SHEET   78  78 1 ASN B2099  ILE B2104  0
SHEET   79  79 1 SER B2117  LEU B2119  0
SHEET   80  80 1 LEU B2123  ARG B2126  0
SHEET   81  81 1 ARG B2149  PHE B2154  0
SHEET   82  82 1 LYS B2174  LEU B2178  0
SHEET   83  83 1 GLU B2182  ILE B2186  0
SHEET   84  84 1 PHE B2190  THR B2196  0
SHEET   85  85 1 GLY B2211  PHE B2215  0
SHEET   86  86 1 GLY B2413  CYS B2417  0
SHEET   87  87 1 ASP B2439  ASN B2444  0
SHEET   88  88 1 VAL B2465  THR B2467  0
SHEET   89  89 1 LEU B2471  LEU B2473  0
SHEET   90  90 1 LEU B2482  ASP B2487  0
SHEET   91  91 1 GLY B2514  TRP B2516  0
SHEET   92  92 1 TRP B2523  THR B2525  0
SHEET   93  93 1 ILE B2529  CYS B2535  0
SHEET   94  94 1 ALA B2554  TYR B2558  0
SHEET   95  95 1 PHE B2696  SER B2697  0
SHEET   96  96 1 LYS B2705  GLU B2706  0
SHEET   97  97 1 GLY B2754  ILE B2759  0
SHEET   98  98 1 LYS B2780  GLN B2783  0
SHEET   99  99 1 THR B2813  ASP B2818  0
SHEET  100 100 1 HIS B2886  ILE B2891  0
SHEET  101 101 1 ILE B2913  TRP B2916  0
SHEET  102 102 1 VAL B3404  LEU B3408  0
SHEET  103 103 1 THR B3426  LEU B3429  0
SHEET  104 104 1 VAL B3449  ILE B3452  0
SHEET  105 105 1 PHE B3470  ALA B3473  0
SHEET  106 106 1 ARG B3476  ILE B3481  0
SHEET  107 107 1 HIS B3484  VAL B3488  0
SHEET  108 108 1 LYS B3493  SER B3498  0
SHEET  109 109 1 VAL B3513  HIS B3517  0
SHEET  110 110 1 TYR B3785  SER B3790  0
SHEET  111 111 1 LYS B3812  PRO B3815  0
SHEET  112 112 1 ILE B3839  GLN B3842  0
SHEET  113 113 1 MET B3873  HIS B3878  0
SHEET  114 114 1 ASP B3893  TYR B3897  0
CISPEP   1 LEU A   54    PRO A   55          0        10.06
CISPEP   2 TRP A  200    PRO A  201          0         3.49
CISPEP   3 VAL A 3946    PRO A 3947          0         6.69
CISPEP   4 LEU B   54    PRO B   55          0         0.52
CISPEP   5 TRP B  200    PRO B  201          0         6.24
CISPEP   6 VAL B 3946    PRO B 3947          0         8.57
SITE     1 AC1 18 SER A2048  GLY A2077  CYS A2078  GLY A2079
SITE     2 AC1 18 LYS A2080  THR A2081  ALA A2082  GLU A2195
SITE     3 AC1 18 VAL A2219  CYS A2220  SER A2224  LYS A2225
SITE     4 AC1 18 HIS A2228  ARG A2507  GLU A2511  ARG A2549
SITE     5 AC1 18 ARG A2552   MG B5404
SITE     1 AC2 14 ILE A2392  PRO A2419  PRO A2420  GLY A2421
SITE     2 AC2 14 SER A2422  GLY A2423  LYS A2424  THR A2425
SITE     3 AC2 14 MET A2426  ILE A2570  TYR A2571  PRO A2619
SITE     4 AC2 14 ARG A2620  THR A2623
SITE     1 AC3 10 MET A2732  VAL A2733  HIS A2735  ARG A2763
SITE     2 AC3 10 THR A2764  GLY A2765  LYS A2766  THR A2767
SITE     3 AC3 10 ILE A2768  ARG A3512
SITE     1 AC4  6 GLY A1799  THR A1800  GLY A1801  LYS A1802
SITE     2 AC4  6 THR A1803  GLU A1849
SITE     1 AC5  5 LYS B2080  THR B2081  ASP B2155  GLU B2195
SITE     2 AC5  5 ATP B5400
SITE     1 AC6 19  MG A5404  SER B2048  GLY B2077  CYS B2078
SITE     2 AC6 19 GLY B2079  LYS B2080  THR B2081  ALA B2082
SITE     3 AC6 19 ASP B2155  GLU B2195  VAL B2219  CYS B2220
SITE     4 AC6 19 SER B2224  LYS B2225  HIS B2228  ARG B2507
SITE     5 AC6 19 GLU B2511  ARG B2549  ARG B2552
SITE     1 AC7 13 ILE B2390  ILE B2392  PRO B2419  PRO B2420
SITE     2 AC7 13 GLY B2421  GLY B2423  LYS B2424  THR B2425
SITE     3 AC7 13 MET B2426  ILE B2570  TYR B2571  ARG B2620
SITE     4 AC7 13 THR B2623
SITE     1 AC8  9 MET B2732  VAL B2733  ARG B2763  THR B2764
SITE     2 AC8  9 GLY B2765  LYS B2766  THR B2767  ILE B2768
SITE     3 AC8  9 ARG B3512
SITE     1 AC9  6 ALA B1798  GLY B1799  THR B1800  GLY B1801
SITE     2 AC9  6 LYS B1802  THR B1803
SITE     1 BC1  5 THR A2081  ASP A2155  GLU A2195  GLU A2511
SITE     2 BC1  5 ATP A5400
CRYST1  174.886  119.175  193.974  90.00  90.18  90.00 P 1 21 1      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      0.005718  0.000000  0.000018        0.00000
SCALE2      0.000000  0.008391  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005155        0.00000
      
PROCHECK
Go to PROCHECK summary
 References