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PDBsum entry 3p9s

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3p9s
Jmol
Contents
Protein chains
726 a.a.
Ligands
HDD-HDE ×2
HDD ×2
HDE ×2
Waters ×3183
HEADER    OXIDOREDUCTASE                          18-OCT-10   3P9S
TITLE     STRUCTURE OF I274A VARIANT OF E. COLI KATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATALASE HPII;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: HYDROXYPEROXIDASE II;
COMPND   5 EC: 1.11.1.6;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 83333;
SOURCE   4 GENE: B1732, JW1721, KATE;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: UM255;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKS
KEYWDS    CATALASE, I274A VARIANT, HEME ORIENTATION, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.C.LOEWEN,V.JHA,S.LOUIS,P.CHELIKANI,X.CARPENA,I.FITA
REVDAT   2   27-JUL-11 3P9S    1       JRNL
REVDAT   1   22-DEC-10 3P9S    0
JRNL        AUTH   V.JHA,S.LOUIS,P.CHELIKANI,X.CARPENA,L.J.DONALD,I.FITA,
JRNL        AUTH 2 P.C.LOEWEN
JRNL        TITL   MODULATION OF HEME ORIENTATION AND BINDING BY A SINGLE
JRNL        TITL 2 RESIDUE IN CATALASE HPII OF ESCHERICHIA COLI.
JRNL        REF    BIOCHEMISTRY                  V.  50  2101 2011
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   21332158
JRNL        DOI    10.1021/BI200027V
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.29
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.6
REMARK   3   NUMBER OF REFLECTIONS             : 197565
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) : 0.140
REMARK   3   R VALUE            (WORKING SET) : 0.137
REMARK   3   FREE R VALUE                     : 0.191
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 9959
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) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11286
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.11
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160
REMARK   3   BIN FREE R VALUE SET COUNT          : 574
REMARK   3   BIN FREE R VALUE                    : 0.2770
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 22952
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 352
REMARK   3   SOLVENT ATOMS            : 3183
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.82
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.04000
REMARK   3    B22 (A**2) : -0.13000
REMARK   3    B33 (A**2) : 0.26000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.13000
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): 0.145
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.387
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 24041 ; 0.024 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 32848 ; 2.000 ; 1.990
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2904 ; 6.653 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1178 ;36.589 ;23.837
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3767 ;14.788 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   177 ;15.092 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3431 ; 0.183 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 18945 ; 0.011 ; 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): 14548 ; 0.995 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23525 ; 1.583 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9493 ; 2.641 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9323 ; 3.915 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     28       A     753      4
REMARK   3           1     B     28       B     753      4
REMARK   3           1     C     28       C     753      4
REMARK   3           1     D     28       D     753      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   5727 ; 0.370 ; 0.500
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   5727 ; 0.310 ; 0.500
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   5727 ; 0.320 ; 0.500
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   5727 ; 0.350 ; 0.500
REMARK   3   MEDIUM THERMAL     1    A (A**2):   5727 ; 1.520 ; 2.000
REMARK   3   MEDIUM THERMAL     1    B (A**2):   5727 ; 1.310 ; 2.000
REMARK   3   MEDIUM THERMAL     1    C (A**2):   5727 ; 1.300 ; 2.000
REMARK   3   MEDIUM THERMAL     1    D (A**2):   5727 ; 1.220 ; 2.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   -10        A  9999
REMARK   3    ORIGIN FOR THE GROUP (A):   2.7290  -9.3936  31.4992
REMARK   3    T TENSOR
REMARK   3      T11:   0.0111 T22:   0.0105
REMARK   3      T33:   0.0307 T12:   0.0029
REMARK   3      T13:   0.0067 T23:   0.0153
REMARK   3    L TENSOR
REMARK   3      L11:   0.1509 L22:   0.1308
REMARK   3      L33:   0.1416 L12:  -0.0012
REMARK   3      L13:   0.0137 L23:  -0.0234
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0067 S12:  -0.0338 S13:  -0.0387
REMARK   3      S21:   0.0276 S22:   0.0161 S23:   0.0339
REMARK   3      S31:   0.0157 S32:  -0.0137 S33:  -0.0094
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   -10        B  9999
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7203  11.9504 -18.6024
REMARK   3    T TENSOR
REMARK   3      T11:   0.0422 T22:   0.0132
REMARK   3      T33:   0.0252 T12:  -0.0039
REMARK   3      T13:  -0.0176 T23:   0.0130
REMARK   3    L TENSOR
REMARK   3      L11:   0.1481 L22:   0.1744
REMARK   3      L33:   0.1282 L12:  -0.0402
REMARK   3      L13:  -0.0113 L23:  -0.0269
REMARK   3    S TENSOR
REMARK   3      S11:   0.0052 S12:   0.0421 S13:   0.0298
REMARK   3      S21:  -0.0789 S22:  -0.0003 S23:   0.0264
REMARK   3      S31:  -0.0108 S32:  -0.0062 S33:  -0.0049
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   -10        C  9999
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5030 -11.9752 -19.5973
REMARK   3    T TENSOR
REMARK   3      T11:   0.0542 T22:   0.0178
REMARK   3      T33:   0.0168 T12:   0.0004
REMARK   3      T13:   0.0152 T23:  -0.0124
REMARK   3    L TENSOR
REMARK   3      L11:   0.1724 L22:   0.1656
REMARK   3      L33:   0.1224 L12:   0.0031
REMARK   3      L13:  -0.0173 L23:  -0.0319
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0114 S12:   0.0414 S13:  -0.0314
REMARK   3      S21:  -0.0886 S22:   0.0029 S23:  -0.0206
REMARK   3      S31:   0.0437 S32:   0.0195 S33:   0.0085
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   -10        D  9999
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0676   9.3232  31.5592
REMARK   3    T TENSOR
REMARK   3      T11:   0.0167 T22:   0.0223
REMARK   3      T33:   0.0167 T12:  -0.0083
REMARK   3      T13:  -0.0064 T23:  -0.0101
REMARK   3    L TENSOR
REMARK   3      L11:   0.1684 L22:   0.1403
REMARK   3      L33:   0.1081 L12:   0.0418
REMARK   3      L13:  -0.0228 L23:   0.0019
REMARK   3    S TENSOR
REMARK   3      S11:   0.0108 S12:  -0.0424 S13:   0.0300
REMARK   3      S21:   0.0402 S22:  -0.0039 S23:  -0.0199
REMARK   3      S31:  -0.0224 S32:   0.0403 S33:  -0.0068
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED
REMARK   4
REMARK   4 3P9S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062135.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-AUG-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CLSI
REMARK 200  BEAMLINE                       : 08ID-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTALS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 197718
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.288
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.9
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.09700
REMARK 200   FOR THE DATA SET  : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.28400
REMARK 200  R SYM FOR SHELL            (I) : 0.28400
REMARK 200   FOR SHELL         : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 1.6 M LICL, 0.1 M TRIS,
REMARK 280  PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       66.58500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 57180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -272.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, 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 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     MET A     1
REMARK 465     SER A     2
REMARK 465     GLN A     3
REMARK 465     HIS A     4
REMARK 465     ASN A     5
REMARK 465     GLU A     6
REMARK 465     LYS A     7
REMARK 465     ASN A     8
REMARK 465     PRO A     9
REMARK 465     HIS A    10
REMARK 465     GLN A    11
REMARK 465     HIS A    12
REMARK 465     GLN A    13
REMARK 465     SER A    14
REMARK 465     PRO A    15
REMARK 465     LEU A    16
REMARK 465     HIS A    17
REMARK 465     ASP A    18
REMARK 465     SER A    19
REMARK 465     SER A    20
REMARK 465     GLU A    21
REMARK 465     ALA A    22
REMARK 465     LYS A    23
REMARK 465     PRO A    24
REMARK 465     GLY A    25
REMARK 465     MET A    26
REMARK 465     ASP A    27
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     GLN B     3
REMARK 465     HIS B     4
REMARK 465     ASN B     5
REMARK 465     GLU B     6
REMARK 465     LYS B     7
REMARK 465     ASN B     8
REMARK 465     PRO B     9
REMARK 465     HIS B    10
REMARK 465     GLN B    11
REMARK 465     HIS B    12
REMARK 465     GLN B    13
REMARK 465     SER B    14
REMARK 465     PRO B    15
REMARK 465     LEU B    16
REMARK 465     HIS B    17
REMARK 465     ASP B    18
REMARK 465     SER B    19
REMARK 465     SER B    20
REMARK 465     GLU B    21
REMARK 465     ALA B    22
REMARK 465     LYS B    23
REMARK 465     PRO B    24
REMARK 465     GLY B    25
REMARK 465     MET B    26
REMARK 465     ASP B    27
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     GLN C     3
REMARK 465     HIS C     4
REMARK 465     ASN C     5
REMARK 465     GLU C     6
REMARK 465     LYS C     7
REMARK 465     ASN C     8
REMARK 465     PRO C     9
REMARK 465     HIS C    10
REMARK 465     GLN C    11
REMARK 465     HIS C    12
REMARK 465     GLN C    13
REMARK 465     SER C    14
REMARK 465     PRO C    15
REMARK 465     LEU C    16
REMARK 465     HIS C    17
REMARK 465     ASP C    18
REMARK 465     SER C    19
REMARK 465     SER C    20
REMARK 465     GLU C    21
REMARK 465     ALA C    22
REMARK 465     LYS C    23
REMARK 465     PRO C    24
REMARK 465     GLY C    25
REMARK 465     MET C    26
REMARK 465     ASP C    27
REMARK 465     MET D     1
REMARK 465     SER D     2
REMARK 465     GLN D     3
REMARK 465     HIS D     4
REMARK 465     ASN D     5
REMARK 465     GLU D     6
REMARK 465     LYS D     7
REMARK 465     ASN D     8
REMARK 465     PRO D     9
REMARK 465     HIS D    10
REMARK 465     GLN D    11
REMARK 465     HIS D    12
REMARK 465     GLN D    13
REMARK 465     SER D    14
REMARK 465     PRO D    15
REMARK 465     LEU D    16
REMARK 465     HIS D    17
REMARK 465     ASP D    18
REMARK 465     SER D    19
REMARK 465     SER D    20
REMARK 465     GLU D    21
REMARK 465     ALA D    22
REMARK 465     LYS D    23
REMARK 465     PRO D    24
REMARK 465     GLY D    25
REMARK 465     MET D    26
REMARK 465     ASP D    27
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OH   TYR B   415    FE    HDD B   760              1.70
REMARK 500   CG   GLN D   546     O    HOH D  2742              1.83
REMARK 500   O    HOH B   755     O    HOH B  1097              1.87
REMARK 500   O    HOH B  2197     O    HOH C  3168              1.92
REMARK 500   O    HOH A  2238     O    HOH A  2416              1.92
REMARK 500   O    HOH C  1026     O    HOH C  2665              1.94
REMARK 500   O    HOH D  1264     O    HOH D  3200              1.98
REMARK 500   NE   ARG D   488     O    HOH D  2698              1.99
REMARK 500   O    HOH B  2909     O    HOH B  2958              1.99
REMARK 500   NH2  ARG A   479     O    HOH A  2607              2.03
REMARK 500   O    HOH C  1263     O    HOH C  2594              2.06
REMARK 500   O    HOH A  2519     O    HOH A  2595              2.08
REMARK 500   O    HOH A  1242     O    HOH A  2274              2.08
REMARK 500   O    HOH B  2490     O    HOH B  3317              2.09
REMARK 500   O    HOH A  2713     O    HOH D  2270              2.10
REMARK 500   O    HOH A  3089     O    HOH D  2735              2.10
REMARK 500   OD2  ASP B   578     O    HOH B  3117              2.12
REMARK 500   O    HOH B   858     O    HOH C  1874              2.13
REMARK 500   O    HOH B   840     O    HOH B  2694              2.15
REMARK 500   O    HOH C  2207     O    HOH C  2380              2.16
REMARK 500   O    HOH D  1236     O    HOH D  2727              2.16
REMARK 500   O    HOH D  1384     O    HOH D  2497              2.16
REMARK 500   O    HOH D  1610     O    HOH D  1696              2.17
REMARK 500   O    HOH A   822     O    HOH A  3091              2.17
REMARK 500   O    HOH A  1712     O    HOH A  3179              2.18
REMARK 500   O    HOH A  2722     O    HOH A  2837              2.18
REMARK 500   O    HOH C  2041     O    HOH C  2576              2.18
REMARK 500   O    GLY C   726     O    HOH C  2714              2.19
REMARK 500   O    ILE B   564     O    HOH B  2603              2.19
REMARK 500   OD1  ASP B   597     O    HOH B  3327              2.19
REMARK 500   O    HOH D  1832     O    HOH D  2497              2.19
REMARK 500   O    HOH B  2271     O    HOH B  3063              2.19
REMARK 500   O    HOH B   755     O    HOH B  1098              2.19
REMARK 500
REMARK 500 REMARK: NULL
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 D  2178     O    HOH D  2976     1655     2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU B  69   CB    GLU B  69   CG      0.116
REMARK 500    VAL B 494   CB    VAL B 494   CG2     0.160
REMARK 500    GLU D 321   CD    GLU D 321   OE1     0.068
REMARK 500    TYR D 460   CD1   TYR D 460   CE1     0.115
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    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ARG A 509   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 740   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG B 536   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    LEU B 552   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES
REMARK 500    ARG C  37   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG D 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    LEU D 340   CB  -  CG  -  CD1 ANGL. DEV. =  13.7 DEGREES
REMARK 500    ASP D 615   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP D 680   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 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    SER A  75      -38.17   -165.34
REMARK 500    THR A 178       34.95    -94.17
REMARK 500    ALA A 274      -56.24     70.26
REMARK 500    ASP A 314       84.89   -155.46
REMARK 500    ASP A 405      118.40    -39.87
REMARK 500    ASP A 446     -142.45     68.87
REMARK 500    ASP A 595       21.30   -149.48
REMARK 500    GLU A 610       59.73   -144.62
REMARK 500    ASP A 725     -159.75   -110.30
REMARK 500    HIS A 739      -63.45     78.72
REMARK 500    SER B  35        0.21    -69.40
REMARK 500    SER B  75      -36.26   -166.93
REMARK 500    VAL B 169      -50.43   -126.12
REMARK 500    THR B 178       36.70    -86.33
REMARK 500    ALA B 274      -54.01     66.93
REMARK 500    ASP B 314       87.13   -154.77
REMARK 500    ASP B 446     -149.21     65.46
REMARK 500    ASN B 580       44.65     39.94
REMARK 500    LYS B 584      170.88    177.95
REMARK 500    ASP B 595       29.75   -141.12
REMARK 500    ARG B 612       99.49    -68.19
REMARK 500    LYS B 705      -38.25    -37.10
REMARK 500    ALA B 724       42.86    -86.00
REMARK 500    ASP B 725     -159.63    -47.78
REMARK 500    HIS B 739      -65.44     77.47
REMARK 500    SER C  75      -32.95   -163.68
REMARK 500    THR C 178       40.31    -91.45
REMARK 500    ALA C 274      -58.05     63.84
REMARK 500    ASP C 314       85.26   -152.22
REMARK 500    ASN C 386      -60.10    -90.43
REMARK 500    ASP C 446     -151.81     65.60
REMARK 500    GLU C 472      152.49    -48.48
REMARK 500    ASN C 580       52.24     39.74
REMARK 500    LYS C 584      167.68    177.69
REMARK 500    ASP C 595       36.36   -143.18
REMARK 500    ASP C 725     -158.47    -94.64
REMARK 500    HIS C 739      -62.92     78.77
REMARK 500    SER D  75      -38.15   -167.51
REMARK 500    THR D 178       35.10    -93.53
REMARK 500    ALA D 274      -62.06     71.22
REMARK 500    ASP D 314       86.26   -151.60
REMARK 500    ASP D 405      114.17    -33.58
REMARK 500    ASN D 442     -167.95   -162.45
REMARK 500    ASP D 446     -147.25     66.49
REMARK 500    HIS D 449       33.24     71.63
REMARK 500    LYS D 584      163.91    178.06
REMARK 500    ASP D 595       38.21   -142.83
REMARK 500    HIS D 739      -67.54     79.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ALA C  724     ASP C  725                 -128.49
REMARK 500 ASP C  725     GLY C  726                  137.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    TRP A 227        24.2      L          L   OUTSIDE RANGE
REMARK 500    LYS A 348        24.3      L          L   OUTSIDE RANGE
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 A1087        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH A2186        DISTANCE =  6.17 ANGSTROMS
REMARK 525    HOH A2213        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A2238        DISTANCE =  5.52 ANGSTROMS
REMARK 525    HOH A2352        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH A2805        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH A2824        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH A2967        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH A2979        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH B 774        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH B 782        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH B2749        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH B2829        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH B3006        DISTANCE =  5.80 ANGSTROMS
REMARK 525    HOH B3312        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH C1262        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH C1533        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH C2237        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH C2871        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH C3052        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH D1620        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH D2208        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH D2412        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH D2468        DISTANCE =  6.45 ANGSTROMS
REMARK 525    HOH D2476        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH D2524        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH D2547        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH D3051        DISTANCE =  6.64 ANGSTROMS
REMARK 525    HOH D3083        DISTANCE =  5.65 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                             HDD A 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 415   OH
REMARK 620 2 HDD A 760   NA   94.5
REMARK 620 3 HDD A 760   NB   90.5  88.7
REMARK 620 4 HDD A 760   NC   89.2 176.1  92.1
REMARK 620 5 HDD A 760   ND   94.4  90.1 175.1  88.8
REMARK 620 6 HOH A2520   O   169.1  81.3  79.4  95.1  95.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDD D 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 415   OH
REMARK 620 2 HDD D 760   NA   91.6
REMARK 620 3 HDD D 760   NB   85.1  86.8
REMARK 620 4 HDD D 760   NC   92.6 175.7  94.2
REMARK 620 5 HDD D 760   ND   98.8  92.1 176.0  86.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDD C 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 415   OH
REMARK 620 2 HDD C 760   NA   95.1
REMARK 620 3 HDD C 760   NB   84.7  90.4
REMARK 620 4 HDD C 760   NC   88.5 176.4  89.8
REMARK 620 5 HDD C 760   ND   99.6  88.5 175.7  91.1
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDE B 761  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 415   OH
REMARK 620 2 HDE B 761   NA   96.1
REMARK 620 3 HDE B 761   NB   92.8  87.5
REMARK 620 4 HDE B 761   NC   86.3 177.6  92.8
REMARK 620 5 HDE B 761   ND   88.6  91.6 178.5  88.0
REMARK 620 6 HOH B2694   O   165.6  98.3  88.4  79.3  90.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDE A 761  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 415   OH
REMARK 620 2 HDE A 761   NA   96.4
REMARK 620 3 HDE A 761   NB   93.0  88.3
REMARK 620 4 HDE A 761   NC   86.1 177.3  92.4
REMARK 620 5 HDE A 761   ND   88.8  91.0 178.1  88.1
REMARK 620 6 HOH A2520   O   156.5 106.8  90.6  70.6  87.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDE D 761  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 415   OH
REMARK 620 2 HDE D 761   NA   94.4
REMARK 620 3 HDE D 761   NB   93.1  88.9
REMARK 620 4 HDE D 761   NC   87.6 177.8  92.0
REMARK 620 5 HDE D 761   ND   88.6  90.2 178.1  88.8
REMARK 620 6 HOH D3200   O   157.8 106.5  94.4  71.3  84.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDE C 761  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 415   OH
REMARK 620 2 HDE C 761   NA   95.1
REMARK 620 3 HDE C 761   NB   93.3  88.3
REMARK 620 4 HDE C 761   NC   87.2 177.7  91.9
REMARK 620 5 HDE C 761   ND   88.1  91.1 178.5  88.6
REMARK 620 6 HOH C2594   O   160.6 104.3  87.4  73.4  91.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDD B 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2694   O
REMARK 620 2 HDD B 760   NA   89.8
REMARK 620 3 HDD B 760   NB   81.2  91.9
REMARK 620 4 HDD B 760   NC   87.2 176.7  89.0
REMARK 620 5 HDD B 760   ND   94.8  87.7 176.0  91.1
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD A 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE A 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD B 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE B 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD C 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE C 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD D 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE D 761
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P9P   RELATED DB: PDB
REMARK 900 RELATED ID: 3P9Q   RELATED DB: PDB
REMARK 900 RELATED ID: 3P9R   RELATED DB: PDB
DBREF  3P9S A    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  3P9S B    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  3P9S C    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  3P9S D    1   753  UNP    P21179   CATE_ECOLI       1    753
SEQADV 3P9S ALA A  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQADV 3P9S ALA B  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQADV 3P9S ALA C  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQADV 3P9S ALA D  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQRES   1 A  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 A  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 A  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 A  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 A  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 A  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 A  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 A  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 A  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 A  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 A  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 A  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 A  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 A  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 A  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 A  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 A  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 A  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 A  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 A  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 A  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 A  753  ALA HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 A  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 A  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 A  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 A  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 A  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 A  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 A  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 A  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 A  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 A  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 A  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 A  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 A  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 A  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 A  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 A  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 A  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 A  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 A  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 A  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 A  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 A  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 A  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 A  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 A  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 A  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 A  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 A  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 A  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 A  753  ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 A  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 A  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 A  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 A  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 A  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 A  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES   1 B  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 B  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 B  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 B  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 B  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 B  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 B  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 B  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 B  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 B  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 B  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 B  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 B  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 B  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 B  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 B  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 B  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 B  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 B  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 B  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 B  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 B  753  ALA HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 B  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 B  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 B  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 B  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 B  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 B  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 B  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 B  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 B  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 B  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 B  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 B  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 B  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 B  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 B  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 B  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 B  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 B  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 B  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 B  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 B  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 B  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 B  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 B  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 B  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 B  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 B  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 B  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 B  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 B  753  ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 B  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 B  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 B  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 B  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 B  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 B  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES   1 C  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 C  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 C  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 C  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 C  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 C  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 C  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 C  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 C  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 C  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 C  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 C  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 C  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 C  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 C  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 C  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 C  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 C  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 C  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 C  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 C  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 C  753  ALA HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 C  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 C  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 C  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 C  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 C  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 C  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 C  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 C  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 C  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 C  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 C  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 C  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 C  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 C  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 C  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 C  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 C  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 C  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 C  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 C  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 C  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 C  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 C  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 C  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 C  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 C  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 C  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 C  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 C  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 C  753  ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 C  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 C  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 C  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 C  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 C  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 C  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES   1 D  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 D  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 D  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 D  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 D  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 D  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 D  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 D  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 D  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 D  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 D  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 D  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 D  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 D  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 D  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 D  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 D  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 D  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 D  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 D  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 D  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 D  753  ALA HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 D  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 D  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 D  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 D  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 D  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 D  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 D  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 D  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 D  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 D  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 D  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 D  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 D  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 D  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 D  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 D  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 D  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 D  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 D  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 D  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 D  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 D  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 D  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 D  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 D  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 D  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 D  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 D  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 D  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 D  753  ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 D  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 D  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 D  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 D  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 D  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 D  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
MODRES 3P9S OCS A  669  CYS  CYSTEINESULFONIC ACID
MODRES 3P9S OCS B  669  CYS  CYSTEINESULFONIC ACID
MODRES 3P9S OCS C  669  CYS  CYSTEINESULFONIC ACID
MODRES 3P9S OCS D  669  CYS  CYSTEINESULFONIC ACID
HET    OCS  A 669       9
HET    OCS  B 669       9
HET    OCS  C 669       9
HET    OCS  D 669       9
HET    HDD  A 760      44
HET    HDE  A 761      44
HET    HDD  B 760      44
HET    HDE  B 761      44
HET    HDD  C 760      44
HET    HDE  C 761      44
HET    HDD  D 760      44
HET    HDE  D 761      44
HETNAM     OCS CYSTEINESULFONIC ACID
HETNAM     HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE
HETNAM     HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S
HETSYN     HDD HEME
FORMUL   1  OCS    4(C3 H7 N O5 S)
FORMUL   5  HDD    4(C34 H32 FE N4 O5)
FORMUL   6  HDE    4(C34 H38 FE N4 O5)
FORMUL  13  HOH   *3183(H2 O)
HELIX    1   1 PRO A   52  ALA A   57  1                                   6
HELIX    2   2 ASN A   62  LEU A   68  1                                   7
HELIX    3   3 ASP A  107  HIS A  119  1                                  13
HELIX    4   4 ALA A  150  SER A  154  5                                   5
HELIX    5   5 ASP A  210  HIS A  212  5                                   3
HELIX    6   6 LYS A  213  LYS A  222  1                                  10
HELIX    7   7 HIS A  236  GLN A  246  1                                  11
HELIX    8   8 THR A  249  SER A  258  1                                  10
HELIX    9   9 ASP A  259  ILE A  262  5                                   4
HELIX   10  10 SER A  265  MET A  269  5                                   5
HELIX   11  11 VAL A  303  ASP A  314  1                                  12
HELIX   12  12 ASP A  316  GLY A  329  1                                  14
HELIX   13  13 GLU A  344  GLU A  346  5                                   3
HELIX   14  14 ASN A  381  ASN A  386  1                                   6
HELIX   15  15 ASP A  405  LEU A  423  1                                  19
HELIX   16  16 ASN A  427  ARG A  435  5                                   9
HELIX   17  17 SER A  498  GLY A  502  5                                   5
HELIX   18  18 TYR A  505  GLN A  515  1                                  11
HELIX   19  19 THR A  516  LYS A  533  1                                  18
HELIX   20  20 ARG A  536  HIS A  549  1                                  14
HELIX   21  21 ASP A  551  GLY A  563  1                                  13
HELIX   22  22 THR A  567  ASN A  572  1                                   6
HELIX   23  23 ASP A  585  SER A  589  5                                   5
HELIX   24  24 ARG A  612  LYS A  626  1                                  15
HELIX   25  25 PRO A  658  VAL A  662  5                                   5
HELIX   26  26 ILE A  672  ASP A  677  1                                   6
HELIX   27  27 ASN A  678  HIS A  691  1                                  14
HELIX   28  28 ASP A  700  THR A  707  5                                   8
HELIX   29  29 ASP A  725  ALA A  738  1                                  14
HELIX   30  30 VAL A  741  SER A  743  5                                   3
HELIX   31  31 ARG A  744  ASP A  749  1                                   6
HELIX   32  32 PRO B   52  ALA B   57  1                                   6
HELIX   33  33 ASN B   62  LEU B   68  1                                   7
HELIX   34  34 ASP B  107  HIS B  119  1                                  13
HELIX   35  35 ALA B  150  SER B  154  5                                   5
HELIX   36  36 ASP B  210  HIS B  212  5                                   3
HELIX   37  37 LYS B  213  LYS B  222  1                                  10
HELIX   38  38 HIS B  236  GLN B  246  1                                  11
HELIX   39  39 THR B  249  SER B  258  1                                  10
HELIX   40  40 ASP B  259  ILE B  262  5                                   4
HELIX   41  41 SER B  265  MET B  269  5                                   5
HELIX   42  42 VAL B  303  ASP B  314  1                                  12
HELIX   43  43 ASP B  316  GLY B  329  1                                  14
HELIX   44  44 GLU B  344  GLU B  346  5                                   3
HELIX   45  45 ASN B  381  ASN B  386  1                                   6
HELIX   46  46 ASP B  405  THR B  418  1                                  14
HELIX   47  47 THR B  418  LEU B  423  1                                   6
HELIX   48  48 ASN B  427  ARG B  435  5                                   9
HELIX   49  49 SER B  498  GLY B  502  5                                   5
HELIX   50  50 TYR B  505  GLN B  515  1                                  11
HELIX   51  51 THR B  516  LYS B  533  1                                  18
HELIX   52  52 ARG B  536  HIS B  549  1                                  14
HELIX   53  53 ASP B  551  LEU B  562  1                                  12
HELIX   54  54 THR B  567  ASN B  572  1                                   6
HELIX   55  55 ASP B  585  SER B  589  5                                   5
HELIX   56  56 ARG B  612  LYS B  626  1                                  15
HELIX   57  57 PRO B  658  VAL B  662  5                                   5
HELIX   58  58 ILE B  672  ASP B  677  1                                   6
HELIX   59  59 ASN B  678  HIS B  691  1                                  14
HELIX   60  60 ASP B  700  THR B  707  5                                   8
HELIX   61  61 ASP B  725  ALA B  738  1                                  14
HELIX   62  62 VAL B  741  SER B  743  5                                   3
HELIX   63  63 ARG B  744  ASP B  749  1                                   6
HELIX   64  64 PRO C   52  ALA C   57  1                                   6
HELIX   65  65 ASN C   62  LEU C   68  1                                   7
HELIX   66  66 ASP C  107  HIS C  119  1                                  13
HELIX   67  67 ALA C  150  SER C  154  5                                   5
HELIX   68  68 ASP C  210  HIS C  212  5                                   3
HELIX   69  69 LYS C  213  LYS C  222  1                                  10
HELIX   70  70 HIS C  236  GLN C  246  1                                  11
HELIX   71  71 THR C  249  SER C  258  1                                  10
HELIX   72  72 ASP C  259  ILE C  262  5                                   4
HELIX   73  73 SER C  265  MET C  269  5                                   5
HELIX   74  74 VAL C  303  ASP C  314  1                                  12
HELIX   75  75 ASP C  316  GLY C  329  1                                  14
HELIX   76  76 GLU C  344  GLU C  346  5                                   3
HELIX   77  77 ASN C  381  ASN C  386  1                                   6
HELIX   78  78 ASP C  405  THR C  418  1                                  14
HELIX   79  79 THR C  418  LEU C  423  1                                   6
HELIX   80  80 ASN C  427  ARG C  435  5                                   9
HELIX   81  81 SER C  498  GLY C  502  5                                   5
HELIX   82  82 TYR C  505  SER C  514  1                                  10
HELIX   83  83 THR C  516  LYS C  533  1                                  18
HELIX   84  84 ARG C  536  HIS C  549  1                                  14
HELIX   85  85 ASP C  551  GLY C  563  1                                  13
HELIX   86  86 THR C  567  ASN C  572  1                                   6
HELIX   87  87 ASP C  585  SER C  589  5                                   5
HELIX   88  88 ARG C  612  LYS C  626  1                                  15
HELIX   89  89 PRO C  658  VAL C  662  5                                   5
HELIX   90  90 ASN C  671  ILE C  675  5                                   5
HELIX   91  91 ASN C  678  HIS C  691  1                                  14
HELIX   92  92 ASP C  700  ALA C  706  5                                   7
HELIX   93  93 SER C  727  ALA C  738  1                                  12
HELIX   94  94 VAL C  741  SER C  743  5                                   3
HELIX   95  95 ARG C  744  ASP C  749  1                                   6
HELIX   96  96 PRO D   52  ALA D   57  1                                   6
HELIX   97  97 ASN D   62  LEU D   68  1                                   7
HELIX   98  98 ASP D  107  HIS D  119  1                                  13
HELIX   99  99 ALA D  150  SER D  154  5                                   5
HELIX  100 100 ASP D  210  HIS D  212  5                                   3
HELIX  101 101 LYS D  213  LYS D  222  1                                  10
HELIX  102 102 HIS D  236  GLN D  246  1                                  11
HELIX  103 103 THR D  249  SER D  258  1                                  10
HELIX  104 104 ASP D  259  ILE D  262  5                                   4
HELIX  105 105 SER D  265  MET D  269  5                                   5
HELIX  106 106 VAL D  303  ASP D  314  1                                  12
HELIX  107 107 ASP D  316  ALA D  328  1                                  13
HELIX  108 108 GLU D  344  GLU D  346  5                                   3
HELIX  109 109 ASN D  381  ASN D  386  1                                   6
HELIX  110 110 ASP D  405  THR D  418  1                                  14
HELIX  111 111 THR D  418  LEU D  423  1                                   6
HELIX  112 112 ASN D  427  ARG D  435  5                                   9
HELIX  113 113 SER D  498  GLY D  502  5                                   5
HELIX  114 114 TYR D  505  GLN D  515  1                                  11
HELIX  115 115 THR D  516  LYS D  533  1                                  18
HELIX  116 116 ARG D  536  HIS D  549  1                                  14
HELIX  117 117 ASP D  551  LEU D  562  1                                  12
HELIX  118 118 THR D  567  ASN D  572  1                                   6
HELIX  119 119 ASP D  585  SER D  589  5                                   5
HELIX  120 120 ARG D  612  LYS D  626  1                                  15
HELIX  121 121 PRO D  658  VAL D  662  5                                   5
HELIX  122 122 ILE D  672  ASP D  677  1                                   6
HELIX  123 123 ASN D  678  HIS D  691  1                                  14
HELIX  124 124 ASP D  700  LYS D  703  5                                   4
HELIX  125 125 PHE D  704  LYS D  709  1                                   6
HELIX  126 126 SER D  727  ALA D  738  1                                  12
HELIX  127 127 VAL D  741  SER D  743  5                                   3
HELIX  128 128 ARG D  744  ASP D  749  1                                   6
SHEET    1   A 2 ARG A  72  LYS A  73  0
SHEET    2   A 2 ILE C 453  ASP C 454  1  O  ILE C 453   N  LYS A  73
SHEET    1   B 4 LEU A  95  ALA A  97  0
SHEET    2   B 4 ARG D 488  ARG D 495 -1  O  VAL D 494   N  ARG A  96
SHEET    3   B 4 ARG C 488  ARG C 495 -1  N  VAL C 489   O  GLY D 491
SHEET    4   B 4 LEU B  95  ALA B  97 -1  N  ARG B  96   O  VAL C 494
SHEET    1   C11 LEU A 400  ASP A 401  0
SHEET    2   C11 PHE A 277  ILE A 280 -1  N  ARG A 278   O  ASP A 401
SHEET    3   C11 ALA A 286  PRO A 295 -1  O  VAL A 289   N  PHE A 277
SHEET    4   C11 GLU A 333  PRO A 342 -1  O  GLU A 335   N  LYS A 294
SHEET    5   C11 GLN A 368  ARG A 377 -1  O  VAL A 370   N  LEU A 336
SHEET    6   C11 GLY A 131  PRO A 140 -1  N  HIS A 135   O  ARG A 377
SHEET    7   C11 THR A 160  SER A 167 -1  O  PHE A 166   N  SER A 132
SHEET    8   C11 GLY A 184  THR A 191 -1  O  LYS A 188   N  PHE A 163
SHEET    9   C11 GLY A 194  ASN A 201 -1  O  GLY A 200   N  PHE A 185
SHEET   10   C11 GLY A 271  PHE A 272 -1  O  PHE A 272   N  ASN A 201
SHEET   11   C11 ALA A 286  PRO A 295 -1  O  TRP A 293   N  GLY A 271
SHEET    1   D 2 ILE A 453  ASP A 454  0
SHEET    2   D 2 ARG C  72  LYS C  73  1  O  LYS C  73   N  ILE A 453
SHEET    1   E 4 ARG C  96  ALA C  97  0
SHEET    2   E 4 ARG B 488  VAL B 494 -1  N  VAL B 494   O  ARG C  96
SHEET    3   E 4 ARG A 488  VAL A 494 -1  N  GLY A 491   O  VAL B 489
SHEET    4   E 4 ARG D  96  ALA D  97 -1  O  ARG D  96   N  VAL A 494
SHEET    1   F 6 ALA A 652  THR A 653  0
SHEET    2   F 6 HIS A 629  TYR A 634  1  N  TYR A 634   O  ALA A 652
SHEET    3   F 6 VAL A 602  LEU A 606  1  N  ILE A 605   O  LEU A 633
SHEET    4   F 6 ALA A 664  VAL A 667  1  O  ILE A 666   N  ALA A 604
SHEET    5   F 6 ILE A 695  ALA A 698  1  O  ALA A 696   N  VAL A 667
SHEET    6   F 6 ILE A 718  ALA A 721  1  O  VAL A 719   N  LEU A 697
SHEET    1   G 2 GLU A 639  THR A 641  0
SHEET    2   G 2 VAL A 647  PRO A 649 -1  O  LEU A 648   N  VAL A 640
SHEET    1   H 2 ARG B  72  LYS B  73  0
SHEET    2   H 2 ILE D 453  ASP D 454  1  O  ILE D 453   N  LYS B  73
SHEET    1   I11 LEU B 400  ASP B 401  0
SHEET    2   I11 PHE B 277  ILE B 280 -1  N  ARG B 278   O  ASP B 401
SHEET    3   I11 ALA B 286  PRO B 295 -1  O  THR B 287   N  LEU B 279
SHEET    4   I11 GLU B 333  PRO B 342 -1  O  GLU B 335   N  LYS B 294
SHEET    5   I11 VAL B 367  ARG B 377 -1  O  GLN B 368   N  PHE B 338
SHEET    6   I11 GLY B 131  PRO B 140 -1  N  HIS B 135   O  ARG B 377
SHEET    7   I11 THR B 160  SER B 167 -1  O  PHE B 166   N  SER B 132
SHEET    8   I11 GLY B 184  THR B 191 -1  O  LYS B 188   N  PHE B 163
SHEET    9   I11 GLY B 194  ASN B 201 -1  O  PHE B 196   N  PHE B 189
SHEET   10   I11 GLY B 271  PHE B 272 -1  O  PHE B 272   N  ASN B 201
SHEET   11   I11 ALA B 286  PRO B 295 -1  O  TRP B 293   N  GLY B 271
SHEET    1   J 2 ILE B 453  ASP B 454  0
SHEET    2   J 2 ARG D  72  LYS D  73  1  O  LYS D  73   N  ILE B 453
SHEET    1   K 6 ALA B 652  THR B 653  0
SHEET    2   K 6 HIS B 629  TYR B 634  1  N  TYR B 634   O  ALA B 652
SHEET    3   K 6 VAL B 602  LEU B 606  1  N  ILE B 605   O  LEU B 633
SHEET    4   K 6 ALA B 664  VAL B 667  1  O  ILE B 666   N  ALA B 604
SHEET    5   K 6 ILE B 695  ALA B 698  1  O  ALA B 696   N  VAL B 667
SHEET    6   K 6 ILE B 718  ALA B 721  1  O  VAL B 719   N  LEU B 697
SHEET    1   L 2 GLU B 639  THR B 641  0
SHEET    2   L 2 VAL B 647  PRO B 649 -1  O  LEU B 648   N  VAL B 640
SHEET    1   M11 LEU C 400  ASP C 401  0
SHEET    2   M11 PHE C 277  ILE C 280 -1  N  ARG C 278   O  ASP C 401
SHEET    3   M11 ALA C 286  PRO C 295 -1  O  VAL C 289   N  PHE C 277
SHEET    4   M11 GLU C 333  PRO C 342 -1  O  GLU C 335   N  LYS C 294
SHEET    5   M11 VAL C 367  ARG C 377 -1  O  GLN C 368   N  PHE C 338
SHEET    6   M11 GLY C 131  PRO C 140 -1  N  HIS C 135   O  ARG C 377
SHEET    7   M11 THR C 160  SER C 167 -1  O  PHE C 166   N  SER C 132
SHEET    8   M11 GLY C 184  THR C 191 -1  O  LYS C 188   N  PHE C 163
SHEET    9   M11 GLY C 194  ASN C 201 -1  O  PHE C 196   N  PHE C 189
SHEET   10   M11 GLY C 271  PHE C 272 -1  O  PHE C 272   N  ASN C 201
SHEET   11   M11 ALA C 286  PRO C 295 -1  O  TRP C 293   N  GLY C 271
SHEET    1   N 6 ALA C 652  THR C 653  0
SHEET    2   N 6 HIS C 629  TYR C 634  1  N  TYR C 634   O  ALA C 652
SHEET    3   N 6 VAL C 602  LEU C 606  1  N  ILE C 605   O  LYS C 631
SHEET    4   N 6 ALA C 664  VAL C 667  1  O  ILE C 666   N  ALA C 604
SHEET    5   N 6 ILE C 695  ALA C 698  1  O  ALA C 696   N  VAL C 667
SHEET    6   N 6 ILE C 718  ALA C 721  1  O  VAL C 719   N  LEU C 697
SHEET    1   O 2 GLU C 639  THR C 641  0
SHEET    2   O 2 VAL C 647  PRO C 649 -1  O  LEU C 648   N  VAL C 640
SHEET    1   P11 LEU D 400  ASP D 401  0
SHEET    2   P11 PHE D 277  ILE D 280 -1  N  ARG D 278   O  ASP D 401
SHEET    3   P11 ALA D 286  PRO D 295 -1  O  VAL D 289   N  PHE D 277
SHEET    4   P11 GLU D 333  PRO D 342 -1  O  GLU D 335   N  LYS D 294
SHEET    5   P11 VAL D 367  ARG D 377 -1  O  VAL D 370   N  LEU D 336
SHEET    6   P11 GLY D 131  PRO D 140 -1  N  HIS D 135   O  ARG D 377
SHEET    7   P11 THR D 160  SER D 167 -1  O  THR D 160   N  PHE D 138
SHEET    8   P11 GLY D 184  THR D 191 -1  O  LYS D 188   N  PHE D 163
SHEET    9   P11 GLY D 194  ASN D 201 -1  O  PHE D 196   N  PHE D 189
SHEET   10   P11 GLY D 271  PHE D 272 -1  O  PHE D 272   N  ASN D 201
SHEET   11   P11 ALA D 286  PRO D 295 -1  O  TRP D 293   N  GLY D 271
SHEET    1   Q 6 ALA D 652  THR D 653  0
SHEET    2   Q 6 HIS D 629  TYR D 634  1  N  TYR D 634   O  ALA D 652
SHEET    3   Q 6 VAL D 602  LEU D 606  1  N  ILE D 605   O  LEU D 633
SHEET    4   Q 6 ALA D 664  VAL D 667  1  O  ILE D 666   N  ALA D 604
SHEET    5   Q 6 ILE D 695  ALA D 698  1  O  ALA D 696   N  VAL D 667
SHEET    6   Q 6 ILE D 718  ALA D 721  1  O  VAL D 719   N  LEU D 697
SHEET    1   R 2 GLU D 639  THR D 641  0
SHEET    2   R 2 VAL D 647  PRO D 649 -1  O  LEU D 648   N  VAL D 640
LINK         C   PRO A 668                 N   OCS A 669     1555   1555  1.32
LINK         C   OCS A 669                 N   GLY A 670     1555   1555  1.31
LINK         C   PRO B 668                 N   OCS B 669     1555   1555  1.32
LINK         C   OCS B 669                 N   GLY B 670     1555   1555  1.33
LINK         C   PRO C 668                 N   OCS C 669     1555   1555  1.32
LINK         C   OCS C 669                 N   GLY C 670     1555   1555  1.33
LINK         C   PRO D 668                 N   OCS D 669     1555   1555  1.32
LINK         C   OCS D 669                 N   GLY D 670     1555   1555  1.33
LINK         OH  TYR A 415                FE  AHDD A 760     1555   1555  1.74
LINK         OH  TYR D 415                FE  AHDD D 760     1555   1555  1.82
LINK         OH  TYR C 415                FE  AHDD C 760     1555   1555  1.83
LINK         OH  TYR B 415                FE  BHDE B 761     1555   1555  2.05
LINK         OH  TYR A 415                FE  BHDE A 761     1555   1555  2.06
LINK         OH  TYR D 415                FE  BHDE D 761     1555   1555  2.17
LINK        FE  BHDE B 761                 O   HOH B2694     1555   1555  2.19
LINK         OH  TYR C 415                FE  BHDE C 761     1555   1555  2.20
LINK        FE  BHDE A 761                 O   HOH A2520     1555   1555  2.44
LINK        FE  BHDE C 761                 O   HOH C2594     1555   1555  2.47
LINK        FE  AHDD B 760                 O   HOH B2694     1555   1555  2.58
LINK        FE  AHDD A 760                 O   HOH A2520     1555   1555  2.69
LINK        FE  BHDE D 761                 O   HOH D3200     1555   1555  2.69
LINK         ND1 HIS A 392                 CB  TYR A 415     1555   1555  1.66
LINK         ND1 HIS B 392                 CB  TYR B 415     1555   1555  1.70
LINK         ND1 HIS C 392                 CB  TYR C 415     1555   1555  1.71
LINK         ND1 HIS D 392                 CB  TYR D 415     1555   1555  1.67
CISPEP   1 ILE A  229    PRO A  230          0         2.48
CISPEP   2 GLU A  461    PRO A  462          0        -0.09
CISPEP   3 TRP A  469    PRO A  470          0        -3.60
CISPEP   4 ILE B  229    PRO B  230          0         0.90
CISPEP   5 GLU B  461    PRO B  462          0         3.34
CISPEP   6 TRP B  469    PRO B  470          0        -8.15
CISPEP   7 ILE C  229    PRO C  230          0         3.72
CISPEP   8 GLU C  461    PRO C  462          0         3.83
CISPEP   9 TRP C  469    PRO C  470          0        -6.35
CISPEP  10 ILE D  229    PRO D  230          0        -1.03
CISPEP  11 GLU D  461    PRO D  462          0         4.07
CISPEP  12 TRP D  469    PRO D  470          0        -2.35
SITE     1 AC1 25 ARG A 125  VAL A 127  HIS A 128  ARG A 165
SITE     2 AC1 25 GLY A 184  PHE A 185  VAL A 199  GLY A 200
SITE     3 AC1 25 ASN A 201  PHE A 206  PHE A 214  ALA A 274
SITE     4 AC1 25 HIS A 275  PHE A 391  LEU A 407  ARG A 411
SITE     5 AC1 25 SER A 414  TYR A 415  THR A 418  GLN A 419
SITE     6 AC1 25 HOH A 793  HOH A 849  HOH A 879  HOH A2520
SITE     7 AC1 25 HOH A3345
SITE     1 AC2 23 ARG A 125  VAL A 127  HIS A 128  ARG A 165
SITE     2 AC2 23 GLY A 184  VAL A 199  GLY A 200  ASN A 201
SITE     3 AC2 23 ALA A 211  PHE A 214  GLY A 273  ALA A 274
SITE     4 AC2 23 PHE A 391  LEU A 407  ARG A 411  SER A 414
SITE     5 AC2 23 TYR A 415  THR A 418  GLN A 419  HOH A 793
SITE     6 AC2 23 HOH A 849  HOH A2520  HOH A3345
SITE     1 AC3 25 ARG B 125  ILE B 126  VAL B 127  HIS B 128
SITE     2 AC3 25 ARG B 165  GLY B 184  VAL B 199  GLY B 200
SITE     3 AC3 25 ASN B 201  PHE B 206  PHE B 214  HIS B 275
SITE     4 AC3 25 PHE B 391  LEU B 407  ARG B 411  SER B 414
SITE     5 AC3 25 TYR B 415  THR B 418  GLN B 419  ARG B 422
SITE     6 AC3 25 HOH B 851  HOH B 904  HOH B 933  HOH B2694
SITE     7 AC3 25 HOH B3346
SITE     1 AC4 23 ARG B 125  VAL B 127  HIS B 128  ARG B 165
SITE     2 AC4 23 GLY B 184  VAL B 199  GLY B 200  ASN B 201
SITE     3 AC4 23 ALA B 211  PHE B 214  GLY B 273  PHE B 391
SITE     4 AC4 23 LEU B 407  ARG B 411  SER B 414  TYR B 415
SITE     5 AC4 23 THR B 418  GLN B 419  HOH B 840  HOH B 851
SITE     6 AC4 23 HOH B 904  HOH B2694  HOH B3346
SITE     1 AC5 22 ARG C 125  VAL C 127  HIS C 128  ARG C 165
SITE     2 AC5 22 GLY C 184  VAL C 199  GLY C 200  ASN C 201
SITE     3 AC5 22 PHE C 206  PHE C 214  HIS C 275  PHE C 391
SITE     4 AC5 22 LEU C 407  ARG C 411  SER C 414  TYR C 415
SITE     5 AC5 22 THR C 418  GLN C 419  HOH C 871  HOH C 929
SITE     6 AC5 22 HOH C2594  HOH C3347
SITE     1 AC6 24 ARG C 125  VAL C 127  HIS C 128  ARG C 165
SITE     2 AC6 24 GLY C 184  VAL C 199  GLY C 200  ASN C 201
SITE     3 AC6 24 ALA C 211  PHE C 214  GLY C 273  ALA C 274
SITE     4 AC6 24 PHE C 391  LEU C 407  ARG C 411  SER C 414
SITE     5 AC6 24 TYR C 415  THR C 418  GLN C 419  HOH C 871
SITE     6 AC6 24 HOH C 929  HOH C1263  HOH C2594  HOH C3347
SITE     1 AC7 23 ARG D 125  VAL D 127  HIS D 128  ARG D 165
SITE     2 AC7 23 GLY D 184  VAL D 199  GLY D 200  ASN D 201
SITE     3 AC7 23 PHE D 206  PHE D 214  ALA D 274  PHE D 391
SITE     4 AC7 23 LEU D 407  ARG D 411  SER D 414  TYR D 415
SITE     5 AC7 23 THR D 418  GLN D 419  HOH D1295  HOH D1353
SITE     6 AC7 23 HOH D1388  HOH D3200  HOH D3348
SITE     1 AC8 22 ARG D 125  VAL D 127  HIS D 128  ARG D 165
SITE     2 AC8 22 GLY D 184  VAL D 199  GLY D 200  ASN D 201
SITE     3 AC8 22 ALA D 211  PHE D 214  GLY D 273  PHE D 391
SITE     4 AC8 22 LEU D 407  ARG D 411  SER D 414  TYR D 415
SITE     5 AC8 22 THR D 418  GLN D 419  HOH D1295  HOH D1353
SITE     6 AC8 22 HOH D3200  HOH D3348
CRYST1   93.560  133.170  122.810  90.00 109.24  90.00 P 1 21 1      8
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      0.010688  0.000000  0.003730        0.00000
SCALE2      0.000000  0.007509  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008624        0.00000
      
PROCHECK
Go to PROCHECK summary
 References