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PDBsum entry 1o04

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
1o04
Jmol
Contents
Protein chain
(+ 2 more) 494 a.a. *
Ligands
NAD ×8
GAI ×18
EDO ×32
Metals
_NA ×8
_MG ×8
Waters ×5025
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          20-FEB-03   1O04
TITLE     CYS302SER MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE
TITLE    2 DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 FRAGMENT: COMPLETE MATURE SEQUENCE (DOES NOT CONTAIN
COMPND   5 MITOCHONDRIAL LEADER SEQUENCE).;
COMPND   6 SYNONYM: ALDH CLASS 2, ALDHI, ALDH-E2;
COMPND   7 EC: 1.2.1.3;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: ALDH2 OR ALDM;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET7-7
KEYWDS    ALDH, NAD, NADH, ISOMERIZATION, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.J.PEREZ-MILLER,T.D.HURLEY
REVDAT   2   24-FEB-09 1O04    1       VERSN
REVDAT   1   24-JUN-03 1O04    0
JRNL        AUTH   S.J.PEREZ-MILLER,T.D.HURLEY
JRNL        TITL   COENZYME ISOMERIZATION IS INTEGRAL TO CATALYSIS IN
JRNL        TITL 2 ALDEHYDE DEHYDROGENASE
JRNL        REF    BIOCHEMISTRY                  V.  42  7100 2003
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12795606
JRNL        DOI    10.1021/BI034182W
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.42 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9
REMARK   3   NUMBER OF REFLECTIONS             : 648549
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) : 0.147
REMARK   3   R VALUE            (WORKING SET) : 0.145
REMARK   3   FREE R VALUE                     : 0.171
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 34234
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) : 1.42
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.46
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 36402
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550
REMARK   3   BIN FREE R VALUE SET COUNT          : 1907
REMARK   3   BIN FREE R VALUE                    : 0.2880
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 30568
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 568
REMARK   3   SOLVENT ATOMS            : 5025
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 10.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.89
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.40000
REMARK   3    B22 (A**2) : -0.09000
REMARK   3    B33 (A**2) : -0.31000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.057
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.059
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.036
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.942
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 31798 ; 0.014 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 43158 ; 1.501 ; 1.962
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3992 ; 6.108 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4720 ; 0.097 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24360 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 16569 ; 0.198 ; 0.200
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):  3825 ; 0.128 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    32 ; 0.052 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    91 ; 0.227 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):   119 ; 0.184 ; 0.200
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): 19782 ; 1.314 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31728 ; 2.092 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12016 ; 3.237 ; 6.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11430 ; 5.129 ; 8.000
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 : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: MLKF REFINEMENT
REMARK   4
REMARK   4 1O04 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-03.
REMARK 100 THE RCSB ID CODE IS RCSB018407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 683580
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.420
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.47
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.43900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1CW3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 34.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ACES, PEG 6000, GUANIDINE HCL,
REMARK 280  MGCL2, DTT., PH 6.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-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       70.60550
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.60000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.24350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.60000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.60550
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.24350
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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     SER A     1
REMARK 465     ALA A     2
REMARK 465     ALA A     3
REMARK 465     ALA A     4
REMARK 465     THR A     5
REMARK 465     GLN A     6
REMARK 465     SER B     1
REMARK 465     ALA B     2
REMARK 465     ALA B     3
REMARK 465     ALA B     4
REMARK 465     THR B     5
REMARK 465     GLN B     6
REMARK 465     SER C     1
REMARK 465     ALA C     2
REMARK 465     ALA C     3
REMARK 465     ALA C     4
REMARK 465     THR C     5
REMARK 465     GLN C     6
REMARK 465     SER D     1
REMARK 465     ALA D     2
REMARK 465     ALA D     3
REMARK 465     ALA D     4
REMARK 465     THR D     5
REMARK 465     GLN D     6
REMARK 465     SER E     1
REMARK 465     ALA E     2
REMARK 465     ALA E     3
REMARK 465     ALA E     4
REMARK 465     THR E     5
REMARK 465     GLN E     6
REMARK 465     SER F     1
REMARK 465     ALA F     2
REMARK 465     ALA F     3
REMARK 465     ALA F     4
REMARK 465     THR F     5
REMARK 465     GLN F     6
REMARK 465     SER G     1
REMARK 465     ALA G     2
REMARK 465     ALA G     3
REMARK 465     ALA G     4
REMARK 465     THR G     5
REMARK 465     GLN G     6
REMARK 465     SER H     1
REMARK 465     ALA H     2
REMARK 465     ALA H     3
REMARK 465     ALA H     4
REMARK 465     THR H     5
REMARK 465     GLN H     6
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    ASP A 239   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 282   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES
REMARK 500    ASP A 336   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ASP A 437   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG B  86   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG B 130   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP B 336   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES
REMARK 500    ARG C  97   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP C 282   CB  -  CG  -  OD2 ANGL. DEV. =   8.5 DEGREES
REMARK 500    ARG D  86   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASP D 282   CB  -  CG  -  OD2 ANGL. DEV. =   7.6 DEGREES
REMARK 500    ARG E  86   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP E 239   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP E 282   CB  -  CG  -  OD2 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ASP E 336   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP E 437   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG F  86   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ASP F 137   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP F 282   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP F 437   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP G 282   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP H  30   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG H  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ASP H 282   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES
REMARK 500    ASP H 336   CB  -  CG  -  OD2 ANGL. DEV. =   8.6 DEGREES
REMARK 500    ASP H 437   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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    ASN A  20       25.61   -149.38
REMARK 500    THR A 227      -82.41    -97.35
REMARK 500    SER A 260     -101.30   -101.86
REMARK 500    LEU A 269     -154.43   -116.80
REMARK 500    TYR A 379       58.91   -106.41
REMARK 500    LYS A 469     -133.90     54.74
REMARK 500    LEU A 477      163.92     70.99
REMARK 500    GLN A 497      111.15   -160.65
REMARK 500    ASN B  20       24.70   -149.05
REMARK 500    VAL B 120      -68.46   -107.27
REMARK 500    THR B 227      -78.34   -100.60
REMARK 500    SER B 260     -102.69   -107.99
REMARK 500    LEU B 269     -154.43   -118.18
REMARK 500    TYR B 379       56.13    -92.14
REMARK 500    LYS B 469     -132.24     50.53
REMARK 500    LEU B 477      162.27     73.70
REMARK 500    ASN C  20       28.63   -152.48
REMARK 500    GLN C  21     -169.65   -124.58
REMARK 500    THR C 227      -81.69    -99.07
REMARK 500    SER C 260     -105.23   -106.97
REMARK 500    LEU C 269     -153.69   -115.47
REMARK 500    ASP C 376      -71.53    -69.28
REMARK 500    LYS C 469     -132.86     57.42
REMARK 500    LEU C 477      165.12     74.50
REMARK 500    GLN C 497      114.08   -160.50
REMARK 500    ASN D  20       25.17   -146.65
REMARK 500    THR D 227      -80.18    -95.79
REMARK 500    SER D 260     -100.83   -103.62
REMARK 500    LEU D 269     -156.24   -116.58
REMARK 500    TYR D 379       58.92    -96.59
REMARK 500    LYS D 469     -134.95     54.84
REMARK 500    LEU D 477      163.47     69.59
REMARK 500    GLN D 497      108.09   -163.26
REMARK 500    ASN E  20       24.70   -152.43
REMARK 500    VAL E 120      -69.38   -109.29
REMARK 500    THR E 227      -79.62   -101.82
REMARK 500    SER E 260      -99.87   -105.03
REMARK 500    LEU E 269     -156.73   -117.38
REMARK 500    TYR E 379       59.39   -104.05
REMARK 500    LYS E 469     -135.08     56.59
REMARK 500    LEU E 477      162.56     73.21
REMARK 500    GLN E 497      109.03   -160.34
REMARK 500    ASN F  20       25.85   -149.89
REMARK 500    THR F 227      -82.38    -99.91
REMARK 500    SER F 260      -98.71   -111.28
REMARK 500    LEU F 269     -154.14   -115.38
REMARK 500    LYS F 469     -132.86     54.50
REMARK 500    LEU F 477      163.39     72.40
REMARK 500    ASN G  20       26.58   -148.48
REMARK 500    VAL G 120      -69.04   -109.85
REMARK 500    THR G 227      -81.46   -102.26
REMARK 500    SER G 260     -100.69   -107.82
REMARK 500    LEU G 269     -156.80   -115.07
REMARK 500    LYS G 469     -134.41     56.41
REMARK 500    LEU G 477      163.80     72.06
REMARK 500    ASN H  20       24.55   -150.21
REMARK 500    VAL H 120      -71.16   -107.40
REMARK 500    THR H 197       59.59   -147.80
REMARK 500    THR H 227      -81.61   -100.31
REMARK 500    SER H 260     -101.15   -102.37
REMARK 500    LEU H 269     -154.81   -115.33
REMARK 500    TYR H 379       59.68    -95.11
REMARK 500    LYS H 469     -135.30     56.37
REMARK 500    LEU H 477      164.92     70.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH D7473        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH D7474        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH G4506        DISTANCE =  5.66 ANGSTROMS
REMARK 525    HOH G4507        DISTANCE =  5.74 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A6701  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD A6501   O2A
REMARK 620 2 HOH A7062   O    88.5
REMARK 620 3 HOH A7058   O    92.4 173.4
REMARK 620 4 HOH A7059   O   176.9  88.4  90.5
REMARK 620 5 HOH A7060   O    92.5  96.7  89.7  88.4
REMARK 620 6 HOH A7257   O    86.6  83.4  90.2  92.5 179.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A6601  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A7169   O
REMARK 620 2 ASP A 109   O    96.2
REMARK 620 3 VAL A  40   O    88.9 100.1
REMARK 620 4 ASP A 109   OD1 165.8  81.4 105.3
REMARK 620 5 GLN A 196   O    78.8  99.7 157.7  87.8
REMARK 620 6 THR A  39   OG1 120.0 138.9  99.5  58.7  71.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B6702  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD B6502   O2A
REMARK 620 2 HOH B7011   O    91.4
REMARK 620 3 HOH B7013   O    89.9  94.2
REMARK 620 4 HOH B7191   O    87.0 177.7  87.5
REMARK 620 5 HOH B7430   O   176.6  91.9  90.5  89.6
REMARK 620 6 HOH B7194   O    92.3  97.2 168.4  81.2  86.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B6602  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 109   O
REMARK 620 2 VAL B  40   O    98.7
REMARK 620 3 ASP B 109   OD1  83.6 107.3
REMARK 620 4 GLN B 196   O    99.2 157.4  88.4
REMARK 620 5 HOH B7433   O    92.5  88.7 163.9  76.8
REMARK 620 6 THR B  39   OG1 139.5 102.7  57.4  71.7 121.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C6703  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD C6503   O2A
REMARK 620 2 HOH C7257   O    92.9
REMARK 620 3 HOH C7000   O    86.8  86.4
REMARK 620 4 HOH C7223   O    88.9 174.0  88.0
REMARK 620 5 HOH C7220   O   178.8  87.6  92.2  90.5
REMARK 620 6 HOH C7221   O    91.7  94.3 178.4  91.4  89.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA C6603  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 109   O
REMARK 620 2 VAL C  40   O    99.6
REMARK 620 3 ASP C 109   OD1  81.8 105.9
REMARK 620 4 GLN C 196   O   100.9 156.2  88.8
REMARK 620 5 HOH C7317   O    92.4  89.2 164.5  78.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D6704  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD D6504   O2A
REMARK 620 2 HOH D7069   O    92.5
REMARK 620 3 HOH D7531   O    92.4  93.0
REMARK 620 4 HOH D7447   O    85.4 177.9  87.0
REMARK 620 5 HOH D7072   O    87.3  97.9 169.1  82.2
REMARK 620 6 HOH D7070   O   175.1  91.9  89.6  90.2  89.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA D6604  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 109   O
REMARK 620 2 ASP D 109   OD1  82.0
REMARK 620 3 VAL D  40   O    99.7 106.3
REMARK 620 4 GLN D 196   O    99.6  88.5 157.1
REMARK 620 5 HOH D7466   O    96.4 163.6  90.0  75.7
REMARK 620 6 THR D  39   OG1 137.8  56.9 100.8  72.4 120.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E6705  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD E6505   O2A
REMARK 620 2 HOH E2627   O    96.2
REMARK 620 3 HOH E2628   O   175.9  87.4
REMARK 620 4 HOH E4785   O    93.7  90.7  88.1
REMARK 620 5 HOH E2631   O    86.6  95.3  91.1 173.9
REMARK 620 6 HOH E2632   O    86.4 176.9  89.9  90.9  83.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA E6605  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 109   O
REMARK 620 2 ASP E 109   OD1  82.5
REMARK 620 3 HOH E3885   O    96.0 161.6
REMARK 620 4 VAL E  40   O   101.2 107.4  90.9
REMARK 620 5 GLN E 196   O    97.9  87.8  74.2 156.9
REMARK 620 6 THR E  39   OG1 139.3  58.1 118.1 100.0  73.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG F6706  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD F6506   O2A
REMARK 620 2 HOH F2815   O    84.7
REMARK 620 3 HOH F2833   O    88.2  88.7
REMARK 620 4 HOH F2834   O    95.3 179.2  92.1
REMARK 620 5 HOH F2814   O    92.1  81.9 170.6  97.2
REMARK 620 6 HOH F2813   O   175.3  91.1  89.4  88.9  89.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA F6606  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F2809   O
REMARK 620 2 ASP F 109   O    89.2
REMARK 620 3 VAL F  40   O    84.3 102.8
REMARK 620 4 ASP F 109   OD1 167.4  82.7 106.9
REMARK 620 5 GLN F 196   O    82.1  99.0 154.1  89.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG G6707  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD G6507   O2A
REMARK 620 2 HOH G4359   O    87.5
REMARK 620 3 HOH G3209   O    87.0  89.4
REMARK 620 4 HOH G4361   O    93.5  95.8 174.8
REMARK 620 5 HOH G4360   O   174.3  89.4  88.2  91.6
REMARK 620 6 HOH G3210   O    92.4 169.2  79.8  95.0  89.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA G6607  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G3200   O
REMARK 620 2 ASP G 109   O    92.7
REMARK 620 3 VAL G  40   O    89.4 100.8
REMARK 620 4 GLN G 196   O    73.1  97.0 155.5
REMARK 620 5 ASP G 109   OD1 162.4  83.1 108.2  90.4
REMARK 620 6 THR G  39   OG1 119.7 140.8 100.9  74.7  59.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H6708  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NAD H6508   O2A
REMARK 620 2 HOH H2235   O    95.9
REMARK 620 3 HOH H2230   O   173.9  90.1
REMARK 620 4 HOH H2227   O    90.0  93.7  88.1
REMARK 620 5 HOH H2231   O    91.0  94.1  90.1 172.0
REMARK 620 6 HOH H2228   O    85.6 177.9  88.4  84.8  87.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA H6608  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH H4701   O
REMARK 620 2 GLN H 196   O    81.8
REMARK 620 3 ASP H 109   OD1 165.4  87.5
REMARK 620 4 ASP H 109   O    90.5  97.7  81.1
REMARK 620 5 VAL H  40   O    89.3 158.0 104.2 102.4
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 6601
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 6602
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 6603
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 6604
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 6605
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 6606
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 6607
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 6608
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 6701
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 6702
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 6703
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 6704
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 6705
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 6706
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 6707
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 6708
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 6501
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 6502
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 6503
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 6504
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 6505
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 6506
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 6507
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 6508
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 6801
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 6811
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 6802
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 6812
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 6803
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 6813
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 6823
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 6804
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 6814
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 6805
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 6815
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 6806
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 6816
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 6826
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 6807
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 6817
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 6808
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 6818
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6901
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6911
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6921
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6941
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6902
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6912
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6922
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6942
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6903
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6913
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6923
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6943
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6963
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 6904
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 6914
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 6944
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 6905
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 6915
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 6925
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6906
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6916
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6926
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6946
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6956
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6966
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 6907
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 6917
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 6927
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 6908
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 6918
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 6928
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 6948
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CW3   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NAD+ AND MN2+
REMARK 900 RELATED ID: 1AG8   RELATED DB: PDB
REMARK 900 ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA (APO)
REMARK 900 RELATED ID: 1A4Z   RELATED DB: PDB
REMARK 900 ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEXED
REMARK 900 WITH NAD AND SM3+
REMARK 900 RELATED ID: 1NZW   RELATED DB: PDB
REMARK 900 CYS302SER MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE
REMARK 900 DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
REMARK 900 RELATED ID: 1NZX   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NAD+ IN THE PRESENCE OF LOW MG2+
REMARK 900 RELATED ID: 1NZZ   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NADH IN THE PRESENCE OF LOW MG2+
REMARK 900 RELATED ID: 1O00   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NAD+ AND MG2+ SHOWING DUAL NAD CONFORMATIONS
REMARK 900 RELATED ID: 1O01   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 CROTONALDEHYDE, NAD(H) AND MG2+
REMARK 900 RELATED ID: 1O02   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NADH IN THE PRESENCE OF MG2+
REMARK 900 RELATED ID: 1O05   RELATED DB: PDB
REMARK 900 APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
DBREF  1O04 A    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O04 B    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O04 C    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O04 D    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O04 E    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O04 F    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O04 G    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O04 H    1   500  UNP    P05091   ALDH2_HUMAN     18    517
SEQADV 1O04 SER A  302  UNP  P05091    CYS   319 ENGINEERED
SEQADV 1O04 SER B  302  UNP  P05091    CYS   319 ENGINEERED
SEQADV 1O04 SER C  302  UNP  P05091    CYS   319 ENGINEERED
SEQADV 1O04 SER D  302  UNP  P05091    CYS   319 ENGINEERED
SEQADV 1O04 SER E  302  UNP  P05091    CYS   319 ENGINEERED
SEQADV 1O04 SER F  302  UNP  P05091    CYS   319 ENGINEERED
SEQADV 1O04 SER G  302  UNP  P05091    CYS   319 ENGINEERED
SEQADV 1O04 SER H  302  UNP  P05091    CYS   319 ENGINEERED
SEQRES   1 A  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 A  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 A  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 A  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 A  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 A  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 A  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 A  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 A  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 A  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 A  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 A  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 A  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 A  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 A  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 A  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 A  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 A  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 A  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 A  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 A  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 A  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 A  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 A  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 A  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 A  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 A  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 A  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 A  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 A  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 A  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 A  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 A  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 A  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 A  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 A  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 A  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 A  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 A  500  VAL PRO GLN LYS ASN SER
SEQRES   1 B  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 B  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 B  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 B  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 B  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 B  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 B  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 B  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 B  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 B  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 B  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 B  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 B  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 B  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 B  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 B  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 B  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 B  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 B  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 B  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 B  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 B  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 B  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 B  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 B  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 B  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 B  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 B  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 B  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 B  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 B  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 B  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 B  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 B  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 B  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 B  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 B  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 B  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 B  500  VAL PRO GLN LYS ASN SER
SEQRES   1 C  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 C  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 C  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 C  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 C  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 C  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 C  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 C  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 C  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 C  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 C  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 C  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 C  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 C  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 C  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 C  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 C  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 C  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 C  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 C  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 C  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 C  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 C  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 C  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 C  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 C  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 C  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 C  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 C  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 C  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 C  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 C  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 C  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 C  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 C  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 C  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 C  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 C  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 C  500  VAL PRO GLN LYS ASN SER
SEQRES   1 D  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 D  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 D  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 D  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 D  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 D  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 D  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 D  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 D  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 D  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 D  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 D  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 D  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 D  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 D  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 D  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 D  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 D  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 D  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 D  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 D  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 D  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 D  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 D  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 D  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 D  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 D  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 D  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 D  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 D  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 D  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 D  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 D  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 D  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 D  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 D  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 D  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 D  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 D  500  VAL PRO GLN LYS ASN SER
SEQRES   1 E  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 E  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 E  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 E  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 E  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 E  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 E  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 E  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 E  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 E  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 E  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 E  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 E  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 E  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 E  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 E  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 E  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 E  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 E  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 E  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 E  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 E  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 E  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 E  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 E  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 E  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 E  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 E  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 E  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 E  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 E  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 E  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 E  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 E  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 E  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 E  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 E  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 E  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 E  500  VAL PRO GLN LYS ASN SER
SEQRES   1 F  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 F  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 F  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 F  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 F  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 F  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 F  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 F  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 F  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 F  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 F  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 F  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 F  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 F  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 F  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 F  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 F  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 F  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 F  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 F  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 F  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 F  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 F  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 F  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 F  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 F  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 F  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 F  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 F  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 F  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 F  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 F  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 F  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 F  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 F  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 F  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 F  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 F  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 F  500  VAL PRO GLN LYS ASN SER
SEQRES   1 G  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 G  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 G  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 G  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 G  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 G  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 G  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 G  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 G  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 G  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 G  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 G  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 G  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 G  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 G  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 G  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 G  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 G  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 G  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 G  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 G  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 G  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 G  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 G  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 G  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 G  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 G  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 G  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 G  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 G  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 G  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 G  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 G  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 G  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 G  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 G  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 G  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 G  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 G  500  VAL PRO GLN LYS ASN SER
SEQRES   1 H  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES   2 H  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES   3 H  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES   4 H  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES   5 H  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES   6 H  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES   7 H  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES   8 H  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES   9 H  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES  10 H  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES  11 H  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES  12 H  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES  13 H  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES  14 H  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES  15 H  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES  16 H  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES  17 H  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES  18 H  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES  19 H  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES  20 H  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES  21 H  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES  22 H  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES  23 H  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES  24 H  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 H  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 H  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 H  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 H  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 H  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 H  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 H  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 H  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 H  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 H  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 H  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 H  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 H  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 H  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 H  500  VAL PRO GLN LYS ASN SER
HET     NA  A6601       1
HET     NA  B6602       1
HET     NA  C6603       1
HET     NA  D6604       1
HET     NA  E6605       1
HET     NA  F6606       1
HET     NA  G6607       1
HET     NA  H6608       1
HET     MG  A6701       1
HET     MG  B6702       1
HET     MG  C6703       1
HET     MG  D6704       1
HET     MG  E6705       1
HET     MG  F6706       1
HET     MG  G6707       1
HET     MG  H6708       1
HET    NAD  A6501      44
HET    NAD  B6502      44
HET    NAD  C6503      44
HET    NAD  D6504      44
HET    NAD  E6505      44
HET    NAD  F6506      44
HET    NAD  G6507      44
HET    NAD  H6508      44
HET    GAI  A6801       4
HET    GAI  A6811       4
HET    GAI  B6802       4
HET    GAI  B6812       4
HET    GAI  C6803       4
HET    GAI  C6813       4
HET    GAI  C6823       4
HET    GAI  D6804       4
HET    GAI  D6814       4
HET    GAI  E6805       4
HET    GAI  E6815       4
HET    GAI  F6806       4
HET    GAI  F6816       4
HET    GAI  F6826       4
HET    GAI  G6807       4
HET    GAI  G6817       4
HET    GAI  H6808       4
HET    GAI  H6818       4
HET    EDO  A6901       4
HET    EDO  A6911       4
HET    EDO  A6921       4
HET    EDO  A6941       4
HET    EDO  B6902       4
HET    EDO  B6912       4
HET    EDO  B6922       4
HET    EDO  B6942       4
HET    EDO  C6903       4
HET    EDO  C6913       4
HET    EDO  C6923       4
HET    EDO  C6943       4
HET    EDO  C6963       4
HET    EDO  D6904       4
HET    EDO  D6914       4
HET    EDO  D6944       4
HET    EDO  E6905       4
HET    EDO  E6915       4
HET    EDO  E6925       4
HET    EDO  F6906       4
HET    EDO  F6916       4
HET    EDO  F6926       4
HET    EDO  F6946       4
HET    EDO  F6956       4
HET    EDO  F6966       4
HET    EDO  G6907       4
HET    EDO  G6917       4
HET    EDO  G6927       4
HET    EDO  H6908       4
HET    EDO  H6918       4
HET    EDO  H6928       4
HET    EDO  H6948       4
HETNAM      NA SODIUM ION
HETNAM      MG MAGNESIUM ION
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM     GAI GUANIDINE
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   9   NA    8(NA 1+)
FORMUL  17   MG    8(MG 2+)
FORMUL  25  NAD    8(C21 H27 N7 O14 P2)
FORMUL  33  GAI    18(C H5 N3)
FORMUL  51  EDO    32(C2 H6 O2)
FORMUL  83  HOH   *5025(H2 O)
HELIX    1   1 ASP A   55  PHE A   70  1                                  16
HELIX    2   2 SER A   74  MET A   79  1                                   6
HELIX    3   3 ASP A   80  ASP A   98  1                                  19
HELIX    4   4 ASP A   98  GLY A  111  1                                  14
HELIX    5   5 PRO A  113  VAL A  120  1                                   8
HELIX    6   6 VAL A  120  ALA A  136  1                                  17
HELIX    7   7 PHE A  170  THR A  185  1                                  16
HELIX    8   8 PRO A  198  GLY A  212  1                                  15
HELIX    9   9 THR A  227  SER A  234  1                                   8
HELIX   10  10 SER A  246  SER A  260  1                                  15
HELIX   11  11 ASP A  282  PHE A  296  1                                  15
HELIX   12  12 ASN A  297  GLN A  300  5                                   4
HELIX   13  13 GLU A  312  ARG A  329  1                                  18
HELIX   14  14 ASP A  346  GLU A  363  1                                  18
HELIX   15  15 MET A  393  GLU A  398  1                                   6
HELIX   16  16 THR A  412  ASN A  422  1                                  11
HELIX   17  17 ASP A  435  LEU A  446  1                                  12
HELIX   18  18 TYR A  468  MET A  470  5                                   3
HELIX   19  19 GLY A  478  ALA A  484  5                                   7
HELIX   20  20 ASP B   55  PHE B   70  1                                  16
HELIX   21  21 SER B   74  MET B   79  1                                   6
HELIX   22  22 ASP B   80  ASP B   98  1                                  19
HELIX   23  23 ASP B   98  GLY B  111  1                                  14
HELIX   24  24 PRO B  113  VAL B  120  1                                   8
HELIX   25  25 VAL B  120  ALA B  136  1                                  17
HELIX   26  26 PHE B  170  THR B  185  1                                  16
HELIX   27  27 PRO B  198  GLY B  212  1                                  15
HELIX   28  28 THR B  227  SER B  234  1                                   8
HELIX   29  29 SER B  246  SER B  260  1                                  15
HELIX   30  30 ASP B  282  PHE B  296  1                                  15
HELIX   31  31 ASN B  297  GLN B  300  5                                   4
HELIX   32  32 ILE B  314  ARG B  329  1                                  16
HELIX   33  33 ASP B  346  GLU B  363  1                                  18
HELIX   34  34 MET B  393  GLU B  398  1                                   6
HELIX   35  35 THR B  412  ASN B  422  1                                  11
HELIX   36  36 ASP B  435  LEU B  446  1                                  12
HELIX   37  37 TYR B  468  MET B  470  5                                   3
HELIX   38  38 GLY B  478  ALA B  484  5                                   7
HELIX   39  39 ASP C   55  PHE C   70  1                                  16
HELIX   40  40 SER C   74  MET C   79  1                                   6
HELIX   41  41 ASP C   80  ASP C   98  1                                  19
HELIX   42  42 ASP C   98  GLY C  111  1                                  14
HELIX   43  43 PRO C  113  VAL C  120  1                                   8
HELIX   44  44 VAL C  120  ALA C  136  1                                  17
HELIX   45  45 PHE C  170  THR C  185  1                                  16
HELIX   46  46 PRO C  198  GLY C  212  1                                  15
HELIX   47  47 THR C  227  SER C  234  1                                   8
HELIX   48  48 SER C  246  SER C  260  1                                  15
HELIX   49  49 ASP C  282  PHE C  296  1                                  15
HELIX   50  50 ASN C  297  GLN C  300  5                                   4
HELIX   51  51 ILE C  314  ARG C  329  1                                  16
HELIX   52  52 ASP C  346  GLU C  363  1                                  18
HELIX   53  53 MET C  393  GLU C  398  1                                   6
HELIX   54  54 THR C  412  ASN C  422  1                                  11
HELIX   55  55 ASP C  435  LEU C  446  1                                  12
HELIX   56  56 TYR C  468  MET C  470  5                                   3
HELIX   57  57 GLY C  478  ALA C  484  5                                   7
HELIX   58  58 ASP D   55  PHE D   70  1                                  16
HELIX   59  59 SER D   74  MET D   79  1                                   6
HELIX   60  60 ASP D   80  ASP D   98  1                                  19
HELIX   61  61 ASP D   98  GLY D  111  1                                  14
HELIX   62  62 PRO D  113  VAL D  120  1                                   8
HELIX   63  63 VAL D  120  ALA D  136  1                                  17
HELIX   64  64 PHE D  170  THR D  185  1                                  16
HELIX   65  65 PRO D  198  GLY D  212  1                                  15
HELIX   66  66 THR D  227  SER D  234  1                                   8
HELIX   67  67 SER D  246  SER D  260  1                                  15
HELIX   68  68 ASP D  282  PHE D  296  1                                  15
HELIX   69  69 ASN D  297  GLN D  300  5                                   4
HELIX   70  70 ILE D  314  ARG D  329  1                                  16
HELIX   71  71 ASP D  346  GLU D  363  1                                  18
HELIX   72  72 MET D  393  LYS D  397  5                                   5
HELIX   73  73 THR D  412  ASN D  422  1                                  11
HELIX   74  74 ASP D  435  LEU D  446  1                                  12
HELIX   75  75 TYR D  468  MET D  470  5                                   3
HELIX   76  76 GLY D  478  ALA D  484  5                                   7
HELIX   77  77 ASP E   55  PHE E   70  1                                  16
HELIX   78  78 SER E   74  MET E   79  1                                   6
HELIX   79  79 ASP E   80  ASP E   98  1                                  19
HELIX   80  80 ASP E   98  GLY E  111  1                                  14
HELIX   81  81 PRO E  113  VAL E  120  1                                   8
HELIX   82  82 VAL E  120  ALA E  136  1                                  17
HELIX   83  83 PHE E  170  THR E  185  1                                  16
HELIX   84  84 PRO E  198  GLY E  212  1                                  15
HELIX   85  85 THR E  227  SER E  234  1                                   8
HELIX   86  86 SER E  246  SER E  260  1                                  15
HELIX   87  87 ASP E  282  PHE E  296  1                                  15
HELIX   88  88 ASN E  297  GLN E  300  5                                   4
HELIX   89  89 GLU E  312  ARG E  329  1                                  18
HELIX   90  90 ASP E  346  GLU E  363  1                                  18
HELIX   91  91 MET E  393  GLU E  398  1                                   6
HELIX   92  92 THR E  412  ASN E  422  1                                  11
HELIX   93  93 ASP E  435  LEU E  446  1                                  12
HELIX   94  94 TYR E  468  MET E  470  5                                   3
HELIX   95  95 GLY E  478  ALA E  484  5                                   7
HELIX   96  96 ASP F   55  PHE F   70  1                                  16
HELIX   97  97 SER F   74  MET F   79  1                                   6
HELIX   98  98 ASP F   80  ASP F   98  1                                  19
HELIX   99  99 ASP F   98  GLY F  111  1                                  14
HELIX  100 100 PRO F  113  VAL F  120  1                                   8
HELIX  101 101 VAL F  120  ALA F  136  1                                  17
HELIX  102 102 PHE F  170  THR F  185  1                                  16
HELIX  103 103 PRO F  198  GLY F  212  1                                  15
HELIX  104 104 THR F  227  SER F  234  1                                   8
HELIX  105 105 SER F  246  SER F  260  1                                  15
HELIX  106 106 ASP F  282  PHE F  296  1                                  15
HELIX  107 107 ASN F  297  GLN F  300  5                                   4
HELIX  108 108 GLU F  312  ARG F  329  1                                  18
HELIX  109 109 ASP F  346  GLU F  363  1                                  18
HELIX  110 110 MET F  393  GLU F  398  1                                   6
HELIX  111 111 THR F  412  ASN F  422  1                                  11
HELIX  112 112 ASP F  435  LEU F  446  1                                  12
HELIX  113 113 TYR F  468  MET F  470  5                                   3
HELIX  114 114 GLY F  478  ALA F  484  5                                   7
HELIX  115 115 ASP G   55  PHE G   70  1                                  16
HELIX  116 116 SER G   74  MET G   79  1                                   6
HELIX  117 117 ASP G   80  ASP G   98  1                                  19
HELIX  118 118 ASP G   98  GLY G  111  1                                  14
HELIX  119 119 PRO G  113  VAL G  120  1                                   8
HELIX  120 120 VAL G  120  ALA G  136  1                                  17
HELIX  121 121 PHE G  170  THR G  185  1                                  16
HELIX  122 122 PRO G  198  GLY G  212  1                                  15
HELIX  123 123 THR G  227  SER G  234  1                                   8
HELIX  124 124 SER G  246  SER G  260  1                                  15
HELIX  125 125 ASP G  282  PHE G  296  1                                  15
HELIX  126 126 ASN G  297  GLN G  300  5                                   4
HELIX  127 127 GLU G  312  ARG G  329  1                                  18
HELIX  128 128 ASP G  346  GLU G  363  1                                  18
HELIX  129 129 MET G  393  GLU G  398  1                                   6
HELIX  130 130 THR G  412  ASN G  422  1                                  11
HELIX  131 131 ASP G  435  LEU G  446  1                                  12
HELIX  132 132 TYR G  468  MET G  470  5                                   3
HELIX  133 133 GLY G  478  ALA G  484  5                                   7
HELIX  134 134 ASP H   55  PHE H   70  1                                  16
HELIX  135 135 SER H   74  MET H   79  1                                   6
HELIX  136 136 ASP H   80  ASP H   98  1                                  19
HELIX  137 137 ASP H   98  GLY H  111  1                                  14
HELIX  138 138 PRO H  113  VAL H  120  1                                   8
HELIX  139 139 VAL H  120  ALA H  136  1                                  17
HELIX  140 140 PHE H  170  THR H  185  1                                  16
HELIX  141 141 PRO H  198  GLY H  212  1                                  15
HELIX  142 142 THR H  227  SER H  234  1                                   8
HELIX  143 143 SER H  246  SER H  260  1                                  15
HELIX  144 144 ASP H  282  PHE H  296  1                                  15
HELIX  145 145 ASN H  297  GLN H  300  5                                   4
HELIX  146 146 GLU H  312  ARG H  329  1                                  18
HELIX  147 147 ASP H  346  GLU H  363  1                                  18
HELIX  148 148 MET H  393  GLU H  398  1                                   6
HELIX  149 149 THR H  412  ASN H  422  1                                  11
HELIX  150 150 ASP H  435  LEU H  446  1                                  12
HELIX  151 151 TYR H  468  MET H  470  5                                   3
HELIX  152 152 GLY H  478  ALA H  484  5                                   7
SHEET    1   A 2 ILE A  22  ILE A  24  0
SHEET    2   A 2 GLU A  27  HIS A  29 -1  O  HIS A  29   N  ILE A  22
SHEET    1   B 2 THR A  36  VAL A  40  0
SHEET    2   B 2 VAL A  47  ALA A  52 -1  O  ILE A  48   N  THR A  39
SHEET    1   C20 LYS B 366  CYS B 369  0
SHEET    2   C20 THR B 384  GLY B 387 -1  O  GLY B 387   N  LYS B 366
SHEET    3   C20 VAL B 404  PHE B 410  1  O  MET B 405   N  PHE B 386
SHEET    4   C20 ARG B 307  GLN B 311  1  N  VAL B 310   O  LEU B 408
SHEET    5   C20 PRO B 274  ILE B 277  1  N  ILE B 277   O  PHE B 309
SHEET    6   C20 ALA B 428  PHE B 432  1  O  ALA B 430   N  ILE B 276
SHEET    7   C20 THR B 450  VAL B 453  1  O  TRP B 452   N  ALA B 429
SHEET    8   C20 THR A 486  LYS A 494  1  N  THR A 490   O  VAL B 451
SHEET    9   C20 PHE A 150  PRO A 158 -1  N  PHE A 151   O  VAL A 493
SHEET   10   C20 GLY A 141  ILE A 144 -1  N  ILE A 144   O  SER A 152
SHEET   11   C20 GLY D 141  ILE D 144 -1  O  GLY D 141   N  THR A 143
SHEET   12   C20 PHE D 150  PRO D 158 -1  O  SER D 152   N  ILE D 144
SHEET   13   C20 THR D 486  LYS D 494 -1  O  VAL D 493   N  PHE D 151
SHEET   14   C20 THR C 450  VAL C 453  1  N  VAL C 451   O  THR D 490
SHEET   15   C20 ALA C 428  PHE C 432  1  N  ALA C 429   O  TRP C 452
SHEET   16   C20 PRO C 274  ILE C 277  1  N  ILE C 276   O  ALA C 430
SHEET   17   C20 ARG C 307  GLN C 311  1  O  PHE C 309   N  ILE C 277
SHEET   18   C20 VAL C 404  PHE C 410  1  O  LEU C 408   N  VAL C 310
SHEET   19   C20 THR C 384  GLY C 387  1  N  PHE C 386   O  MET C 405
SHEET   20   C20 LYS C 366  CYS C 369 -1  N  LYS C 366   O  GLY C 387
SHEET    1   D 6 VAL A 218  ILE A 220  0
SHEET    2   D 6 VAL A 188  LYS A 192  1  N  MET A 191   O  ASN A 219
SHEET    3   D 6 VAL A 161  ILE A 165  1  N  GLN A 164   O  LYS A 192
SHEET    4   D 6 LYS A 240  THR A 244  1  O  LYS A 240   N  GLY A 163
SHEET    5   D 6 ARG A 264  GLU A 268  1  O  ARG A 264   N  VAL A 241
SHEET    6   D 6 GLY A 472  SER A 473 -1  O  SER A 473   N  LEU A 267
SHEET    1   E20 LYS A 366  CYS A 369  0
SHEET    2   E20 THR A 384  GLY A 387 -1  O  GLY A 387   N  LYS A 366
SHEET    3   E20 VAL A 404  PHE A 410  1  O  MET A 405   N  PHE A 386
SHEET    4   E20 GLY A 305  GLN A 311  1  N  VAL A 310   O  LEU A 408
SHEET    5   E20 SER A 273  ILE A 277  1  N  ILE A 277   O  PHE A 309
SHEET    6   E20 ALA A 428  PHE A 432  1  O  ALA A 430   N  ILE A 276
SHEET    7   E20 THR A 450  VAL A 453  1  O  TRP A 452   N  ALA A 429
SHEET    8   E20 THR B 486  LYS B 494  1  O  THR B 490   N  VAL A 451
SHEET    9   E20 PHE B 150  PRO B 158 -1  N  PHE B 151   O  VAL B 493
SHEET   10   E20 GLY B 141  ILE B 144 -1  N  ILE B 144   O  SER B 152
SHEET   11   E20 GLY C 141  ILE C 144 -1  O  THR C 143   N  GLY B 141
SHEET   12   E20 PHE C 150  PRO C 158 -1  O  SER C 152   N  ILE C 144
SHEET   13   E20 THR C 486  LYS C 494 -1  O  VAL C 493   N  PHE C 151
SHEET   14   E20 THR D 450  VAL D 453  1  O  VAL D 451   N  THR C 490
SHEET   15   E20 ALA D 428  PHE D 432  1  N  ALA D 429   O  TRP D 452
SHEET   16   E20 PRO D 274  ILE D 277  1  N  ILE D 276   O  ALA D 430
SHEET   17   E20 ARG D 307  GLN D 311  1  O  PHE D 309   N  ILE D 277
SHEET   18   E20 VAL D 404  PHE D 410  1  O  LEU D 408   N  VAL D 310
SHEET   19   E20 THR D 384  GLY D 387  1  N  THR D 384   O  MET D 405
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LYS D 366   O  GLY D 387
SHEET    1   F 2 ILE B  22  ILE B  24  0
SHEET    2   F 2 GLU B  27  HIS B  29 -1  O  HIS B  29   N  ILE B  22
SHEET    1   G 2 THR B  36  VAL B  40  0
SHEET    2   G 2 VAL B  47  ALA B  52 -1  O  ILE B  48   N  THR B  39
SHEET    1   H 6 VAL B 218  ILE B 220  0
SHEET    2   H 6 VAL B 188  LYS B 192  1  N  MET B 191   O  ASN B 219
SHEET    3   H 6 VAL B 161  ILE B 165  1  N  GLN B 164   O  LYS B 192
SHEET    4   H 6 LYS B 240  THR B 244  1  O  LYS B 240   N  GLY B 163
SHEET    5   H 6 ARG B 264  GLU B 268  1  O  ARG B 264   N  VAL B 241
SHEET    6   H 6 GLY B 472  SER B 473 -1  O  SER B 473   N  LEU B 267
SHEET    1   I 2 ILE C  22  ILE C  24  0
SHEET    2   I 2 GLU C  27  HIS C  29 -1  O  HIS C  29   N  ILE C  22
SHEET    1   J 2 THR C  36  VAL C  40  0
SHEET    2   J 2 VAL C  47  ALA C  52 -1  O  ILE C  48   N  THR C  39
SHEET    1   K 6 VAL C 218  ILE C 220  0
SHEET    2   K 6 VAL C 188  LYS C 192  1  N  MET C 191   O  ASN C 219
SHEET    3   K 6 VAL C 161  ILE C 165  1  N  CYS C 162   O  VAL C 188
SHEET    4   K 6 LYS C 240  THR C 244  1  O  LYS C 240   N  GLY C 163
SHEET    5   K 6 ARG C 264  GLU C 268  1  O  ARG C 264   N  VAL C 241
SHEET    6   K 6 GLY C 472  SER C 473 -1  O  SER C 473   N  LEU C 267
SHEET    1   L 2 ILE D  22  ILE D  24  0
SHEET    2   L 2 GLU D  27  HIS D  29 -1  O  HIS D  29   N  ILE D  22
SHEET    1   M 2 THR D  36  VAL D  40  0
SHEET    2   M 2 VAL D  47  ALA D  52 -1  O  ILE D  48   N  THR D  39
SHEET    1   N 6 VAL D 218  ILE D 220  0
SHEET    2   N 6 VAL D 188  LYS D 192  1  N  MET D 191   O  ASN D 219
SHEET    3   N 6 VAL D 161  ILE D 165  1  N  CYS D 162   O  VAL D 188
SHEET    4   N 6 LYS D 240  THR D 244  1  O  LYS D 240   N  GLY D 163
SHEET    5   N 6 ARG D 264  GLU D 268  1  O  ARG D 264   N  VAL D 241
SHEET    6   N 6 GLY D 472  SER D 473 -1  O  SER D 473   N  LEU D 267
SHEET    1   O 2 ILE E  22  ILE E  24  0
SHEET    2   O 2 GLU E  27  HIS E  29 -1  O  HIS E  29   N  ILE E  22
SHEET    1   P 2 THR E  36  VAL E  40  0
SHEET    2   P 2 VAL E  47  ALA E  52 -1  O  ILE E  48   N  THR E  39
SHEET    1   Q20 LYS F 366  CYS F 369  0
SHEET    2   Q20 THR F 384  GLY F 387 -1  O  GLY F 387   N  LYS F 366
SHEET    3   Q20 VAL F 404  PHE F 410  1  O  MET F 405   N  PHE F 386
SHEET    4   Q20 ARG F 307  GLN F 311  1  N  THR F 308   O  LEU F 408
SHEET    5   Q20 PRO F 274  ILE F 277  1  N  ILE F 277   O  PHE F 309
SHEET    6   Q20 ALA F 428  PHE F 432  1  O  ALA F 430   N  ILE F 276
SHEET    7   Q20 THR F 450  VAL F 453  1  O  TRP F 452   N  ALA F 429
SHEET    8   Q20 THR E 486  LYS E 494  1  N  THR E 490   O  VAL F 451
SHEET    9   Q20 PHE E 150  PRO E 158 -1  N  PHE E 151   O  VAL E 493
SHEET   10   Q20 GLY E 141  ILE E 144 -1  N  ILE E 144   O  SER E 152
SHEET   11   Q20 GLY H 141  ILE H 144 -1  O  THR H 143   N  GLY E 141
SHEET   12   Q20 PHE H 150  PRO H 158 -1  O  SER H 152   N  ILE H 144
SHEET   13   Q20 THR H 486  LYS H 494 -1  O  VAL H 493   N  PHE H 151
SHEET   14   Q20 THR G 450  VAL G 453  1  N  VAL G 451   O  THR H 490
SHEET   15   Q20 ALA G 428  PHE G 432  1  N  ALA G 429   O  TRP G 452
SHEET   16   Q20 PRO G 274  ILE G 277  1  N  ILE G 276   O  ALA G 430
SHEET   17   Q20 ARG G 307  GLN G 311  1  O  PHE G 309   N  ILE G 277
SHEET   18   Q20 VAL G 404  PHE G 410  1  O  LEU G 408   N  VAL G 310
SHEET   19   Q20 THR G 384  GLY G 387  1  N  PHE G 386   O  MET G 405
SHEET   20   Q20 LYS G 366  CYS G 369 -1  N  LYS G 366   O  GLY G 387
SHEET    1   R 6 VAL E 218  ILE E 220  0
SHEET    2   R 6 VAL E 188  LYS E 192  1  N  MET E 191   O  ASN E 219
SHEET    3   R 6 VAL E 161  ILE E 165  1  N  GLN E 164   O  LYS E 192
SHEET    4   R 6 LYS E 240  THR E 244  1  O  LYS E 240   N  GLY E 163
SHEET    5   R 6 ARG E 264  GLU E 268  1  O  ARG E 264   N  VAL E 241
SHEET    6   R 6 GLY E 472  SER E 473 -1  O  SER E 473   N  LEU E 267
SHEET    1   S20 LYS E 366  CYS E 369  0
SHEET    2   S20 THR E 384  GLY E 387 -1  O  GLY E 387   N  LYS E 366
SHEET    3   S20 VAL E 404  PHE E 410  1  O  MET E 405   N  PHE E 386
SHEET    4   S20 ARG E 307  GLN E 311  1  N  VAL E 310   O  LEU E 408
SHEET    5   S20 PRO E 274  ILE E 277  1  N  ILE E 277   O  PHE E 309
SHEET    6   S20 ALA E 428  PHE E 432  1  O  ALA E 430   N  ILE E 276
SHEET    7   S20 THR E 450  VAL E 453  1  O  TRP E 452   N  ALA E 429
SHEET    8   S20 THR F 486  LYS F 494  1  O  THR F 490   N  VAL E 451
SHEET    9   S20 PHE F 150  PRO F 158 -1  N  PHE F 151   O  VAL F 493
SHEET   10   S20 GLY F 141  ILE F 144 -1  N  ILE F 144   O  SER F 152
SHEET   11   S20 GLY G 141  ILE G 144 -1  O  THR G 143   N  GLY F 141
SHEET   12   S20 PHE G 150  PRO G 158 -1  O  SER G 152   N  ILE G 144
SHEET   13   S20 THR G 486  LYS G 494 -1  O  VAL G 493   N  PHE G 151
SHEET   14   S20 THR H 450  VAL H 453  1  O  VAL H 451   N  THR G 490
SHEET   15   S20 ALA H 428  PHE H 432  1  N  ALA H 429   O  TRP H 452
SHEET   16   S20 PRO H 274  ILE H 277  1  N  ILE H 276   O  ALA H 430
SHEET   17   S20 ARG H 307  GLN H 311  1  O  PHE H 309   N  ILE H 277
SHEET   18   S20 VAL H 404  PHE H 410  1  O  LEU H 408   N  THR H 308
SHEET   19   S20 THR H 384  GLY H 387  1  N  PHE H 386   O  MET H 405
SHEET   20   S20 LYS H 366  CYS H 369 -1  N  LYS H 366   O  GLY H 387
SHEET    1   T 2 ILE F  22  ILE F  24  0
SHEET    2   T 2 GLU F  27  HIS F  29 -1  O  HIS F  29   N  ILE F  22
SHEET    1   U 2 THR F  36  VAL F  40  0
SHEET    2   U 2 VAL F  47  ALA F  52 -1  O  ILE F  48   N  THR F  39
SHEET    1   V 6 VAL F 218  ILE F 220  0
SHEET    2   V 6 VAL F 188  LYS F 192  1  N  MET F 191   O  ASN F 219
SHEET    3   V 6 VAL F 161  ILE F 165  1  N  CYS F 162   O  VAL F 188
SHEET    4   V 6 LYS F 240  THR F 244  1  O  LYS F 240   N  GLY F 163
SHEET    5   V 6 ARG F 264  GLU F 268  1  O  ARG F 264   N  VAL F 241
SHEET    6   V 6 GLY F 472  SER F 473 -1  O  SER F 473   N  LEU F 267
SHEET    1   W 2 ILE G  22  ILE G  24  0
SHEET    2   W 2 GLU G  27  HIS G  29 -1  O  HIS G  29   N  ILE G  22
SHEET    1   X 2 THR G  36  VAL G  40  0
SHEET    2   X 2 VAL G  47  ALA G  52 -1  O  ILE G  48   N  THR G  39
SHEET    1   Y 6 VAL G 218  ILE G 220  0
SHEET    2   Y 6 VAL G 188  LYS G 192  1  N  MET G 191   O  ASN G 219
SHEET    3   Y 6 VAL G 161  ILE G 165  1  N  GLN G 164   O  LYS G 192
SHEET    4   Y 6 LYS G 240  THR G 244  1  O  LYS G 240   N  GLY G 163
SHEET    5   Y 6 ARG G 264  GLU G 268  1  O  ARG G 264   N  VAL G 241
SHEET    6   Y 6 GLY G 472  SER G 473 -1  O  SER G 473   N  LEU G 267
SHEET    1   Z 2 ILE H  22  ILE H  24  0
SHEET    2   Z 2 GLU H  27  HIS H  29 -1  O  HIS H  29   N  ILE H  22
SHEET    1  AA 2 THR H  36  VAL H  40  0
SHEET    2  AA 2 VAL H  47  ALA H  52 -1  O  ILE H  48   N  THR H  39
SHEET    1  AB 6 VAL H 218  ILE H 220  0
SHEET    2  AB 6 VAL H 188  LYS H 192  1  N  MET H 191   O  ASN H 219
SHEET    3  AB 6 VAL H 161  ILE H 165  1  N  GLN H 164   O  LYS H 192
SHEET    4  AB 6 LYS H 240  THR H 244  1  O  LYS H 240   N  GLY H 163
SHEET    5  AB 6 ARG H 264  GLU H 268  1  O  ARG H 264   N  VAL H 241
SHEET    6  AB 6 GLY H 472  SER H 473 -1  O  SER H 473   N  LEU H 267
LINK         O2A NAD A6501                MG    MG A6701     1555   1555  2.00
LINK        NA    NA A6601                 O   HOH A7169     1555   1555  2.36
LINK        NA    NA A6601                 O   ASP A 109     1555   1555  2.40
LINK        NA    NA A6601                 O   VAL A  40     1555   1555  2.36
LINK        NA    NA A6601                 OD1 ASP A 109     1555   1555  2.44
LINK        NA    NA A6601                 O   GLN A 196     1555   1555  2.46
LINK        MG    MG A6701                 O   HOH A7062     1555   1555  2.10
LINK        MG    MG A6701                 O   HOH A7058     1555   1555  2.21
LINK        MG    MG A6701                 O   HOH A7059     1555   1555  2.06
LINK        MG    MG A6701                 O   HOH A7060     1555   1555  2.08
LINK        MG    MG A6701                 O   HOH A7257     1555   1555  2.11
LINK         O2A NAD B6502                MG    MG B6702     1555   1555  1.96
LINK        NA    NA B6602                 O   ASP B 109     1555   1555  2.39
LINK        NA    NA B6602                 O   VAL B  40     1555   1555  2.39
LINK        NA    NA B6602                 OD1 ASP B 109     1555   1555  2.40
LINK        NA    NA B6602                 O   GLN B 196     1555   1555  2.50
LINK        NA    NA B6602                 O   HOH B7433     1555   1555  2.33
LINK        MG    MG B6702                 O   HOH B7011     1555   1555  2.08
LINK        MG    MG B6702                 O   HOH B7013     1555   1555  2.16
LINK        MG    MG B6702                 O   HOH B7191     1555   1555  2.11
LINK        MG    MG B6702                 O   HOH B7430     1555   1555  2.05
LINK        MG    MG B6702                 O   HOH B7194     1555   1555  2.07
LINK         O2A NAD C6503                MG    MG C6703     1555   1555  1.99
LINK        NA    NA C6603                 O   ASP C 109     1555   1555  2.42
LINK        NA    NA C6603                 O   VAL C  40     1555   1555  2.37
LINK        NA    NA C6603                 OD1 ASP C 109     1555   1555  2.47
LINK        NA    NA C6603                 O   GLN C 196     1555   1555  2.45
LINK        NA    NA C6603                 O   HOH C7317     1555   1555  2.38
LINK        MG    MG C6703                 O   HOH C7257     1555   1555  2.18
LINK        MG    MG C6703                 O   HOH C7000     1555   1555  2.28
LINK        MG    MG C6703                 O   HOH C7223     1555   1555  2.19
LINK        MG    MG C6703                 O   HOH C7220     1555   1555  2.05
LINK        MG    MG C6703                 O   HOH C7221     1555   1555  2.09
LINK         O2A NAD D6504                MG    MG D6704     1555   1555  1.97
LINK        NA    NA D6604                 O   ASP D 109     1555   1555  2.40
LINK        NA    NA D6604                 OD1 ASP D 109     1555   1555  2.45
LINK        NA    NA D6604                 O   VAL D  40     1555   1555  2.36
LINK        NA    NA D6604                 O   GLN D 196     1555   1555  2.53
LINK        NA    NA D6604                 O   HOH D7466     1555   1555  2.35
LINK        MG    MG D6704                 O   HOH D7069     1555   1555  2.07
LINK        MG    MG D6704                 O   HOH D7531     1555   1555  2.12
LINK        MG    MG D6704                 O   HOH D7447     1555   1555  2.23
LINK        MG    MG D6704                 O   HOH D7072     1555   1555  2.07
LINK        MG    MG D6704                 O   HOH D7070     1555   1555  2.06
LINK         O2A NAD E6505                MG    MG E6705     1555   1555  1.98
LINK        NA    NA E6605                 O   ASP E 109     1555   1555  2.36
LINK        NA    NA E6605                 OD1 ASP E 109     1555   1555  2.43
LINK        NA    NA E6605                 O   HOH E3885     1555   1555  2.35
LINK        NA    NA E6605                 O   VAL E  40     1555   1555  2.35
LINK        NA    NA E6605                 O   GLN E 196     1555   1555  2.50
LINK        MG    MG E6705                 O   HOH E2627     1555   1555  2.00
LINK        MG    MG E6705                 O   HOH E2628     1555   1555  2.10
LINK        MG    MG E6705                 O   HOH E4785     1555   1555  2.22
LINK        MG    MG E6705                 O   HOH E2631     1555   1555  2.03
LINK        MG    MG E6705                 O   HOH E2632     1555   1555  2.17
LINK         O2A NAD F6506                MG    MG F6706     1555   1555  1.95
LINK        NA    NA F6606                 O   HOH F2809     1555   1555  2.28
LINK        NA    NA F6606                 O   ASP F 109     1555   1555  2.38
LINK        NA    NA F6606                 O   VAL F  40     1555   1555  2.38
LINK        NA    NA F6606                 OD1 ASP F 109     1555   1555  2.43
LINK        NA    NA F6606                 O   GLN F 196     1555   1555  2.45
LINK        MG    MG F6706                 O   HOH F2815     1555   1555  2.19
LINK        MG    MG F6706                 O   HOH F2833     1555   1555  2.31
LINK        MG    MG F6706                 O   HOH F2834     1555   1555  2.07
LINK        MG    MG F6706                 O   HOH F2814     1555   1555  1.98
LINK        MG    MG F6706                 O   HOH F2813     1555   1555  2.12
LINK         O2A NAD G6507                MG    MG G6707     1555   1555  1.99
LINK        NA    NA G6607                 O   HOH G3200     1555   1555  2.27
LINK        NA    NA G6607                 O   ASP G 109     1555   1555  2.37
LINK        NA    NA G6607                 O   VAL G  40     1555   1555  2.38
LINK        NA    NA G6607                 O   GLN G 196     1555   1555  2.53
LINK        NA    NA G6607                 OD1 ASP G 109     1555   1555  2.42
LINK        MG    MG G6707                 O   HOH G4359     1555   1555  2.10
LINK        MG    MG G6707                 O   HOH G3209     1555   1555  2.10
LINK        MG    MG G6707                 O   HOH G4361     1555   1555  2.05
LINK        MG    MG G6707                 O   HOH G4360     1555   1555  2.11
LINK        MG    MG G6707                 O   HOH G3210     1555   1555  2.08
LINK         O2A NAD H6508                MG    MG H6708     1555   1555  1.94
LINK        NA    NA H6608                 O   HOH H4701     1555   1555  2.36
LINK        NA    NA H6608                 O   GLN H 196     1555   1555  2.45
LINK        NA    NA H6608                 OD1 ASP H 109     1555   1555  2.49
LINK        NA    NA H6608                 O   ASP H 109     1555   1555  2.38
LINK        NA    NA H6608                 O   VAL H  40     1555   1555  2.41
LINK        MG    MG H6708                 O   HOH H2235     1555   1555  2.06
LINK        MG    MG H6708                 O   HOH H2230     1555   1555  2.09
LINK        MG    MG H6708                 O   HOH H2227     1555   1555  2.21
LINK        MG    MG H6708                 O   HOH H2231     1555   1555  1.99
LINK        MG    MG H6708                 O   HOH H2228     1555   1555  2.14
LINK         OG1 THR A  39                NA    NA A6601     1555   1555  2.95
LINK         OG1 THR B  39                NA    NA B6602     1555   1555  2.92
LINK         OG1 THR D  39                NA    NA D6604     1555   1555  2.99
LINK         OG1 THR E  39                NA    NA E6605     1555   1555  2.95
LINK         OG1 THR G  39                NA    NA G6607     1555   1555  2.92
SITE     1 AC1  5 THR A  39  VAL A  40  ASP A 109  GLN A 196
SITE     2 AC1  5 HOH A7169
SITE     1 AC2  5 THR B  39  VAL B  40  ASP B 109  GLN B 196
SITE     2 AC2  5 HOH B7433
SITE     1 AC3  5 THR C  39  VAL C  40  ASP C 109  GLN C 196
SITE     2 AC3  5 HOH C7317
SITE     1 AC4  5 THR D  39  VAL D  40  ASP D 109  GLN D 196
SITE     2 AC4  5 HOH D7466
SITE     1 AC5  5 THR E  39  VAL E  40  ASP E 109  GLN E 196
SITE     2 AC5  5 HOH E3885
SITE     1 AC6  5 THR F  39  VAL F  40  ASP F 109  GLN F 196
SITE     2 AC6  5 HOH F2809
SITE     1 AC7  5 THR G  39  VAL G  40  ASP G 109  GLN G 196
SITE     2 AC7  5 HOH G3200
SITE     1 AC8  5 THR H  39  VAL H  40  ASP H 109  GLN H 196
SITE     2 AC8  5 HOH H4701
SITE     1 AC9  6 NAD A6501  HOH A7058  HOH A7059  HOH A7060
SITE     2 AC9  6 HOH A7062  HOH A7257
SITE     1 BC1  6 NAD B6502  HOH B7011  HOH B7013  HOH B7191
SITE     2 BC1  6 HOH B7194  HOH B7430
SITE     1 BC2  6 NAD C6503  HOH C7000  HOH C7220  HOH C7221
SITE     2 BC2  6 HOH C7223  HOH C7257
SITE     1 BC3  6 NAD D6504  HOH D7069  HOH D7070  HOH D7072
SITE     2 BC3  6 HOH D7447  HOH D7531
SITE     1 BC4  6 HOH E2627  HOH E2628  HOH E2631  HOH E2632
SITE     2 BC4  6 HOH E4785  NAD E6505
SITE     1 BC5  6 HOH F2813  HOH F2814  HOH F2815  HOH F2833
SITE     2 BC5  6 HOH F2834  NAD F6506
SITE     1 BC6  6 HOH G3209  HOH G3210  HOH G4359  HOH G4360
SITE     2 BC6  6 HOH G4361  NAD G6507
SITE     1 BC7  6 HOH H2227  HOH H2228  HOH H2230  HOH H2231
SITE     2 BC7  6 HOH H2235  NAD H6508
SITE     1 BC8 36 ILE A 165  ILE A 166  PRO A 167  TRP A 168
SITE     2 BC8 36 ASN A 169  LYS A 192  GLU A 195  GLY A 225
SITE     3 BC8 36 GLY A 229  ALA A 230  PHE A 243  THR A 244
SITE     4 BC8 36 GLY A 245  SER A 246  ILE A 249  ILE A 253
SITE     5 BC8 36 GLU A 268  LEU A 269  GLY A 270  SER A 302
SITE     6 BC8 36 GLU A 399  PHE A 401  PHE A 465   MG A6701
SITE     7 BC8 36 HOH A7045  HOH A7058  HOH A7060  HOH A7061
SITE     8 BC8 36 HOH A7062  HOH A7063  HOH A7064  HOH A7159
SITE     9 BC8 36 HOH A7257  HOH A7259  HOH A7507  HOH A7508
SITE     1 BC9 35 ILE B 165  ILE B 166  PRO B 167  TRP B 168
SITE     2 BC9 35 ASN B 169  LYS B 192  GLU B 195  GLY B 225
SITE     3 BC9 35 GLY B 229  ALA B 230  PHE B 243  THR B 244
SITE     4 BC9 35 GLY B 245  SER B 246  ILE B 249  ILE B 253
SITE     5 BC9 35 GLU B 268  LEU B 269  GLY B 270  SER B 302
SITE     6 BC9 35 GLU B 399  PHE B 401  PHE B 465   MG B6702
SITE     7 BC9 35 HOH B6966  HOH B7011  HOH B7012  HOH B7013
SITE     8 BC9 35 HOH B7184  HOH B7189  HOH B7190  HOH B7191
SITE     9 BC9 35 HOH B7194  HOH B7195  HOH B7453
SITE     1 CC1 35 ILE C 165  ILE C 166  PRO C 167  TRP C 168
SITE     2 CC1 35 ASN C 169  LYS C 192  GLU C 195  GLY C 225
SITE     3 CC1 35 GLY C 229  ALA C 230  PHE C 243  THR C 244
SITE     4 CC1 35 GLY C 245  SER C 246  ILE C 249  ILE C 253
SITE     5 CC1 35 GLU C 268  LEU C 269  GLY C 270  SER C 302
SITE     6 CC1 35 GLU C 399  PHE C 401  PHE C 465   MG C6703
SITE     7 CC1 35 HOH C6999  HOH C7000  HOH C7221  HOH C7222
SITE     8 CC1 35 HOH C7223  HOH C7242  HOH C7244  HOH C7256
SITE     9 CC1 35 HOH C7257  HOH C7501  HOH C7504
SITE     1 CC2 36 ILE D 165  ILE D 166  PRO D 167  TRP D 168
SITE     2 CC2 36 ASN D 169  LYS D 192  GLU D 195  GLY D 225
SITE     3 CC2 36 GLY D 229  ALA D 230  PHE D 243  THR D 244
SITE     4 CC2 36 GLY D 245  SER D 246  ILE D 249  ILE D 253
SITE     5 CC2 36 GLU D 268  LEU D 269  GLY D 270  SER D 302
SITE     6 CC2 36 GLU D 399  PHE D 401  PHE D 465   MG D6704
SITE     7 CC2 36 HOH D7067  HOH D7068  HOH D7069  HOH D7072
SITE     8 CC2 36 HOH D7073  HOH D7074  HOH D7076  HOH D7440
SITE     9 CC2 36 HOH D7447  HOH D7448  HOH D7525  HOH D7531
SITE     1 CC3 37 ILE E 165  ILE E 166  PRO E 167  TRP E 168
SITE     2 CC3 37 ASN E 169  LYS E 192  ALA E 194  GLU E 195
SITE     3 CC3 37 GLY E 225  GLY E 229  ALA E 230  PHE E 243
SITE     4 CC3 37 THR E 244  GLY E 245  SER E 246  ILE E 249
SITE     5 CC3 37 ILE E 253  GLU E 268  LEU E 269  GLY E 270
SITE     6 CC3 37 SER E 302  GLU E 399  PHE E 401  PHE E 465
SITE     7 CC3 37 HOH E2625  HOH E2626  HOH E2627  HOH E2630
SITE     8 CC3 37 HOH E2631  HOH E2632  HOH E2866  HOH E2871
SITE     9 CC3 37 HOH E3894  HOH E4784  HOH E4785  HOH E4814
SITE    10 CC3 37  MG E6705
SITE     1 CC4 36 ILE F 165  ILE F 166  PRO F 167  TRP F 168
SITE     2 CC4 36 ASN F 169  LYS F 192  GLU F 195  GLY F 225
SITE     3 CC4 36 GLY F 229  ALA F 230  PHE F 243  THR F 244
SITE     4 CC4 36 GLY F 245  SER F 246  ILE F 249  ILE F 253
SITE     5 CC4 36 GLU F 268  LEU F 269  GLY F 270  SER F 302
SITE     6 CC4 36 GLU F 399  PHE F 401  PHE F 465  HOH F2814
SITE     7 CC4 36 HOH F2815  HOH F2833  HOH F2834  HOH F2835
SITE     8 CC4 36 HOH F2837  HOH F2838  HOH F2841  HOH F3074
SITE     9 CC4 36 HOH F3080  HOH F4917  HOH F4945   MG F6706
SITE     1 CC5 36 ILE G 165  ILE G 166  PRO G 167  TRP G 168
SITE     2 CC5 36 ASN G 169  LYS G 192  GLU G 195  GLY G 225
SITE     3 CC5 36 GLY G 229  ALA G 230  PHE G 243  THR G 244
SITE     4 CC5 36 GLY G 245  SER G 246  ILE G 249  ILE G 253
SITE     5 CC5 36 GLU G 268  LEU G 269  GLY G 270  SER G 302
SITE     6 CC5 36 GLU G 399  PHE G 401  PHE G 465  HOH G3209
SITE     7 CC5 36 HOH G3210  HOH G3211  HOH G3212  HOH G3227
SITE     8 CC5 36 HOH G4358  HOH G4359  HOH G4361  HOH G4362
SITE     9 CC5 36 HOH G4509  HOH G4654  HOH G4688   MG G6707
SITE     1 CC6 35 ILE H 165  ILE H 166  PRO H 167  TRP H 168
SITE     2 CC6 35 ASN H 169  LYS H 192  GLU H 195  GLY H 225
SITE     3 CC6 35 GLY H 229  ALA H 230  PHE H 243  THR H 244
SITE     4 CC6 35 GLY H 245  SER H 246  ILE H 249  ILE H 253
SITE     5 CC6 35 GLU H 268  LEU H 269  GLY H 270  SER H 302
SITE     6 CC6 35 GLU H 399  PHE H 401  PHE H 465  HOH H2227
SITE     7 CC6 35 HOH H2228  HOH H2231  HOH H2232  HOH H2235
SITE     8 CC6 35 HOH H2236  HOH H2237  HOH H4314  HOH H4682
SITE     9 CC6 35 HOH H4685  HOH H4743   MG H6708
SITE     1 CC7  5 GLU A 157  PRO A 158  VAL A 159  HOH A7072
SITE     2 CC7  5 TYR B 468
SITE     1 CC8  6 ILE A 146  ASP A 147  PHE A 150  HOH A7138
SITE     2 CC8  6 PHE B 459  HOH B7147
SITE     1 CC9  5 TYR A 468  GLU B 157  PRO B 158  VAL B 159
SITE     2 CC9  5 HOH B7265
SITE     1 DC1  7 VAL A 458  PHE A 459  HOH A7185  ILE B 146
SITE     2 DC1  7 ASP B 147  PHE B 150  HOH B7128
SITE     1 DC2  8 PHE C  70  GLU C 157  PRO C 158  VAL C 159
SITE     2 DC2  8 HOH C7072  HOH C7073  HOH C7451  TYR D 468
SITE     1 DC3  6 ILE C 146  ASP C 147  PHE C 150  HOH C6969
SITE     2 DC3  6 VAL D 458  PHE D 459
SITE     1 DC4  7 PHE C 350  ILE C 373  ALA C 375  ASP C 376
SITE     2 DC4  7 GLY C 378  EDO C6963  HOH C7203
SITE     1 DC5  5 TYR C 468  GLU D 157  PRO D 158  VAL D 159
SITE     2 DC5  5 HOH D7111
SITE     1 DC6  6 PHE C 459  HOH C7527  ILE D 146  ASP D 147
SITE     2 DC6  6 PHE D 150  HOH D7239
SITE     1 DC7  5 GLU E 157  PRO E 158  VAL E 159  HOH E2569
SITE     2 DC7  5 HOH E4541
SITE     1 DC8  6 ILE E 146  ASP E 147  PHE E 150  HOH E2357
SITE     2 DC8  6 PHE F 459  HOH F3085
SITE     1 DC9  7 TYR E 468  GLU F 157  PRO F 158  VAL F 159
SITE     2 DC9  7 HOH F4222  HOH F4303  HOH F4304
SITE     1 EC1  6 PHE E 459  HOH E4761  ILE F 146  ASP F 147
SITE     2 EC1  6 PHE F 150  HOH F2606
SITE     1 EC2  8 PHE F 350  ILE F 373  ALA F 375  ASP F 376
SITE     2 EC2  8 GLY F 378  HOH F2777  HOH F2779  EDO F6966
SITE     1 EC3  8 PHE G  70  GLU G 157  PRO G 158  VAL G 159
SITE     2 EC3  8 HOH G3302  HOH G3303  HOH G4755  TYR H 468
SITE     1 EC4  7 ILE G 146  ASP G 147  PHE G 150  HOH G2726
SITE     2 EC4  7 HOH G4157  HOH G4309  PHE H 459
SITE     1 EC5  6 TYR G 468  PHE H  70  GLU H 157  PRO H 158
SITE     2 EC5  6 VAL H 159  HOH H3996
SITE     1 EC6  6 PHE G 459  HOH G4513  ILE H 146  ASP H 147
SITE     2 EC6  6 PHE H 150  HOH H3013
SITE     1 EC7  5 TYR A 153  ARG A 155  HOH A7127  SER B 443
SITE     2 EC7  5 PHE D 151
SITE     1 EC8  5 GLN A  14  ASN A  41  THR A  44  GLU A  46
SITE     2 EC8  5 HOH A6983
SITE     1 EC9  3 PHE A  18  TYR A 203  HOH A6966
SITE     1 FC1  7 TYR A 441  GLN A 444  ALA A 445  HOH A7090
SITE     2 FC1  7 LEU B  72  GLN C 497  HOH C7063
SITE     1 FC2  5 SER A 443  TYR B 153  ARG B 155  HOH B7271
SITE     2 FC2  5 PHE C 151
SITE     1 FC3  6 GLN B  14  ASN B  41  THR B  44  LEU B 108
SITE     2 FC3  6 HOH B7321  HOH B7539
SITE     1 FC4  9 ARG B  97  ASP B  98  THR B 100  TYR B 101
SITE     2 FC4  9 HOH B7348  HOH B7350  ALA E   7  HOH E3841
SITE     3 FC4  9 HOH E4765
SITE     1 FC5  7 LEU A  72  TYR B 441  GLN B 444  ALA B 445
SITE     2 FC5  7 HOH B6951  GLN D 497  HOH D7253
SITE     1 FC6  5 PHE B 151  TYR C 153  ARG C 155  HOH C7453
SITE     2 FC6  5 SER D 443
SITE     1 FC7  6 ASN C  41  THR C  44  GLU C  46  LEU C 108
SITE     2 FC7  6 HOH C7328  HOH C7329
SITE     1 FC8  5 PHE C  18  TYR C 101  TYR C 203  HOH C7484
SITE     2 FC8  5 HOH C7485
SITE     1 FC9  5 GLN A 497  TYR C 441  GLN C 444  ALA C 445
SITE     2 FC9  5 LEU D  72
SITE     1 GC1  5 GLU C 347  PHE C 350  GAI C6823  HOH C7203
SITE     2 GC1  5 GLY F  45
SITE     1 GC2  5 PHE A 151  SER C 443  TYR D 153  ARG D 155
SITE     2 GC2  5 HOH D7419
SITE     1 GC3  6 ASN D  41  THR D  44  GLU D  46  HOH D6951
SITE     2 GC3  6 HOH D6952  GLU H  46
SITE     1 GC4  6 GLU D 414  TYR D 441  HOH D7193  HOH D7198
SITE     2 GC4  6 HOH D7292  LYS G 361
SITE     1 GC5  4 TYR E 153  ARG E 155  SER F 443  PHE H 151
SITE     1 GC6  4 GLN E  14  ASN E  41  THR E  44  LEU E 108
SITE     1 GC7  5 PHE E  18  TYR E 101  TYR E 203  HOH E3847
SITE     2 GC7  5 HOH E4623
SITE     1 GC8  4 SER E 443  TYR F 153  ARG F 155  PHE G 151
SITE     1 GC9  7 ASN F  41  THR F  44  GLU F  46  ILE F  48
SITE     2 GC9  7 LEU F 108  HOH F2762  HOH F2763
SITE     1 HC1  7 HOH E3765  HOH E3766  PHE F  18  TYR F 101
SITE     2 HC1  7 TYR F 203  HOH F2416  HOH F4269
SITE     1 HC2  5 LEU E  72  TYR F 441  GLN F 444  ALA F 445
SITE     2 HC2  5 GLN H 497
SITE     1 HC3  4 HOH B7527  ALA F  68  SER F  74  HOH F2706
SITE     1 HC4  4 GLY C  45  GLU F 347  HOH F2777  GAI F6826
SITE     1 HC5  5 PHE F 151  TYR G 153  ARG G 155  HOH G3827
SITE     2 HC5  5 SER H 443
SITE     1 HC6  4 ASN G  41  THR G  44  GLU G  46  HOH G3185
SITE     1 HC7  6 PHE G  18  TYR G 101  TYR G 203  HOH G2948
SITE     2 HC7  6 HOH G2949  HOH G3180
SITE     1 HC8  5 PHE E 151  SER G 443  TYR H 153  ARG H 155
SITE     2 HC8  5 HOH H4030
SITE     1 HC9  8 GLU D  46  ARG D 377  ASN H  41  THR H  44
SITE     2 HC9  8 GLU H  46  HOH H3651  HOH H3653  HOH H3655
SITE     1 IC1  5 LYS E 361  PHE H  18  TYR H 101  TYR H 203
SITE     2 IC1  5 HOH H2278
SITE     1 IC2  5 GLN F 497  LEU G  72  TYR H 441  GLN H 444
SITE     2 IC2  5 ALA H 445
CRYST1  141.211  152.487  177.200  90.00  90.00  90.00 P 21 21 21   32
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      0.007082  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006558  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005643        0.00000
      
PROCHECK
Go to PROCHECK summary
 References