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PDBsum entry 3n80

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3n80
Jmol
Contents
Protein chain
(+ 2 more) 494 a.a.
Ligands
GAI ×21
EDO ×36
Metals
_NA ×7
_MG
Waters ×4890
HEADER    OXIDOREDUCTASE                          27-MAY-10   3N80
TITLE     HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, APO FORM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 FRAGMENT: MATURE SEQUENCE, RESIDUES 18-517;
COMPND   5 SYNONYM: ALDH CLASS 2, ALDHI, ALDH-E2;
COMPND   6 EC: 1.2.1.3;
COMPND   7 ENGINEERED: 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, ALDM;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT-7-7
KEYWDS    OXIDOREDUCTASE, ALDH, ROSSMANN FOLD
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.GONZALEZ-SEGURA,T.D.HURLEY
REVDAT   1   13-APR-11 3N80    0
JRNL        AUTH   K.-K.HO,L.GONZALEZ-SEGURA,S.PEREZ-MILLER,H.WEINER,T.D.HURLEY
JRNL        TITL   CONFORMATIONAL SELECTION DURING CATALYSIS: THE ROLE OF
JRNL        TITL 2 THREONINE 244 IN ALDH2
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.-K HO,T.D.HURLEY,H.WEINER
REMARK   1  TITL   SELECTIVE ALTERATION OF THE RATE-LIMITING STEP IN CYTOSOLIC
REMARK   1  TITL 2 ALDEHYDE DEHYDROGENASE THROUGH RANDOM MUTAGENESIS
REMARK   1  REF    BIOCHEMISTRY                  V.  45  9445 2006
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 2
REMARK   1  AUTH   H.N.LARSON,J.ZHOU,Z.CHEN,J.S.STAMLER,H.WEINER,T.D.HURLEY
REMARK   1  TITL   STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF COENZYME BINDING
REMARK   1  TITL 2 TO THE INACTIVE ASIAN VARIANT OF MITOCHONDRIAL ALDEHYDE
REMARK   1  TITL 3 DEHYDROGENASE (ROLES OF RESIDUES 475 AND 487)
REMARK   1  REF    J. BIOL. CHEM.                V. 282 12940 2007
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.3.0037
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0
REMARK   3   NUMBER OF REFLECTIONS             : 599778
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) : 0.151
REMARK   3   R VALUE            (WORKING SET) : 0.149
REMARK   3   FREE R VALUE                     : 0.175
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 30068
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) : 1.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 42334
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1780
REMARK   3   BIN FREE R VALUE SET COUNT          : 2225
REMARK   3   BIN FREE R VALUE                    : 0.2120
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 30401
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 236
REMARK   3   SOLVENT ATOMS            : 4887
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 18.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.40000
REMARK   3    B22 (A**2) : -0.16000
REMARK   3    B33 (A**2) : -0.23000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.039
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.035
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 31945 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 43399 ; 1.535 ; 1.954
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4175 ;12.619 ; 5.077
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1440 ;34.740 ;24.729
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5206 ;11.776 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   162 ;17.466 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4752 ; 0.104 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24687 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 20056 ; 0.847 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 32264 ; 1.423 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11889 ; 2.492 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11064 ; 4.074 ; 4.500
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   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3N80 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059495.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-05
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) : 1.04
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : APS-1
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 599824
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : 3.100
REMARK 200  R MERGE                    (I) : 0.05600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.26700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT REFINEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1O05
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ACES (N-[2-ACETAMIDO]-2-
REMARK 280  AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE
REMARK 280  HCL, 16-17% W/V PEG 6000, PH 6.4, VAPOR DIFFUSION, TEMPERATURE
REMARK 280  292K
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       70.83100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.64100
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.14550
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.64100
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.83100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.14550
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: 26930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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: 27400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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     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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH B  3202     O    HOH E  2423     3645     2.09
REMARK 500   O    HOH C  4579     O    HOH D  4636     4556     2.16
REMARK 500   O    HOH C   650     O    HOH G  4035     3646     2.18
REMARK 500   O    HOH E  4734     O    HOH H  2040     4466     2.19
REMARK 500
REMARK 500 REMARK: NULL
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 282   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP B 282   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES
REMARK 500    ARG F  86   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG H  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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       24.30   -149.63
REMARK 500    ARG A  34        9.79     59.92
REMARK 500    THR A 197       59.87   -146.12
REMARK 500    THR A 227      -75.04   -107.82
REMARK 500    SER A 260     -103.83   -112.41
REMARK 500    LEU A 269     -156.42   -121.45
REMARK 500    TYR A 379       57.89   -102.79
REMARK 500    LYS A 469     -134.59     57.78
REMARK 500    LEU A 477      164.56     69.57
REMARK 500    ASN B  20       28.66   -148.88
REMARK 500    VAL B 120      -68.70   -108.07
REMARK 500    THR B 197       59.01   -143.65
REMARK 500    THR B 227      -74.32   -108.13
REMARK 500    SER B 260     -101.30   -109.24
REMARK 500    LEU B 269     -156.89   -118.70
REMARK 500    LYS B 469     -133.55     51.10
REMARK 500    LEU B 477      163.93     71.97
REMARK 500    ASN C  20       28.73   -153.92
REMARK 500    VAL C 120      -70.18   -111.22
REMARK 500    THR C 227      -78.04   -103.81
REMARK 500    SER C 260     -106.19   -107.38
REMARK 500    LEU C 269     -156.60   -120.45
REMARK 500    ASP C 376      -70.54    -70.09
REMARK 500    LYS C 469     -135.91     55.58
REMARK 500    LEU C 477      165.09     74.22
REMARK 500    GLN C 497      108.50   -161.41
REMARK 500    ASN D  20       26.00   -149.28
REMARK 500    THR D 227      -78.76   -103.25
REMARK 500    SER D 260     -100.39   -105.79
REMARK 500    LEU D 269     -160.03   -120.25
REMARK 500    TYR D 379       57.59    -98.05
REMARK 500    LYS D 469     -135.98     56.19
REMARK 500    LEU D 477      164.41     73.30
REMARK 500    GLN D 497      108.39   -160.61
REMARK 500    ASN E  20       26.44   -148.43
REMARK 500    VAL E 120      -70.49   -109.67
REMARK 500    THR E 197       58.20   -147.24
REMARK 500    THR E 227      -77.68   -106.40
REMARK 500    SER E 260     -101.60   -108.19
REMARK 500    LEU E 269     -156.89   -118.53
REMARK 500    TYR E 379       56.12   -101.98
REMARK 500    LYS E 469     -136.87     55.61
REMARK 500    LEU E 477      163.13     71.58
REMARK 500    ASN F  20       27.71   -150.43
REMARK 500    VAL F 120      -70.27   -108.27
REMARK 500    THR F 227      -76.98   -106.66
REMARK 500    SER F 260      -99.86   -109.20
REMARK 500    LEU F 269     -159.34   -115.79
REMARK 500    ASP F 376      -70.08    -73.23
REMARK 500    LYS F 469     -135.26     53.27
REMARK 500
REMARK 500 THIS ENTRY HAS      71 RAMACHANDRAN OUTLIERS.
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 A 509        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH A 546        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH A 599        DISTANCE =  6.34 ANGSTROMS
REMARK 525    HOH A 701        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH A1115        DISTANCE =  6.79 ANGSTROMS
REMARK 525    HOH A1116        DISTANCE =  6.81 ANGSTROMS
REMARK 525    HOH A3035        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH A3036        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH A3041        DISTANCE =  5.83 ANGSTROMS
REMARK 525    HOH A3042        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH A4883        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH B1270        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH B1273        DISTANCE =  5.42 ANGSTROMS
REMARK 525    HOH B1274        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH B1413        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH B1417        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH B1639        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH C 766        DISTANCE =  5.55 ANGSTROMS
REMARK 525    HOH C 770        DISTANCE =  5.80 ANGSTROMS
REMARK 525    HOH C 872        DISTANCE =  6.84 ANGSTROMS
REMARK 525    HOH C 948        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH C 965        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH C 980        DISTANCE =  5.48 ANGSTROMS
REMARK 525    HOH C1164        DISTANCE =  5.86 ANGSTROMS
REMARK 525    HOH D 696        DISTANCE =  6.87 ANGSTROMS
REMARK 525    HOH D 718        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH D 719        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH D 725        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH D1505        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH D3106        DISTANCE =  6.08 ANGSTROMS
REMARK 525    HOH E2273        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH E2360        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH E2602        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH E2603        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH E2751        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH E3401        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH F 815        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH F2157        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH F2217        DISTANCE =  5.90 ANGSTROMS
REMARK 525    HOH F4099        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH F4478        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH F4479        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH F4481        DISTANCE =  6.93 ANGSTROMS
REMARK 525    HOH G2124        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH G2801        DISTANCE =  5.80 ANGSTROMS
REMARK 525    HOH G2883        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH G2917        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH G2918        DISTANCE =  5.75 ANGSTROMS
REMARK 525    HOH G2919        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH G2923        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH G2924        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH G3940        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH G3952        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH G4051        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH G4192        DISTANCE =  7.06 ANGSTROMS
REMARK 525    HOH H3313        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH H3567        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH H3614        DISTANCE =  6.73 ANGSTROMS
REMARK 525    HOH H3615        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH H3616        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH H3911        DISTANCE =  6.25 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 H 609  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR H  36   O
REMARK 620 2 HOH H1978   O    82.0
REMARK 620 3 HOH H1976   O    89.1  90.4
REMARK 620 4 HOH H1979   O    89.5  84.4 174.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA D 604  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL D  40   O
REMARK 620 2 GLN D 196   O   166.0
REMARK 620 3 ASP D 109   O   100.1  93.0
REMARK 620 4 ASP D 109   OD1 102.3  84.0  83.5
REMARK 620 5 THR D  39   OG1 102.1  70.5 137.9  57.1
REMARK 620 6 HOH D3100   O    91.7  83.0  91.9 165.9 122.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA H 608  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN H 196   O
REMARK 620 2 VAL H  40   O   164.8
REMARK 620 3 ASP H 109   O    92.5 102.2
REMARK 620 4 ASP H 109   OD1  84.1 101.7  81.5
REMARK 620 5 THR H  39   OG1  70.5 100.8 135.2  56.3
REMARK 620 6 HOH H4243   O    89.0  90.8  76.0 156.2 141.2
REMARK 620 7 HOH H4242   O    82.5  82.5 155.9 121.0  65.0  80.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA F 606  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL F  40   O
REMARK 620 2 GLN F 196   O   160.5
REMARK 620 3 ASP F 109   O   102.7  94.3
REMARK 620 4 ASP F 109   OD1 105.8  85.7  82.6
REMARK 620 5 THR F  39   OG1  98.7  74.0 138.2  57.0
REMARK 620 6 HOH F3832   O    88.3  83.5  85.4 163.1 131.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA E 605  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL E  40   O
REMARK 620 2 GLN E 196   O   164.1
REMARK 620 3 ASP E 109   O   100.3  93.9
REMARK 620 4 ASP E 109   OD1 104.9  83.9  82.4
REMARK 620 5 THR E  39   OG1 102.3  71.2 137.0  56.7
REMARK 620 6 HOH E3502   O    92.7  78.9  94.9 162.3 119.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B 602  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 196   O
REMARK 620 2 ASP B 109   O    93.9
REMARK 620 3 VAL B  40   O   166.8  98.9
REMARK 620 4 ASP B 109   OD1  82.7  81.0 102.5
REMARK 620 5 THR B  39   OG1  71.3 135.7 101.2  56.3
REMARK 620 6 HOH B 578   O    85.8  94.3  90.0 167.2 124.6
REMARK 620 7 HOH B1635   O    83.6 155.5  83.4 122.5  66.4  61.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA C 603  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 196   O
REMARK 620 2 VAL C  40   O   162.2
REMARK 620 3 ASP C 109   O    96.9  98.9
REMARK 620 4 ASP C 109   OD1  87.3 103.1  81.2
REMARK 620 5 THR C  39   OG1  73.1 100.2 137.1  57.2
REMARK 620 6 HOH C 606   O    81.3  90.3  91.1 165.5 126.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA G 607  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL G  40   O
REMARK 620 2 GLN G 196   O   162.6
REMARK 620 3 ASP G 109   O   101.1  94.3
REMARK 620 4 ASP G 109   OD1 102.6  87.4  82.1
REMARK 620 5 THR G  39   OG1  99.8  73.3 138.1  58.0
REMARK 620 6 HOH G2861   O    91.7  80.0  90.4 164.9 124.8
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 921
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 941
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 912
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 922
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 942
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 823
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 913
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 923
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 943
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 963
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 833
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 914
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 944
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 815
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 915
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 925
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 826
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 839
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 916
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 919
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 926
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 946
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 956
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 966
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 817
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 838
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 917
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 927
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 818
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 918
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 928
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 948
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N81   RELATED DB: PDB
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE,
REMARK 900 APO FORM
REMARK 900 RELATED ID: 3N82   RELATED DB: PDB
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE,
REMARK 900 NADH COMPLEX
REMARK 900 RELATED ID: 3N83   RELATED DB: PDB
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE,
REMARK 900 NAD COMPLEX
DBREF  3N80 A    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  3N80 B    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  3N80 C    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  3N80 D    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  3N80 E    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  3N80 F    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  3N80 G    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  3N80 H    1   500  UNP    P05091   ALDH2_HUMAN     18    517
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 CSO 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 CSO 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 CSO 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 CSO 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 CSO 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 CSO 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 CSO 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 CSO 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
MODRES 3N80 CSO A  302  CYS  S-HYDROXYCYSTEINE
MODRES 3N80 CSO B  302  CYS  S-HYDROXYCYSTEINE
MODRES 3N80 CSO C  302  CYS  S-HYDROXYCYSTEINE
MODRES 3N80 CSO D  302  CYS  S-HYDROXYCYSTEINE
MODRES 3N80 CSO E  302  CYS  S-HYDROXYCYSTEINE
MODRES 3N80 CSO F  302  CYS  S-HYDROXYCYSTEINE
MODRES 3N80 CSO G  302  CYS  S-HYDROXYCYSTEINE
MODRES 3N80 CSO H  302  CYS  S-HYDROXYCYSTEINE
HET    CSO  A 302      11
HET    CSO  B 302      11
HET    CSO  C 302      11
HET    CSO  D 302      11
HET    CSO  E 302      11
HET    CSO  F 302      11
HET    CSO  G 302      11
HET    CSO  H 302      11
HET    GAI  A 801       4
HET    GAI  A 811       4
HET    GAI  A 812       4
HET    EDO  A 901       4
HET    EDO  A 910       4
HET    EDO  A 911       4
HET    EDO  A 921       4
HET    EDO  A 941       4
HET     NA  B 602       1
HET    GAI  B 802       4
HET    EDO  B 902       4
HET    EDO  B 909       4
HET    EDO  B 912       4
HET    EDO  B 922       4
HET    EDO  B 942       4
HET     NA  C 603       1
HET    GAI  C 803       4
HET    GAI  C 813       4
HET    GAI  C 823       4
HET    EDO  C 903       4
HET    EDO  C 913       4
HET    EDO  C 923       4
HET    EDO  C 943       4
HET    EDO  C 963       4
HET     NA  D 604       1
HET    GAI  D 804       4
HET    GAI  D 814       4
HET    GAI  D 833       4
HET    EDO  D 904       4
HET    EDO  D 914       4
HET    EDO  D 944       4
HET     NA  E 605       1
HET    GAI  E 805       4
HET    GAI  E 815       4
HET    EDO  E 905       4
HET    EDO  E 915       4
HET    EDO  E 920       4
HET    EDO  E 925       4
HET     NA  F 606       1
HET    GAI  F 806       4
HET    GAI  F 816       4
HET    GAI  F 826       4
HET    GAI  F 839       4
HET    EDO  F 906       4
HET    EDO  F 916       4
HET    EDO  F 919       4
HET    EDO  F 926       4
HET    EDO  F 946       4
HET    EDO  F 956       4
HET    EDO  F 966       4
HET     NA  G 607       1
HET    GAI  G 807       4
HET    GAI  G 817       4
HET    GAI  G 838       4
HET    EDO  G 907       4
HET    EDO  G 917       4
HET    EDO  G 927       4
HET     NA  H 608       1
HET     MG  H 609       1
HET    GAI  H 808       4
HET    GAI  H 818       4
HET    EDO  H 908       4
HET    EDO  H 918       4
HET    EDO  H 928       4
HET    EDO  H 948       4
HETNAM     CSO S-HYDROXYCYSTEINE
HETNAM     GAI GUANIDINE
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM      NA SODIUM ION
HETNAM      MG MAGNESIUM ION
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   1  CSO    8(C3 H7 N O3 S)
FORMUL   9  GAI    21(C H5 N3)
FORMUL  12  EDO    36(C2 H6 O2)
FORMUL  17   NA    7(NA 1+)
FORMUL  67   MG    MG 2+
FORMUL  74  HOH   *4887(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 ILE A  314  ARG A  329  1                                  16
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 GLU B  312  ARG B  329  1                                  18
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  HIS C  235  1                                   9
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 ILE E  314  ARG E  329  1                                  16
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  VAL B 385   N  LEU B 368
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  THR D 143   N  GLY A 141
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 491   N  TYR D 153
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  LEU C 368   O  VAL C 385
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  CYS A 162   O  VAL A 188
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  VAL A 385   N  LEU A 368
SHEET    3   E20 VAL A 404  PHE A 410  1  O  MET A 405   N  PHE A 386
SHEET    4   E20 ARG A 307  GLN A 311  1  N  VAL A 310   O  LEU A 408
SHEET    5   E20 PRO A 274  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  GLY C 141   N  THR B 143
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  PHE D 386   O  MET D 405
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LEU D 368   O  VAL D 385
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  VAL F 385   N  LEU F 368
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  VAL F 310   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  GLY H 141   N  THR E 143
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  LEU G 368   O  VAL G 385
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  VAL E 385   N  LEU E 368
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  VAL H 310
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  LEU H 368   O  VAL H 385
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  CYS H 162   O  VAL H 188
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         C  ACYS A 301                 N   CSO A 302     1555   1555  1.33
LINK         C  BCYS A 301                 N   CSO A 302     1555   1555  1.32
LINK         C   CSO A 302                 N   CYS A 303     1555   1555  1.32
LINK         C  ACYS B 301                 N   CSO B 302     1555   1555  1.34
LINK         C  BCYS B 301                 N   CSO B 302     1555   1555  1.33
LINK         C   CSO B 302                 N   CYS B 303     1555   1555  1.32
LINK         C  ACYS C 301                 N   CSO C 302     1555   1555  1.33
LINK         C  BCYS C 301                 N   CSO C 302     1555   1555  1.32
LINK         C   CSO C 302                 N   CYS C 303     1555   1555  1.32
LINK         C  ACYS D 301                 N   CSO D 302     1555   1555  1.33
LINK         C  BCYS D 301                 N   CSO D 302     1555   1555  1.32
LINK         C   CSO D 302                 N   CYS D 303     1555   1555  1.32
LINK         C  ACYS E 301                 N   CSO E 302     1555   1555  1.34
LINK         C  BCYS E 301                 N   CSO E 302     1555   1555  1.32
LINK         C   CSO E 302                 N   CYS E 303     1555   1555  1.33
LINK         C  ACYS F 301                 N   CSO F 302     1555   1555  1.34
LINK         C  BCYS F 301                 N   CSO F 302     1555   1555  1.33
LINK         C   CSO F 302                 N   CYS F 303     1555   1555  1.32
LINK         C  ACYS G 301                 N   CSO G 302     1555   1555  1.34
LINK         C  BCYS G 301                 N   CSO G 302     1555   1555  1.33
LINK         C   CSO G 302                 N   CYS G 303     1555   1555  1.32
LINK         C  ACYS H 301                 N   CSO H 302     1555   1555  1.33
LINK         C  BCYS H 301                 N   CSO H 302     1555   1555  1.33
LINK         C   CSO H 302                 N   CYS H 303     1555   1555  1.32
LINK         O   THR H  36                MG    MG H 609     1555   1555  2.18
LINK         O   VAL D  40                NA    NA D 604     1555   1555  2.29
LINK         O   GLN H 196                NA    NA H 608     1555   1555  2.30
LINK         O   VAL F  40                NA    NA F 606     1555   1555  2.30
LINK         O   VAL E  40                NA    NA E 605     1555   1555  2.31
LINK         O   GLN B 196                NA    NA B 602     1555   1555  2.33
LINK         O   GLN C 196                NA    NA C 603     1555   1555  2.33
LINK         O   VAL G  40                NA    NA G 607     1555   1555  2.34
LINK         O   GLN D 196                NA    NA D 604     1555   1555  2.35
LINK         O   VAL H  40                NA    NA H 608     1555   1555  2.36
LINK         O   GLN F 196                NA    NA F 606     1555   1555  2.36
LINK         O   GLN G 196                NA    NA G 607     1555   1555  2.37
LINK         O   ASP G 109                NA    NA G 607     1555   1555  2.37
LINK         O   GLN E 196                NA    NA E 605     1555   1555  2.37
LINK         O   ASP E 109                NA    NA E 605     1555   1555  2.39
LINK         O   VAL C  40                NA    NA C 603     1555   1555  2.39
LINK         O   ASP D 109                NA    NA D 604     1555   1555  2.39
LINK         O   ASP B 109                NA    NA B 602     1555   1555  2.39
LINK         O   VAL B  40                NA    NA B 602     1555   1555  2.40
LINK         O   ASP F 109                NA    NA F 606     1555   1555  2.46
LINK         OD1 ASP B 109                NA    NA B 602     1555   1555  2.47
LINK         O   ASP C 109                NA    NA C 603     1555   1555  2.47
LINK         O   ASP H 109                NA    NA H 608     1555   1555  2.47
LINK         OD1 ASP F 109                NA    NA F 606     1555   1555  2.48
LINK         OD1 ASP D 109                NA    NA D 604     1555   1555  2.48
LINK         OD1 ASP C 109                NA    NA C 603     1555   1555  2.50
LINK         OD1 ASP E 109                NA    NA E 605     1555   1555  2.50
LINK         OD1 ASP G 109                NA    NA G 607     1555   1555  2.51
LINK         OD1 ASP H 109                NA    NA H 608     1555   1555  2.58
LINK         OG1 THR F  39                NA    NA F 606     1555   1555  2.99
LINK         OG1 THR B  39                NA    NA B 602     1555   1555  3.04
LINK         OG1 THR E  39                NA    NA E 605     1555   1555  3.04
LINK         OG1 THR C  39                NA    NA C 603     1555   1555  3.05
LINK         OG1 THR G  39                NA    NA G 607     1555   1555  3.06
LINK         OG1 THR D  39                NA    NA D 604     1555   1555  3.06
LINK         OG1 THR H  39                NA    NA H 608     1555   1555  3.16
LINK        NA    NA B 602                 O   HOH B 578     1555   1555  2.24
LINK        NA    NA F 606                 O   HOH F3832     1555   1555  2.25
LINK        MG    MG H 609                 O   HOH H1978     1555   1555  2.27
LINK        MG    MG H 609                 O   HOH H1976     1555   1555  2.27
LINK        MG    MG H 609                 O   HOH H1979     1555   1555  2.30
LINK        NA    NA C 603                 O   HOH C 606     1555   1555  2.32
LINK        NA    NA G 607                 O   HOH G2861     1555   1555  2.33
LINK        NA    NA H 608                 O   HOH H4243     1555   1555  2.33
LINK        NA    NA D 604                 O   HOH D3100     1555   1555  2.36
LINK        NA    NA E 605                 O   HOH E3502     1555   1555  2.45
LINK        NA    NA H 608                 O   HOH H4242     1555   1555  2.84
LINK        NA    NA B 602                 O   HOH B1635     1555   1555  2.91
SITE     1 AC1  6 GLU A 157  PRO A 158  VAL A 159  HOH A 618
SITE     2 AC1  6 HOH A 619  TYR B 468
SITE     1 AC2  7 ILE A 146  ASP A 147  PHE A 150  HOH A1033
SITE     2 AC2  7 HOH A1034  VAL B 458  PHE B 459
SITE     1 AC3  6 PHE A 459  HOH A 708  HOH A1119  ILE B 146
SITE     2 AC3  6 ASP B 147  PHE B 150
SITE     1 AC4  4 TYR A 153  ARG A 155  SER B 443  PHE D 151
SITE     1 AC5  6 HIS A 140  GLY A 141  LYS A 142  HIS D 140
SITE     2 AC5  6 GLY D 141  LYS D 142
SITE     1 AC6  5 GLN A  14  ASN A  41  THR A  44  GLU A  46
SITE     2 AC6  5 LEU A 108
SITE     1 AC7  5 PHE A  18  TYR A 101  TYR A 203  HOH A 522
SITE     2 AC7  5 HOH A 525
SITE     1 AC8  7 TYR A 441  GLN A 444  ALA A 445  HOH A 519
SITE     2 AC8  7 HOH A 549  LEU B  72  GLN C 497
SITE     1 AC9  6 THR B  39  VAL B  40  ASP B 109  GLN B 196
SITE     2 AC9  6 HOH B 578  HOH B1635
SITE     1 BC1  7 TYR A 468  PHE B  70  GLU B 157  PRO B 158
SITE     2 BC1  7 VAL B 159  HOH B1309  HOH B1316
SITE     1 BC2  5 SER A 443  TYR B 153  ARG B 155  HOH B1318
SITE     2 BC2  5 PHE C 151
SITE     1 BC3  6 HIS B 140  GLY B 141  LYS B 142  HIS C 140
SITE     2 BC3  6 GLY C 141  LYS C 142
SITE     1 BC4  5 GLN B  14  ASN B  41  THR B  44  LEU B 108
SITE     2 BC4  5 HOH B1439
SITE     1 BC5  9 ARG B  97  ASP B  98  THR B 100  TYR B 101
SITE     2 BC5  9 HOH B1464  HOH B1466  ALA E   7  HOH E3463
SITE     3 BC5  9 HOH E4303
SITE     1 BC6  6 TYR B 441  GLN B 444  ALA B 445  HOH B 519
SITE     2 BC6  6 HOH B 748  GLN D 497
SITE     1 BC7  5 THR C  39  VAL C  40  ASP C 109  GLN C 196
SITE     2 BC7  5 HOH C 606
SITE     1 BC8  6 GLU C 157  PRO C 158  VAL C 159  HOH C 616
SITE     2 BC8  6 HOH C 617  TYR D 468
SITE     1 BC9  5 ILE C 146  ASP C 147  PHE C 150  HOH C 506
SITE     2 BC9  5 PHE D 459
SITE     1 CC1  7 PHE C 350  ILE C 373  ALA C 375  ASP C 376
SITE     2 CC1  7 GLY C 378  EDO C 963  HOH C4557
SITE     1 CC2  5 PHE B 151  TYR C 153  ARG C 155  HOH C1555
SITE     2 CC2  5 SER D 443
SITE     1 CC3  5 ASN C  41  THR C  44  LEU C 108  HOH C 954
SITE     2 CC3  5 HOH C 955
SITE     1 CC4  5 PHE C  18  TYR C 101  TYR C 203  HOH C1751
SITE     2 CC4  5 HOH C4659
SITE     1 CC5  7 GLN A 497  TYR C 441  GLN C 444  ALA C 445
SITE     2 CC5  7 HOH C 597  HOH C1399  LEU D  72
SITE     1 CC6  5 GLU C 347  PHE C 350  GAI C 823  HOH C4557
SITE     2 CC6  5 GLY F  45
SITE     1 CC7  5 THR D  39  VAL D  40  ASP D 109  GLN D 196
SITE     2 CC7  5 HOH D3100
SITE     1 CC8  6 TYR C 468  GLU D 157  PRO D 158  VAL D 159
SITE     2 CC8  6 HOH D 746  HOH D 756
SITE     1 CC9  6 PHE C 459  ILE D 146  ASP D 147  PHE D 150
SITE     2 CC9  6 HOH D 728  HOH D1790
SITE     1 DC1  7 GLN D  14  PRO D  15  LEU D 108  HOH D 507
SITE     2 DC1  7 HOH D 508  HOH D 509  HOH H3296
SITE     1 DC2  5 PHE A 151  SER C 443  TYR D 153  ARG D 155
SITE     2 DC2  5 HOH D3044
SITE     1 DC3  6 ASN D  41  THR D  44  GLU D  46  HOH D 508
SITE     2 DC3  6 HOH D 509  GLU H  46
SITE     1 DC4  6 GLU D 414  TYR D 441  HOH D 611  HOH D 658
SITE     2 DC4  6 HOH D1158  LYS G 361
SITE     1 DC5  5 THR E  39  VAL E  40  ASP E 109  GLN E 196
SITE     2 DC5  5 HOH E3502
SITE     1 DC6  6 PHE E  70  GLU E 157  PRO E 158  VAL E 159
SITE     2 DC6  6 HOH E4095  TYR F 468
SITE     1 DC7  6 ILE E 146  ASP E 147  PHE E 150  HOH E2116
SITE     2 DC7  6 PHE F 459  HOH F2775
SITE     1 DC8  5 TYR E 153  ARG E 155  HOH E4165  SER F 443
SITE     2 DC8  5 PHE H 151
SITE     1 DC9  5 GLN E  14  ASN E  41  THR E  44  GLU E  46
SITE     2 DC9  5 LEU E 108
SITE     1 EC1  6 HIS E 140  GLY E 141  LYS E 142  HIS H 140
SITE     2 EC1  6 GLY H 141  LYS H 142
SITE     1 EC2  4 PHE E  18  TYR E 101  TYR E 203  HOH E3469
SITE     1 EC3  5 THR F  39  VAL F  40  ASP F 109  GLN F 196
SITE     2 EC3  5 HOH F3832
SITE     1 EC4  6 TYR E 468  GLU F 157  PRO F 158  VAL F 159
SITE     2 EC4  6 HOH F3882  HOH F3883
SITE     1 EC5  6 PHE E 459  HOH E4299  ILE F 146  ASP F 147
SITE     2 EC5  6 PHE F 150  HOH F2347
SITE     1 EC6  7 PHE F 350  ILE F 373  ALA F 375  ASP F 376
SITE     2 EC6  7 GLY F 378  EDO F 966  HOH F2504
SITE     1 EC7  9 ALA F 326  LYS F 327  ARG F 329  VAL F 331
SITE     2 EC7  9 PRO F 383  HOH F2185  HOH F2186  HOH F4668
SITE     3 EC7  9 HOH F4795
SITE     1 EC8  5 SER E 443  TYR F 153  ARG F 155  HOH F3874
SITE     2 EC8  5 PHE G 151
SITE     1 EC9  6 ASN F  41  THR F  44  GLU F  46  LEU F 108
SITE     2 EC9  6 HOH F2489  HOH F2490
SITE     1 FC1  6 HIS F 140  GLY F 141  LYS F 142  HIS G 140
SITE     2 FC1  6 GLY G 141  LYS G 142
SITE     1 FC2  7 ARG E 321  HOH E3393  HOH E3394  TYR F 101
SITE     2 FC2  7 TYR F 203  HOH F2173  HOH F3848
SITE     1 FC3  7 LEU E  72  TYR F 441  GLN F 444  ALA F 445
SITE     2 FC3  7 HOH F2734  HOH F2735  GLN H 497
SITE     1 FC4  4 HOH B3215  ALA F  68  SER F  74  HOH F2437
SITE     1 FC5  4 GLY C  45  GLU F 347  GAI F 826  HOH F2504
SITE     1 FC6  5 THR G  39  VAL G  40  ASP G 109  GLN G 196
SITE     2 FC6  5 HOH G2861
SITE     1 FC7  8 PHE G  70  GLU G 157  PRO G 158  VAL G 159
SITE     2 FC7  8 HOH G2959  HOH G2960  HOH G4293  TYR H 468
SITE     1 FC8  7 ILE G 146  ASP G 147  PHE G 150  HOH G3741
SITE     2 FC8  7 HOH G3888  VAL H 458  PHE H 459
SITE     1 FC9  5 ALA G 326  LYS G 327  ARG G 329  PRO G 383
SITE     2 FC9  5 HOH G2832
SITE     1 GC1  5 PHE F 151  TYR G 153  ARG G 155  HOH G3449
SITE     2 GC1  5 SER H 443
SITE     1 GC2  3 ASN G  41  THR G  44  GLU G  46
SITE     1 GC3  5 PHE G  18  TYR G 101  TYR G 203  HOH G2647
SITE     2 GC3  5 HOH G2856
SITE     1 GC4  6 THR H  39  VAL H  40  ASP H 109  GLN H 196
SITE     2 GC4  6 HOH H4242  HOH H4243
SITE     1 GC5  5 HOH D 502  THR H  36  HOH H1976  HOH H1978
SITE     2 GC5  5 HOH H1979
SITE     1 GC6  6 PHE H  70  GLU H 157  PRO H 158  VAL H 159
SITE     2 GC6  6 HOH H3602  HOH H4209
SITE     1 GC7  5 PHE G 459  HOH G4070  ILE H 146  ASP H 147
SITE     2 GC7  5 PHE H 150
SITE     1 GC8  5 PHE E 151  SER G 443  TYR H 153  ARG H 155
SITE     2 GC8  5 HOH H3634
SITE     1 GC9  8 GLU D  46  ARG D 377  ASN H  41  THR H  44
SITE     2 GC9  8 GLU H  46  HOH H3290  HOH H3292  HOH H3294
SITE     1 HC1  6 LYS E 361  HOH E3327  PHE H  18  TYR H 101
SITE     2 HC1  6 TYR H 203  HOH H2038
SITE     1 HC2  7 GLN F 497  LEU G  72  TYR H 441  GLN H 444
SITE     2 HC2  7 ALA H 445  HOH H3409  HOH H4298
CRYST1  141.662  152.291  177.282  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      0.007059  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006566  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005641        0.00000
      
PROCHECK
Go to PROCHECK summary
 References