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PDBsum entry 1o05

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Top Page protein metals Protein-protein interface(s) links
Oxidoreductase PDB id
1o05
Jmol
Contents
Protein chain
(+ 2 more) 494 a.a. *
Metals
_NA ×8
Waters ×3210
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          20-FEB-03   1O05
TITLE     APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 FRAGMENT: COMPLETE MATURE SEQUENCE (DOES NOT CONTAIN
COMPND   5 MITOCHONDRIAL LEADER SEQUENCE).;
COMPND   6 SYNONYM: ALDH CLASS 2, ALDHI, ALDH-E2;
COMPND   7 EC: 1.2.1.3;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: ALDH2 OR ALDM;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET7-7
KEYWDS    ALDH, NAD, NADH, ISOMERIZATION, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.D.HURLEY,S.PEREZ-MILLER,H.BREEN
REVDAT   3   24-FEB-09 1O05    1       VERSN
REVDAT   2   24-JUN-03 1O05    1       JRNL
REVDAT   1   04-MAR-03 1O05    0
JRNL        AUTH   T.D.HURLEY,S.PEREZ-MILLER,H.BREEN
JRNL        TITL   ORDER AND DISORDER IN MITOCHONDRIAL ALDEHYDE
JRNL        TITL 2 DEHYDROGENASE
JRNL        REF    CHEM.BIOL.INTERACT.           V.130-     3 2001
JRNL        REFN                   ISSN 0009-2797
JRNL        PMID   11306026
JRNL        DOI    10.1016/S0009-2797(00)00217-9
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.J.PEREZ-MILLER,T.D.HURLEY
REMARK   1  TITL   COENZYME ISOMERIZATION IS INTEGRAL TO CATALYSIS IN
REMARK   1  TITL 2 ALDEHYDE DEHYDROGENASE
REMARK   1  REF    BIOCHEMISTRY                  V.  42  7100 2003
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  DOI    10.1021/BI034182W
REMARK   2
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.96
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 5593690.140
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.7
REMARK   3   NUMBER OF REFLECTIONS             : 165412
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 SET) : 0.174
REMARK   3   FREE R VALUE                     : 0.216
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 8362
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10937
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190
REMARK   3   BIN FREE R VALUE                    : 0.2650
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 572
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 30384
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 8
REMARK   3   SOLVENT ATOMS            : 3210
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 12.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.55000
REMARK   3    B22 (A**2) : 0.09000
REMARK   3    B33 (A**2) : -2.64000
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21
REMARK   3   ESD FROM SIGMAA              (A) : 0.20
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.27
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.27
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.13
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.080 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.640 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.010 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.820 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.30
REMARK   3   BSOL        : 10.00
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN.PARAM
REMARK   3  PARAMETER FILE  2  : WATER.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD TARGET USING
REMARK   3  AMPLITUDES
REMARK   4
REMARK   4 1O05 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-03.
REMARK 100 THE RCSB ID CODE IS RCSB018408.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-99
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 6.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200HB
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 165756
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : 0.07200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.21400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1CW3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ACES, PEG 6000, GUANIDINE HCL,
REMARK 280  MGCL2, DTT., PH 6.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       70.59000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.56000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.97000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.56000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.59000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.97000
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: 21270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 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: 21320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     SER A     1
REMARK 465     ALA A     2
REMARK 465     ALA A     3
REMARK 465     ALA A     4
REMARK 465     THR A     5
REMARK 465     GLN A     6
REMARK 465     SER B     1
REMARK 465     ALA B     2
REMARK 465     ALA B     3
REMARK 465     ALA B     4
REMARK 465     THR B     5
REMARK 465     GLN B     6
REMARK 465     SER C     1
REMARK 465     ALA C     2
REMARK 465     ALA C     3
REMARK 465     ALA C     4
REMARK 465     THR C     5
REMARK 465     GLN C     6
REMARK 465     SER D     1
REMARK 465     ALA D     2
REMARK 465     ALA D     3
REMARK 465     ALA D     4
REMARK 465     THR D     5
REMARK 465     GLN D     6
REMARK 465     SER E     1
REMARK 465     ALA E     2
REMARK 465     ALA E     3
REMARK 465     ALA E     4
REMARK 465     THR E     5
REMARK 465     GLN E     6
REMARK 465     SER F     1
REMARK 465     ALA F     2
REMARK 465     ALA F     3
REMARK 465     ALA F     4
REMARK 465     THR F     5
REMARK 465     GLN F     6
REMARK 465     SER G     1
REMARK 465     ALA G     2
REMARK 465     ALA G     3
REMARK 465     ALA G     4
REMARK 465     THR G     5
REMARK 465     GLN G     6
REMARK 465     SER H     1
REMARK 465     ALA H     2
REMARK 465     ALA H     3
REMARK 465     ALA H     4
REMARK 465     THR H     5
REMARK 465     GLN H     6
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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       20.27   -152.45
REMARK 500    VAL A 120      -66.38   -104.85
REMARK 500    THR A 227      -76.38   -104.01
REMARK 500    SER A 260     -114.96    -99.68
REMARK 500    LEU A 269     -157.22   -106.83
REMARK 500    LYS A 272       58.79   -155.02
REMARK 500    TYR A 379       53.68   -113.60
REMARK 500    LYS A 469     -130.99     50.91
REMARK 500    LEU A 477      164.73     74.90
REMARK 500    ASN B  20       26.04   -151.08
REMARK 500    VAL B 120      -73.40   -105.31
REMARK 500    THR B 227      -79.76   -104.41
REMARK 500    SER B 260     -108.45    -98.18
REMARK 500    LEU B 269     -161.97   -107.10
REMARK 500    LYS B 272       57.83   -141.05
REMARK 500    GLN B 300       56.79    -93.79
REMARK 500    LYS B 469     -132.96     52.83
REMARK 500    LEU B 477      162.24     75.06
REMARK 500    GLN B 497      111.86   -160.81
REMARK 500    ASN C  20       31.33   -151.00
REMARK 500    ASN C  26       16.98     59.15
REMARK 500    VAL C 120      -71.87   -109.63
REMARK 500    THR C 227      -77.70   -104.31
REMARK 500    SER C 260     -108.97    -98.46
REMARK 500    LEU C 269     -158.85   -104.39
REMARK 500    LYS C 272       56.21   -150.54
REMARK 500    LYS C 469     -129.87     52.43
REMARK 500    LEU C 477      158.52     71.47
REMARK 500    ASN D  20       25.26   -150.90
REMARK 500    VAL D 120      -69.34   -107.02
REMARK 500    THR D 227      -83.24    -99.97
REMARK 500    SER D 260     -109.01    -93.55
REMARK 500    LEU D 269     -159.31   -100.67
REMARK 500    LYS D 272       54.60   -151.70
REMARK 500    TYR D 379       53.82   -106.62
REMARK 500    LYS D 469     -124.53     49.63
REMARK 500    LEU D 477      161.94     75.75
REMARK 500    GLN D 497      111.46   -161.76
REMARK 500    ASN E  20       29.00   -153.66
REMARK 500    VAL E 120      -70.06   -108.35
REMARK 500    THR E 227      -84.15   -101.70
REMARK 500    SER E 260     -108.24    -95.98
REMARK 500    LYS E 272       57.26   -149.23
REMARK 500    TYR E 379       59.55    -97.57
REMARK 500    PRO E 403       59.02    -69.28
REMARK 500    LYS E 469     -129.95     52.42
REMARK 500    LEU E 477      163.94     75.69
REMARK 500    ASN F  20       29.08   -150.45
REMARK 500    ARG F  34       -0.26     75.40
REMARK 500    VAL F 120      -69.57   -106.26
REMARK 500    THR F 227      -79.14   -104.85
REMARK 500    SER F 260     -108.64    -97.00
REMARK 500    LEU F 269     -164.01   -101.26
REMARK 500    LYS F 272       56.94   -153.23
REMARK 500    LYS F 469     -126.81     52.74
REMARK 500    LEU F 477      159.05     71.66
REMARK 500    GLN F 497      108.56   -162.71
REMARK 500    ASN G  20       27.11   -151.15
REMARK 500    ARG G  34       -0.67     71.20
REMARK 500    VAL G 120      -72.36   -103.49
REMARK 500    THR G 227      -76.03   -106.51
REMARK 500    SER G 260     -114.69    -96.18
REMARK 500    LEU G 269     -163.33   -104.21
REMARK 500    LYS G 272       55.33   -145.13
REMARK 500    TYR G 379       58.52   -110.60
REMARK 500    LYS G 469     -132.98     50.04
REMARK 500    LEU G 477      161.02     70.94
REMARK 500    ASN H  20       21.78   -146.96
REMARK 500    ASP H  98       30.42    -99.53
REMARK 500    VAL H 120      -73.91   -102.82
REMARK 500    THR H 227      -77.62   -102.13
REMARK 500    SER H 260     -116.50    -95.96
REMARK 500    LEU H 269     -163.27   -107.19
REMARK 500    LYS H 272       56.33   -149.89
REMARK 500    TYR H 379       58.94   -104.38
REMARK 500    LYS H 411      -64.42   -105.93
REMARK 500    LYS H 469     -135.12     52.97
REMARK 500    LEU H 477      163.54     71.44
REMARK 500    GLN H 497      113.29   -164.32
REMARK 500
REMARK 500 REMARK: NULL
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                              NA A5001  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 196   O
REMARK 620 2 HOH A5307   O    85.8
REMARK 620 3 VAL A  40   O   173.9 100.1
REMARK 620 4 ASP A 109   O    89.9  78.5  92.6
REMARK 620 5 ASP A 109   OD1  82.4 148.0  93.1  71.8
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B5002  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B  40   O
REMARK 620 2 ASP B 109   O   101.6
REMARK 620 3 ASP B 109   OD1  99.3  80.6
REMARK 620 4 GLN B 196   O   162.0  96.4  84.2
REMARK 620 5 HOH B5298   O   103.1  74.0 148.9  81.1
REMARK 620 6 HOH B5291   O    86.3 159.3 117.3  76.5  85.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA E5005  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL E  40   O
REMARK 620 2 ASP E 109   O   101.3
REMARK 620 3 GLN E 196   O   159.9  98.3
REMARK 620 4 HOH E2942   O    93.3  84.4  83.9
REMARK 620 5 ASP E 109   OD1 101.0  82.5  86.2 162.2
REMARK 620 6 HOH E2575   O    84.7 153.5  75.7  69.4 122.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA F5006  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F2891   O
REMARK 620 2 GLU F  96   OE1 109.0
REMARK 620 3 ARG F  99   NH2  89.9  96.0
REMARK 620 4 HOH F1374   O   119.1 104.7 134.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA G5007  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 196   O
REMARK 620 2 VAL G  40   O   167.6
REMARK 620 3 ASP G 109   O    92.3  96.8
REMARK 620 4 ASP G 109   OD1  91.5  97.9  82.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA H5008  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 109   O
REMARK 620 2 ASP H 109   OD1  82.5
REMARK 620 3 HOH H2601   O    74.0 156.0
REMARK 620 4 GLN H 196   O    98.2  89.3  89.4
REMARK 620 5 VAL H  40   O    99.2  96.6  91.9 162.2
REMARK 620 6 HOH H2621   O   161.6 114.0  88.8  74.8  87.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B5003  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 299   O
REMARK 620 2 HOH B5241   O   139.6
REMARK 620 3 HOH B5242   O    88.2  87.6
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA C5004  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 290   O
REMARK 620 2 THR C 308   OG1 130.2
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 5001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 5002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 5003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 5004
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 5005
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 5006
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 5007
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 5008
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CW3   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NAD+ AND MN2+
REMARK 900 RELATED ID: 1AG8   RELATED DB: PDB
REMARK 900 ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA (APO)
REMARK 900 RELATED ID: 1A4Z   RELATED DB: PDB
REMARK 900 ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEXED
REMARK 900 WITH NAD AND SM3+
REMARK 900 RELATED ID: 1NZW   RELATED DB: PDB
REMARK 900 CYS302SER MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE
REMARK 900 DEHYDROGENASE COMPLEXED WITH NADH AND MG2+
REMARK 900 RELATED ID: 1NZX   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NAD+ IN THE PRESENCE OF LOW MG2+
REMARK 900 RELATED ID: 1NZZ   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NADH IN THE PRESENCE OF LOW MG2+
REMARK 900 RELATED ID: 1O00   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NAD+ AND MG2+ SHOWING DUAL NAD CONFORMATIONS
REMARK 900 RELATED ID: 1O01   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 CROTONALDEHYDE, NAD(H) AND MG2+
REMARK 900 RELATED ID: 1O02   RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH
REMARK 900 NADH IN THE PRESENCE OF MG2+
REMARK 900 RELATED ID: 1O04   RELATED DB: PDB
REMARK 900 CYS302SER MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE
REMARK 900 DEHYDROGENASE COMPLEXED WITH NAD+ AND MG2+
DBREF  1O05 A    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O05 B    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O05 C    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O05 D    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O05 E    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O05 F    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O05 G    1   500  UNP    P05091   ALDH2_HUMAN     18    517
DBREF  1O05 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES  25 H  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES  26 H  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES  27 H  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES  28 H  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES  29 H  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES  30 H  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES  31 H  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES  32 H  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES  33 H  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES  34 H  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES  35 H  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES  36 H  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES  37 H  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES  38 H  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES  39 H  500  VAL PRO GLN LYS ASN SER
HET     NA  A5001       1
HET     NA  B5002       1
HET     NA  B5003       1
HET     NA  C5004       1
HET     NA  E5005       1
HET     NA  F5006       1
HET     NA  G5007       1
HET     NA  H5008       1
HETNAM      NA SODIUM ION
FORMUL   9   NA    8(NA 1+)
FORMUL  17  HOH   *3210(H2 O)
HELIX    1   1 ASP A   55  GLN A   71  1                                  17
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  SER A  328  1                                  15
HELIX   14  14 ASP A  346  GLU A  363  1                                  18
HELIX   15  15 MET A  393  LYS A  397  5                                   5
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  HIS B  235  1                                   9
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  LYS B  397  5                                   5
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 GLU B  479  ALA B  484  5                                   6
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  GLY C  134  1                                  15
HELIX   45  45 PHE C  170  THR C  185  1                                  16
HELIX   46  46 PRO C  198  ALA C  211  1                                  14
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  GLY C  364  1                                  19
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  GLY D  134  1                                  15
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  HIS D  235  1                                   9
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 GLU D  312  ARG D  329  1                                  18
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 GLU D  479  ALA D  484  5                                   6
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  HIS E  235  1                                   9
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  LYS E  397  5                                   5
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  GLY F  134  1                                  15
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  HIS F  235  1                                   9
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  GLY F  364  1                                  19
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  HIS G  235  1                                   9
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  LYS G  397  5                                   5
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  SER H  328  1                                  17
HELIX  147 147 ASP H  346  GLU H  363  1                                  18
HELIX  148 148 MET H  393  GLU H  398  1                                   6
HELIX  149 149 THR H  412  ASN H  422  1                                  11
HELIX  150 150 ASP H  435  LEU H  446  1                                  12
HELIX  151 151 TYR H  468  MET H  470  5                                   3
HELIX  152 152 GLY H  478  ALA H  484  5                                   7
SHEET    1   A 2 ILE A  22  ILE A  24  0
SHEET    2   A 2 GLU A  27  HIS A  29 -1  O  HIS A  29   N  ILE A  22
SHEET    1   B 2 THR A  36  VAL A  40  0
SHEET    2   B 2 VAL A  47  ALA A  52 -1  O  ILE A  48   N  THR A  39
SHEET    1   C20 LYS B 366  CYS B 369  0
SHEET    2   C20 THR B 384  GLY B 387 -1  O  GLY B 387   N  LYS B 366
SHEET    3   C20 VAL B 404  PHE B 410  1  O  MET B 405   N  PHE B 386
SHEET    4   C20 ARG B 307  GLN B 311  1  N  VAL B 310   O  LEU B 408
SHEET    5   C20 PRO B 274  ILE B 277  1  N  ILE B 277   O  PHE B 309
SHEET    6   C20 ALA B 428  PHE B 432  1  O  ALA B 430   N  ILE B 276
SHEET    7   C20 THR B 450  VAL B 453  1  O  TRP B 452   N  ALA B 429
SHEET    8   C20 THR A 486  LYS A 494  1  N  THR A 490   O  VAL B 451
SHEET    9   C20 PHE A 150  PRO A 158 -1  N  GLU A 157   O  GLU A 487
SHEET   10   C20 GLY A 141  ILE A 144 -1  N  ILE A 144   O  SER A 152
SHEET   11   C20 GLY D 141  ILE D 144 -1  O  GLY D 141   N  THR A 143
SHEET   12   C20 PHE D 150  PRO D 158 -1  O  SER D 152   N  ILE D 144
SHEET   13   C20 THR D 486  LYS D 494 -1  O  GLU D 487   N  GLU D 157
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  GLN C 406   N  THR C 308
SHEET   19   C20 THR C 384  GLY C 387  1  N  PHE C 386   O  MET C 405
SHEET   20   C20 LYS C 366  CYS C 369 -1  N  LYS C 366   O  GLY C 387
SHEET    1   D 6 VAL A 218  ILE A 220  0
SHEET    2   D 6 VAL A 188  LYS A 192  1  N  MET A 191   O  ASN A 219
SHEET    3   D 6 VAL A 161  ILE A 165  1  N  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  GLY A 387   N  LYS A 366
SHEET    3   E20 VAL A 404  PHE A 410  1  O  MET A 405   N  THR A 384
SHEET    4   E20 ARG A 307  GLN A 311  1  N  THR A 308   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  VAL A 431
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  GLU B 157   O  GLU B 487
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  THR D 308
SHEET   19   E20 THR D 384  GLY D 387  1  N  THR D 384   O  MET D 405
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LYS D 366   O  GLY D 387
SHEET    1   F 2 ILE B  22  ILE B  24  0
SHEET    2   F 2 GLU B  27  HIS B  29 -1  O  HIS B  29   N  ILE B  22
SHEET    1   G 2 THR B  36  VAL B  40  0
SHEET    2   G 2 VAL B  47  ALA B  52 -1  O  ILE B  48   N  THR B  39
SHEET    1   H 6 VAL B 218  ILE B 220  0
SHEET    2   H 6 VAL B 188  LYS B 192  1  N  MET B 191   O  ASN B 219
SHEET    3   H 6 VAL B 161  ILE B 165  1  N  GLN B 164   O  LYS B 192
SHEET    4   H 6 LYS B 240  THR B 244  1  O  LYS B 240   N  GLY B 163
SHEET    5   H 6 ARG B 264  GLU B 268  1  O  ARG B 264   N  VAL B 241
SHEET    6   H 6 GLY B 472  SER B 473 -1  O  SER B 473   N  LEU B 267
SHEET    1   I 2 ILE C  22  ILE C  24  0
SHEET    2   I 2 GLU C  27  HIS C  29 -1  O  HIS C  29   N  ILE C  22
SHEET    1   J 2 THR C  36  VAL C  40  0
SHEET    2   J 2 VAL C  47  ALA C  52 -1  O  VAL C  51   N  PHE C  37
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  GLN C 164   O  LYS C 192
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  GLN D 164   O  LYS D 192
SHEET    4   N 6 LYS D 240  THR D 244  1  O  LYS D 240   N  GLY D 163
SHEET    5   N 6 ARG D 264  GLU D 268  1  O  ARG D 264   N  VAL D 241
SHEET    6   N 6 GLY D 472  SER D 473 -1  O  SER D 473   N  LEU D 267
SHEET    1   O 2 ILE E  22  ILE E  24  0
SHEET    2   O 2 GLU E  27  HIS E  29 -1  O  HIS E  29   N  ILE E  22
SHEET    1   P 2 THR E  36  VAL E  40  0
SHEET    2   P 2 VAL E  47  ALA E  52 -1  O  ILE E  48   N  THR E  39
SHEET    1   Q20 LYS F 366  CYS F 369  0
SHEET    2   Q20 THR F 384  GLY F 387 -1  O  GLY F 387   N  LYS F 366
SHEET    3   Q20 VAL F 404  PHE F 410  1  O  MET F 405   N  PHE F 386
SHEET    4   Q20 ARG F 307  GLN F 311  1  N  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  VAL G 431   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  THR G 384   O  MET G 405
SHEET   20   Q20 LYS G 366  CYS G 369 -1  N  LYS G 366   O  GLY G 387
SHEET    1   R 6 VAL E 218  ILE E 220  0
SHEET    2   R 6 VAL E 188  LYS E 192  1  N  MET E 191   O  ASN E 219
SHEET    3   R 6 VAL E 161  ILE E 165  1  N  GLN E 164   O  LYS E 192
SHEET    4   R 6 LYS E 240  THR E 244  1  O  LYS E 240   N  GLY E 163
SHEET    5   R 6 ARG E 264  GLU E 268  1  O  ARG E 264   N  VAL E 241
SHEET    6   R 6 GLY E 472  SER E 473 -1  O  SER E 473   N  LEU E 267
SHEET    1   S20 LYS E 366  CYS E 369  0
SHEET    2   S20 THR E 384  GLY E 387 -1  O  GLY E 387   N  LYS E 366
SHEET    3   S20 VAL E 404  PHE E 410  1  O  MET E 405   N  THR E 384
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  VAL E 431
SHEET    8   S20 THR F 486  LYS F 494  1  O  THR F 490   N  VAL E 451
SHEET    9   S20 PHE F 150  PRO F 158 -1  N  PHE F 151   O  VAL F 493
SHEET   10   S20 GLY F 141  ILE F 144 -1  N  ILE F 144   O  SER F 152
SHEET   11   S20 GLY G 141  ILE G 144 -1  O  THR G 143   N  GLY F 141
SHEET   12   S20 PHE G 150  PRO G 158 -1  O  SER G 152   N  ILE G 144
SHEET   13   S20 THR G 486  LYS G 494 -1  O  VAL G 493   N  PHE G 151
SHEET   14   S20 THR H 450  VAL H 453  1  O  VAL H 451   N  THR G 490
SHEET   15   S20 ALA H 428  PHE H 432  1  N  ALA H 429   O  TRP H 452
SHEET   16   S20 PRO H 274  ILE H 277  1  N  ILE H 276   O  ALA H 430
SHEET   17   S20 ARG H 307  GLN H 311  1  O  PHE H 309   N  ILE H 277
SHEET   18   S20 VAL H 404  PHE H 410  1  O  LEU H 408   N  THR H 308
SHEET   19   S20 THR H 384  GLY H 387  1  N  PHE H 386   O  MET H 405
SHEET   20   S20 LYS H 366  CYS H 369 -1  N  LYS H 366   O  GLY H 387
SHEET    1   T 2 ILE F  22  ILE F  24  0
SHEET    2   T 2 GLU F  27  HIS F  29 -1  O  HIS F  29   N  ILE F  22
SHEET    1   U 2 THR F  36  VAL F  40  0
SHEET    2   U 2 VAL F  47  ALA F  52 -1  O  VAL F  51   N  PHE F  37
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  VAL G  51   N  PHE G  37
SHEET    1   Y 6 VAL G 218  ILE G 220  0
SHEET    2   Y 6 VAL G 188  LYS G 192  1  N  MET G 191   O  ASN G 219
SHEET    3   Y 6 VAL G 161  ILE G 165  1  N  GLN G 164   O  LYS G 192
SHEET    4   Y 6 LYS G 240  THR G 244  1  O  LYS G 240   N  GLY G 163
SHEET    5   Y 6 ARG G 264  GLU G 268  1  O  ARG G 264   N  VAL G 241
SHEET    6   Y 6 GLY G 472  SER G 473 -1  O  SER G 473   N  LEU G 267
SHEET    1   Z 2 ILE H  22  ILE H  24  0
SHEET    2   Z 2 GLU H  27  HIS H  29 -1  O  HIS H  29   N  ILE H  22
SHEET    1  AA 2 THR H  36  VAL H  40  0
SHEET    2  AA 2 VAL H  47  ALA H  52 -1  O  ILE H  48   N  THR H  39
SHEET    1  AB 6 VAL H 218  ILE H 220  0
SHEET    2  AB 6 VAL H 188  LYS H 192  1  N  MET H 191   O  ASN H 219
SHEET    3  AB 6 VAL H 161  ILE H 165  1  N  GLN H 164   O  LYS H 192
SHEET    4  AB 6 LYS H 240  THR H 244  1  O  LYS H 240   N  GLY H 163
SHEET    5  AB 6 ARG H 264  GLU H 268  1  O  ARG H 264   N  VAL H 241
SHEET    6  AB 6 GLY H 472  SER H 473 -1  O  SER H 473   N  LEU H 267
LINK        NA    NA A5001                 O   GLN A 196     1555   1555  2.26
LINK        NA    NA A5001                 O   HOH A5307     1555   1555  2.54
LINK        NA    NA A5001                 O   VAL A  40     1555   1555  2.38
LINK        NA    NA B5002                 O   VAL B  40     1555   1555  2.35
LINK        NA    NA B5002                 O   ASP B 109     1555   1555  2.42
LINK        NA    NA B5002                 OD1 ASP B 109     1555   1555  2.45
LINK        NA    NA B5002                 O   GLN B 196     1555   1555  2.44
LINK        NA    NA B5002                 O   HOH B5298     1555   1555  2.51
LINK        NA    NA E5005                 O   VAL E  40     1555   1555  2.33
LINK        NA    NA E5005                 O   ASP E 109     1555   1555  2.39
LINK        NA    NA E5005                 O   GLN E 196     1555   1555  2.40
LINK        NA    NA E5005                 O   HOH E2942     1555   1555  2.49
LINK        NA    NA E5005                 OD1 ASP E 109     1555   1555  2.44
LINK        NA    NA F5006                 O   HOH F2891     1555   1555  2.54
LINK        NA    NA G5007                 O   GLN G 196     1555   1555  2.39
LINK        NA    NA G5007                 O   VAL G  40     1555   1555  2.33
LINK        NA    NA G5007                 O   ASP G 109     1555   1555  2.52
LINK        NA    NA G5007                 OD1 ASP G 109     1555   1555  2.40
LINK        NA    NA H5008                 O   ASP H 109     1555   1555  2.50
LINK        NA    NA H5008                 OD1 ASP H 109     1555   1555  2.47
LINK        NA    NA H5008                 O   HOH H2601     1555   1555  2.55
LINK        NA    NA H5008                 O   GLN H 196     1555   1555  2.33
LINK        NA    NA H5008                 O   VAL H  40     1555   1555  2.44
LINK         O   ASP A 109                NA    NA A5001     1555   1555  2.74
LINK         OD1 ASP A 109                NA    NA A5001     1555   1555  2.62
LINK         O   GLY B 299                NA    NA B5003     1555   1555  2.78
LINK         O   ALA C 290                NA    NA C5004     1555   1555  2.67
LINK         OG1 THR C 308                NA    NA C5004     1555   1555  2.81
LINK         OE1 GLU F  96                NA    NA F5006     1555   1555  2.89
LINK         NH2 ARG F  99                NA    NA F5006     1555   1555  2.88
LINK        NA    NA B5002                 O   HOH B5291     1555   1555  2.98
LINK        NA    NA B5003                 O   HOH B5241     1555   1555  2.68
LINK        NA    NA B5003                 O   HOH B5242     1555   1555  2.63
LINK        NA    NA E5005                 O   HOH E2575     1555   1555  2.91
LINK        NA    NA F5006                 O   HOH F1374     1555   1555  2.77
LINK        NA    NA H5008                 O   HOH H2621     1555   1555  2.69
SITE     1 AC1  6 THR A  39  VAL A  40  ASP A 109  GLN A 196
SITE     2 AC1  6 HOH A5279  HOH A5307
SITE     1 AC2  6 THR B  39  VAL B  40  ASP B 109  GLN B 196
SITE     2 AC2  6 HOH B5291  HOH B5298
SITE     1 AC3  5 GLY B 299  ALA B 304  GLY B 402  HOH B5241
SITE     2 AC3  5 HOH B5242
SITE     1 AC4  5 ASN C 275  ALA C 290  GLY C 305  THR C 308
SITE     2 AC4  5 MET C 405
SITE     1 AC5  6 THR E  39  VAL E  40  ASP E 109  GLN E 196
SITE     2 AC5  6 HOH E2575  HOH E2942
SITE     1 AC6  4 GLU F  96  ARG F  99  HOH F1374  HOH F2891
SITE     1 AC7  4 THR G  39  VAL G  40  ASP G 109  GLN G 196
SITE     1 AC8  6 THR H  39  VAL H  40  ASP H 109  GLN H 196
SITE     2 AC8  6 HOH H2601  HOH H2621
CRYST1  141.180  151.940  177.120  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      0.007083  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006582  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005646        0.00000
      
PROCHECK
Go to PROCHECK summary
 References