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PDBsum entry 3p9q

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3p9q
Jmol
Contents
Protein chains
726 a.a.
Ligands
HDD-HDE ×4
H2S ×4
Waters ×3496
HEADER    OXIDOREDUCTASE                          18-OCT-10   3P9Q
TITLE     STRUCTURE OF I274C VARIANT OF E. COLI KATE
CAVEAT     3P9Q    CHIRALITY ERROR AT ILE159C
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, I274C 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 3P9Q    1       JRNL
REVDAT   1   22-DEC-10 3P9Q    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.    1.48 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) : 1.48
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.55
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.7
REMARK   3   NUMBER OF REFLECTIONS             : 429789
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) : 0.145
REMARK   3   R VALUE            (WORKING SET) : 0.143
REMARK   3   FREE R VALUE                     : 0.177
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 21507
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) : 1.48
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 25943
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.78
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640
REMARK   3   BIN FREE R VALUE SET COUNT          : 1321
REMARK   3   BIN FREE R VALUE                    : 0.3000
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 22936
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 356
REMARK   3   SOLVENT ATOMS            : 3496
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.43
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.18000
REMARK   3    B22 (A**2) : -0.48000
REMARK   3    B33 (A**2) : 0.93000
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : 0.40000
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): 0.071
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.518
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 24090 ; 0.029 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 32914 ; 2.357 ; 1.989
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2908 ; 6.416 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1183 ;36.801 ;23.838
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3782 ;13.830 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   178 ;14.016 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3447 ; 0.226 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 18986 ; 0.015 ; 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): 14571 ; 1.239 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23577 ; 1.921 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9519 ; 2.838 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9337 ; 4.230 ; 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):   5699 ; 0.370 ; 0.500
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   5699 ; 0.320 ; 0.500
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   5699 ; 0.310 ; 0.500
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   5699 ; 0.340 ; 0.500
REMARK   3   MEDIUM THERMAL     1    A (A**2):   5699 ; 1.860 ; 2.000
REMARK   3   MEDIUM THERMAL     1    B (A**2):   5699 ; 1.620 ; 2.000
REMARK   3   MEDIUM THERMAL     1    C (A**2):   5699 ; 1.520 ; 2.000
REMARK   3   MEDIUM THERMAL     1    D (A**2):   5699 ; 1.410 ; 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):   2.6378  -9.3164  31.5070
REMARK   3    T TENSOR
REMARK   3      T11:   0.0088 T22:   0.0104
REMARK   3      T33:   0.0205 T12:   0.0036
REMARK   3      T13:   0.0085 T23:   0.0135
REMARK   3    L TENSOR
REMARK   3      L11:   0.0929 L22:   0.1072
REMARK   3      L33:   0.0741 L12:  -0.0043
REMARK   3      L13:   0.0115 L23:  -0.0134
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0090 S12:  -0.0232 S13:  -0.0307
REMARK   3      S21:   0.0221 S22:   0.0133 S23:   0.0308
REMARK   3      S31:   0.0081 S32:  -0.0060 S33:  -0.0043
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):   3.6654  11.8338 -18.5991
REMARK   3    T TENSOR
REMARK   3      T11:   0.0379 T22:   0.0112
REMARK   3      T33:   0.0174 T12:  -0.0050
REMARK   3      T13:  -0.0138 T23:   0.0127
REMARK   3    L TENSOR
REMARK   3      L11:   0.0820 L22:   0.1425
REMARK   3      L33:   0.0797 L12:  -0.0255
REMARK   3      L13:  -0.0180 L23:  -0.0118
REMARK   3    S TENSOR
REMARK   3      S11:   0.0024 S12:   0.0236 S13:   0.0296
REMARK   3      S21:  -0.0675 S22:   0.0029 S23:   0.0168
REMARK   3      S31:  -0.0099 S32:  -0.0080 S33:  -0.0052
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):  26.5891 -12.0283 -19.6280
REMARK   3    T TENSOR
REMARK   3      T11:   0.0486 T22:   0.0112
REMARK   3      T33:   0.0081 T12:  -0.0032
REMARK   3      T13:   0.0128 T23:  -0.0068
REMARK   3    L TENSOR
REMARK   3      L11:   0.0874 L22:   0.1310
REMARK   3      L33:   0.0731 L12:   0.0114
REMARK   3      L13:   0.0025 L23:  -0.0091
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0129 S12:   0.0202 S13:  -0.0204
REMARK   3      S21:  -0.0722 S22:   0.0097 S23:  -0.0163
REMARK   3      S31:   0.0274 S32:   0.0167 S33:   0.0033
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):  30.0749   9.4418  31.5180
REMARK   3    T TENSOR
REMARK   3      T11:   0.0102 T22:   0.0205
REMARK   3      T33:   0.0076 T12:  -0.0015
REMARK   3      T13:  -0.0051 T23:  -0.0062
REMARK   3    L TENSOR
REMARK   3      L11:   0.1007 L22:   0.1024
REMARK   3      L33:   0.0581 L12:   0.0290
REMARK   3      L13:  -0.0220 L23:  -0.0002
REMARK   3    S TENSOR
REMARK   3      S11:   0.0028 S12:  -0.0305 S13:   0.0168
REMARK   3      S21:   0.0230 S22:  -0.0009 S23:  -0.0144
REMARK   3      S31:  -0.0127 S32:   0.0262 S33:  -0.0019
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 3P9Q 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 RCSB062133.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-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 CRYSTAL
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   : 429958
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.550
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8
REMARK 200  DATA REDUNDANCY                : 3.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08100
REMARK 200   FOR THE DATA SET  : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.48300
REMARK 200  R SYM FOR SHELL            (I) : 0.48300
REMARK 200   FOR SHELL         : 1.600
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   (%): 42.42
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       66.51000
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: 57570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -299.0 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   O    HOH A  2305     O    HOH A  3509              1.59
REMARK 500   O    HOH A  1712     O    HOH A  3179              1.81
REMARK 500   O    HOH D  2813     O    HOH D  3139              1.85
REMARK 500   O    HOH D  1721     O    HOH D  2639              1.86
REMARK 500   O    HOH D  1832     O    HOH D  2497              1.90
REMARK 500   O    HOH D  2393     O    HOH D  2703              1.91
REMARK 500   OH   TYR C   440     O    HOH C  1792              1.94
REMARK 500   CD   LYS A    73     O    HOH C  3442              1.94
REMARK 500   O    HOH C  2088     O    HOH C  2444              1.95
REMARK 500   O    HOH C  1971     O    HOH C  2082              1.96
REMARK 500   O    HOH B  1083     O    HOH B  3420              2.03
REMARK 500   CG2  THR D   416     O    HOH D  3576              2.03
REMARK 500   O    HOH A  2377     O    HOH A  3042              2.04
REMARK 500   O    HOH B  2909     O    HOH B  2958              2.04
REMARK 500   O    HOH B  2689     O    HOH D  3582              2.06
REMARK 500   OD1  ASP D   700     O    HOH D  3236              2.07
REMARK 500   OE2  GLU D   731     O    HOH D  3028              2.07
REMARK 500   CB   ASP C   578     O    HOH C  2919              2.07
REMARK 500   OD1  ASP C   578     O    HOH C  3157              2.08
REMARK 500   O    HOH A  1111     O    HOH A  3235              2.09
REMARK 500   O    HOH C  2300     O    HOH C  3144              2.09
REMARK 500   O    HOH A  3198     O    HOH C  2554              2.09
REMARK 500   O    HOH A  2363     O    HOH A  2782              2.12
REMARK 500   O    HOH A   820     O    HOH D  2275              2.13
REMARK 500   O    ASP C   725     O    HOH C  2403              2.14
REMARK 500   OG   SER A   532     O    HOH A  2410              2.15
REMARK 500   O    HOH D  1959     O    HOH D  3443              2.15
REMARK 500   OD1  ASP B    70     O    HOH B  2761              2.15
REMARK 500   O    HOH B  2392     O    HOH C  3469              2.16
REMARK 500   OD2  ASP C    59     O    HOH C  2529              2.17
REMARK 500   O    HOH B  1854     O    HOH B  2865              2.18
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 A  3241     O    HOH D  2457     2646     1.92
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    LEU A  29   N     LEU A  29   CA     -0.132
REMARK 500    GLU A 321   CD    GLU A 321   OE1     0.107
REMARK 500    TYR A 460   CE1   TYR A 460   CZ      0.091
REMARK 500    ARG B  37   CZ    ARG B  37   NH2     0.096
REMARK 500    PHE B 272   CZ    PHE B 272   CE2     0.117
REMARK 500    GLU B 333   CD    GLU B 333   OE1    -0.069
REMARK 500    ARG B 521   CG    ARG B 521   CD      0.173
REMARK 500    ASP C  59   CB    ASP C  59   CG      0.182
REMARK 500    ASP C  59   CG    ASP C  59   OD1     0.148
REMARK 500    ARG C 377   CZ    ARG C 377   NH1     0.082
REMARK 500    ARG C 495   CZ    ARG C 495   NH1     0.079
REMARK 500    SER D  28   CB    SER D  28   OG      0.126
REMARK 500    PHE D 206   CD1   PHE D 206   CE1     0.138
REMARK 500    PHE D 214   CZ    PHE D 214   CE2     0.120
REMARK 500    GLU D 321   CD    GLU D 321   OE1     0.098
REMARK 500    GLU D 333   CD    GLU D 333   OE2    -0.077
REMARK 500    ARG D 369   CG    ARG D 369   CD      0.155
REMARK 500    TYR D 415   CE1   TYR D 415   CZ      0.079
REMARK 500    TYR D 440   CE1   TYR D 440   CZ      0.098
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    LEU A  29   C   -  N   -  CA  ANGL. DEV. = -18.4 DEGREES
REMARK 500    ASP A 118   CB  -  CG  -  OD1 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG A 130   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ARG A 165   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ASP A 177   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 313   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ARG A 479   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    LEU A 552   CB  -  CG  -  CD1 ANGL. DEV. =  10.9 DEGREES
REMARK 500    ARG A 612   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP A 663   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    ASP B  70   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG B  96   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    PHE B 108   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    LYS B 158   CA  -  CB  -  CG  ANGL. DEV. = -14.0 DEGREES
REMARK 500    ARG B 278   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG B 313   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG B 369   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG B 495   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG B 521   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    MET B 686   CG  -  SD  -  CE  ANGL. DEV. =  -9.8 DEGREES
REMARK 500    ARG B 740   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG C  37   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG C  37   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ASP C  59   CB  -  CG  -  OD1 ANGL. DEV. =   9.4 DEGREES
REMARK 500    ASP C  59   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP C  70   CB  -  CG  -  OD1 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    ASP C  70   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG C 125   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG C 267   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG C 319   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG C 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG C 445   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG C 471   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    LEU C 606   CB  -  CG  -  CD1 ANGL. DEV. =  10.4 DEGREES
REMARK 500    ARG C 612   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG C 636   NE  -  CZ  -  NH1 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ARG C 636   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    ARG D  61   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG D  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ASP D 177   CB  -  CG  -  OD1 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    ARG D 180   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    PHE D 185   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG D 278   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG D 313   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    GLU D 344   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES
REMARK 500    ARG D 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      60 ANGLE DEVIATIONS.
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      -37.66   -166.56
REMARK 500    THR A 178       39.53    -92.83
REMARK 500    CYS A 274      -43.85     83.20
REMARK 500    ASP A 446     -148.32     69.70
REMARK 500    ASP A 595       33.21   -150.75
REMARK 500    HIS A 739      -61.63     74.67
REMARK 500    ALA B  40       58.43    -91.51
REMARK 500    SER B  75      -38.51   -163.27
REMARK 500    THR B 178       38.55    -94.13
REMARK 500    CYS B 274      -42.60     71.06
REMARK 500    ASP B 314       83.36   -151.96
REMARK 500    ASN B 427       30.87    -95.76
REMARK 500    ASP B 446     -149.12     68.37
REMARK 500    ASP B 595       25.09   -154.98
REMARK 500    ARG B 612       99.18    -66.36
REMARK 500    ALA B 724       29.03    -77.48
REMARK 500    ASP B 725     -175.48    -30.99
REMARK 500    HIS B 739      -64.42     74.96
REMARK 500    SER C  75      -42.22   -167.43
REMARK 500    THR C 178       37.52    -93.03
REMARK 500    CYS C 274      -38.12     76.70
REMARK 500    ASN C 442     -169.36   -166.08
REMARK 500    ASP C 446     -149.08     69.93
REMARK 500    LYS C 584      162.04    171.68
REMARK 500    ASP C 595       35.11   -141.53
REMARK 500    ALA C 724       33.67    -85.20
REMARK 500    ASP C 725     -123.10   -139.58
REMARK 500    HIS C 739      -63.69     71.01
REMARK 500    SER D  75      -37.25   -165.11
REMARK 500    THR D 178       41.64    -93.15
REMARK 500    CYS D 274      -46.36     78.08
REMARK 500    ASP D 314       88.23   -155.78
REMARK 500    ASN D 427       31.60    -95.96
REMARK 500    ASP D 446     -151.93     65.49
REMARK 500    ASP D 595       36.47   -141.92
REMARK 500    HIS D 739      -65.93     78.59
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                  144.86
REMARK 500 ASP C  725     GLY C  726                 -147.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A 121         0.08    SIDE CHAIN
REMARK 500    ARG B 121         0.08    SIDE CHAIN
REMARK 500    ARG C 121         0.08    SIDE CHAIN
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    LEU A  29        24.5      L          L   OUTSIDE RANGE
REMARK 500    ASP A 350        24.9      L          L   OUTSIDE RANGE
REMARK 500    SER C  28        22.0      L          L   OUTSIDE RANGE
REMARK 500    ASP C 725        11.1      L          L   OUTSIDE RANGE
REMARK 500    SER D  28        21.6      L          L   OUTSIDE RANGE
REMARK 500    ILE C 159       -11.1      S          R   CBETA WRONG HAND
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 A1088        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH A2186        DISTANCE =  6.48 ANGSTROMS
REMARK 525    HOH A2213        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH A2238        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH A2352        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH A2449        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A2805        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A2824        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH A2979        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH B 774        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH B 779        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH B2233        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH B2749        DISTANCE =  6.31 ANGSTROMS
REMARK 525    HOH B2829        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH B3006        DISTANCE =  5.96 ANGSTROMS
REMARK 525    HOH B3034        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH B3216        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH B3373        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH C1533        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH C2237        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH C2871        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH C3052        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH C3207        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH C3486        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH D1620        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH D2004        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH D2187        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH D2212        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH D2468        DISTANCE =  6.63 ANGSTROMS
REMARK 525    HOH D2524        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH D2547        DISTANCE =  5.81 ANGSTROMS
REMARK 525    HOH D2693        DISTANCE =  6.45 ANGSTROMS
REMARK 525    HOH D2736        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH D2999        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH D3051        DISTANCE =  6.20 ANGSTROMS
REMARK 525    HOH D3083        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH D3544        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH D3581        DISTANCE =  5.84 ANGSTROMS
REMARK 525    HOH D3587        DISTANCE =  5.73 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 B 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 415   OH
REMARK 620 2 HDD B 760   NA   93.8
REMARK 620 3 HDD B 760   NB   84.6  92.3
REMARK 620 4 HDD B 760   NC   92.1 174.0  89.2
REMARK 620 5 HDD B 760   ND  100.6  87.1 174.7  90.8
REMARK 620 6 HOH B3593   O   165.9  83.0  81.8  91.5  92.9
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   95.8
REMARK 620 3 HDD D 760   NB   85.8  93.0
REMARK 620 4 HDD D 760   NC   90.3 173.7  89.1
REMARK 620 5 HDD D 760   ND   99.7  87.4 174.4  89.9
REMARK 620 6 HOH D3252   O   164.2  79.7  79.4  94.8  95.2
REMARK 620 N                    1     2     3     4     5
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   92.3
REMARK 620 3 HDD C 760   NB   87.1  90.9
REMARK 620 4 HDD C 760   NC   92.8 174.8  89.9
REMARK 620 5 HDD C 760   ND   97.3  89.7 175.6  89.1
REMARK 620 6 HOH C3277   O   167.2  80.0  82.8  95.0  93.0
REMARK 620 N                    1     2     3     4     5
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   96.2
REMARK 620 3 HDD A 760   NB   90.9  88.8
REMARK 620 4 HDD A 760   NC   90.0 173.6  89.7
REMARK 620 5 HDD A 760   ND   94.4  90.4 174.7  90.4
REMARK 620 6 HOH A3592   O   176.2  81.5  86.0  92.2  88.7
REMARK 620 N                    1     2     3     4     5
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 HOH B3593   O
REMARK 620 2 HDE B 761   NA   90.8
REMARK 620 3 HDE B 761   NB   88.1  88.3
REMARK 620 4 HDE B 761   NC   87.1 177.9  91.8
REMARK 620 5 HDE B 761   ND   90.7  90.8 178.5  89.1
REMARK 620 6 TYR B 415   OH  178.9  90.2  91.6  91.8  89.6
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   99.2
REMARK 620 3 HDE A 761   NB   98.0  88.7
REMARK 620 4 HDE A 761   NC   82.9 177.5  92.4
REMARK 620 5 HDE A 761   ND   84.0  91.4 178.0  87.4
REMARK 620 6 HOH A3592   O   154.3 106.1  87.0  71.7  91.1
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 HOH C3277   O
REMARK 620 2 HDE C 761   NA   96.4
REMARK 620 3 HDE C 761   NB   89.6  87.0
REMARK 620 4 HDE C 761   NC   81.3 177.7  93.0
REMARK 620 5 HDE C 761   ND   89.0  92.3 178.4  87.7
REMARK 620 6 TYR C 415   OH  168.0  95.2  94.3  87.1  87.1
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   91.6
REMARK 620 3 HDE D 761   NB   94.4  86.8
REMARK 620 4 HDE D 761   NC   90.8 177.6  93.4
REMARK 620 5 HDE D 761   ND   87.3  92.4 178.2  87.3
REMARK 620 6 HOH D3252   O   170.6  97.3  89.1  80.3  89.4
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 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 H2S A 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD B 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE B 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S B 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD C 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE C 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S C 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD D 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE D 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S D 754
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P9P   RELATED DB: PDB
REMARK 900 RELATED ID: 3P9R   RELATED DB: PDB
REMARK 900 RELATED ID: 3P9S   RELATED DB: PDB
DBREF  3P9Q A    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  3P9Q B    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  3P9Q C    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  3P9Q D    1   753  UNP    P21179   CATE_ECOLI       1    753
SEQADV 3P9Q CYS A  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQADV 3P9Q ALA A  438  UNP  P21179    CYS   438 ENGINEERED MUTATION
SEQADV 3P9Q ALA A  669  UNP  P21179    CYS   669 ENGINEERED MUTATION
SEQADV 3P9Q CYS B  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQADV 3P9Q ALA B  438  UNP  P21179    CYS   438 ENGINEERED MUTATION
SEQADV 3P9Q ALA B  669  UNP  P21179    CYS   669 ENGINEERED MUTATION
SEQADV 3P9Q CYS C  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQADV 3P9Q ALA C  438  UNP  P21179    CYS   438 ENGINEERED MUTATION
SEQADV 3P9Q ALA C  669  UNP  P21179    CYS   669 ENGINEERED MUTATION
SEQADV 3P9Q CYS D  274  UNP  P21179    ILE   274 ENGINEERED MUTATION
SEQADV 3P9Q ALA D  438  UNP  P21179    CYS   438 ENGINEERED MUTATION
SEQADV 3P9Q ALA D  669  UNP  P21179    CYS   669 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  CYS 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 ALA 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 ALA 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  CYS 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 ALA 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 ALA 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  CYS 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 ALA 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 ALA 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  CYS 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 ALA 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 ALA 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
HET    HDD  A 760      44
HET    HDE  A 761      44
HET    H2S  A 754       1
HET    HDD  B 760      44
HET    HDE  B 761      44
HET    H2S  B 754       1
HET    HDD  C 760      44
HET    HDE  C 761      44
HET    H2S  C 754       1
HET    HDD  D 760      44
HET    HDE  D 761      44
HET    H2S  D 754       1
HETNAM     HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE
HETNAM     HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S
HETNAM     H2S HYDROSULFURIC ACID
HETSYN     HDD HEME
HETSYN     H2S HYDROGEN SULFIDE
FORMUL   5  HDD    4(C34 H32 FE N4 O5)
FORMUL   6  HDE    4(C34 H38 FE N4 O5)
FORMUL   7  H2S    4(H2 S)
FORMUL  17  HOH   *3496(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  THR A  418  1                                  14
HELIX   16  16 THR A  418  LEU A  423  1                                   6
HELIX   17  17 ASN A  427  ARG A  435  5                                   9
HELIX   18  18 SER A  498  GLY A  502  5                                   5
HELIX   19  19 TYR A  505  SER A  514  1                                  10
HELIX   20  20 THR A  516  LYS A  533  1                                  18
HELIX   21  21 ARG A  536  HIS A  549  1                                  14
HELIX   22  22 ASP A  551  LEU A  562  1                                  12
HELIX   23  23 THR A  567  ASN A  572  1                                   6
HELIX   24  24 ASP A  585  SER A  589  5                                   5
HELIX   25  25 ARG A  612  LYS A  626  1                                  15
HELIX   26  26 PRO A  658  VAL A  662  5                                   5
HELIX   27  27 ASN A  671  ILE A  675  5                                   5
HELIX   28  28 ASN A  678  HIS A  691  1                                  14
HELIX   29  29 ASP A  700  LYS A  709  5                                  10
HELIX   30  30 ASP A  725  ALA A  738  1                                  14
HELIX   31  31 VAL A  741  SER A  743  5                                   3
HELIX   32  32 ARG A  744  ASP A  749  1                                   6
HELIX   33  33 PRO B   52  ALA B   57  1                                   6
HELIX   34  34 ASN B   62  LEU B   68  1                                   7
HELIX   35  35 ASP B  107  HIS B  119  1                                  13
HELIX   36  36 ALA B  150  SER B  154  5                                   5
HELIX   37  37 ASP B  210  HIS B  212  5                                   3
HELIX   38  38 LYS B  213  LYS B  222  1                                  10
HELIX   39  39 HIS B  236  GLN B  246  1                                  11
HELIX   40  40 THR B  249  SER B  258  1                                  10
HELIX   41  41 ASP B  259  ILE B  262  5                                   4
HELIX   42  42 SER B  265  MET B  269  5                                   5
HELIX   43  43 VAL B  303  ASP B  314  1                                  12
HELIX   44  44 ASP B  316  GLY B  329  1                                  14
HELIX   45  45 GLU B  344  GLU B  346  5                                   3
HELIX   46  46 ASN B  381  ASN B  386  1                                   6
HELIX   47  47 ASP B  405  THR B  418  1                                  14
HELIX   48  48 THR B  418  LEU B  423  1                                   6
HELIX   49  49 ASN B  427  ARG B  435  5                                   9
HELIX   50  50 SER B  498  GLY B  502  5                                   5
HELIX   51  51 TYR B  505  GLN B  515  1                                  11
HELIX   52  52 THR B  516  LYS B  533  1                                  18
HELIX   53  53 ARG B  536  HIS B  549  1                                  14
HELIX   54  54 ASP B  551  LEU B  562  1                                  12
HELIX   55  55 THR B  567  ASN B  572  1                                   6
HELIX   56  56 ASP B  585  SER B  589  5                                   5
HELIX   57  57 ARG B  612  LYS B  626  1                                  15
HELIX   58  58 PRO B  658  VAL B  662  5                                   5
HELIX   59  59 ASN B  671  ILE B  675  5                                   5
HELIX   60  60 ASN B  678  HIS B  691  1                                  14
HELIX   61  61 ASP B  700  THR B  707  5                                   8
HELIX   62  62 ASP B  725  ALA B  738  1                                  14
HELIX   63  63 VAL B  741  SER B  743  5                                   3
HELIX   64  64 ARG B  744  ASP B  749  1                                   6
HELIX   65  65 PRO C   52  ALA C   57  1                                   6
HELIX   66  66 ASN C   62  LEU C   68  1                                   7
HELIX   67  67 ASP C  107  HIS C  119  1                                  13
HELIX   68  68 ALA C  150  SER C  154  5                                   5
HELIX   69  69 ASP C  210  HIS C  212  5                                   3
HELIX   70  70 LYS C  213  LYS C  222  1                                  10
HELIX   71  71 HIS C  236  GLN C  246  1                                  11
HELIX   72  72 THR C  249  SER C  258  1                                  10
HELIX   73  73 ASP C  259  ILE C  262  5                                   4
HELIX   74  74 SER C  265  MET C  269  5                                   5
HELIX   75  75 VAL C  303  ASP C  314  1                                  12
HELIX   76  76 ASP C  316  GLY C  329  1                                  14
HELIX   77  77 GLU C  344  GLU C  346  5                                   3
HELIX   78  78 ASN C  381  ASN C  386  1                                   6
HELIX   79  79 ASP C  405  THR C  418  1                                  14
HELIX   80  80 THR C  418  LEU C  423  1                                   6
HELIX   81  81 ASN C  427  ARG C  435  5                                   9
HELIX   82  82 SER C  498  GLY C  502  5                                   5
HELIX   83  83 TYR C  505  SER C  514  1                                  10
HELIX   84  84 THR C  516  LYS C  533  1                                  18
HELIX   85  85 ARG C  536  HIS C  549  1                                  14
HELIX   86  86 ASP C  551  LEU C  562  1                                  12
HELIX   87  87 THR C  567  ASN C  572  1                                   6
HELIX   88  88 ASP C  585  SER C  589  5                                   5
HELIX   89  89 ARG C  612  LYS C  626  1                                  15
HELIX   90  90 PRO C  658  VAL C  662  5                                   5
HELIX   91  91 ILE C  672  ASP C  677  1                                   6
HELIX   92  92 ASN C  678  HIS C  691  1                                  14
HELIX   93  93 ASP C  700  ALA C  706  5                                   7
HELIX   94  94 SER C  727  ALA C  738  1                                  12
HELIX   95  95 VAL C  741  SER C  743  5                                   3
HELIX   96  96 ARG C  744  ASP C  749  1                                   6
HELIX   97  97 PRO D   52  ALA D   57  1                                   6
HELIX   98  98 ASN D   62  LEU D   68  1                                   7
HELIX   99  99 ASP D  107  HIS D  119  1                                  13
HELIX  100 100 ALA D  150  SER D  154  5                                   5
HELIX  101 101 ASP D  210  HIS D  212  5                                   3
HELIX  102 102 LYS D  213  LYS D  222  1                                  10
HELIX  103 103 HIS D  236  GLN D  246  1                                  11
HELIX  104 104 THR D  249  SER D  258  1                                  10
HELIX  105 105 ASP D  259  ILE D  262  5                                   4
HELIX  106 106 SER D  265  MET D  269  5                                   5
HELIX  107 107 VAL D  303  ASP D  314  1                                  12
HELIX  108 108 ASP D  316  GLY D  329  1                                  14
HELIX  109 109 GLU D  344  GLU D  346  5                                   3
HELIX  110 110 ASN D  381  ASN D  386  1                                   6
HELIX  111 111 ASP D  405  THR D  418  1                                  14
HELIX  112 112 THR D  418  LEU D  423  1                                   6
HELIX  113 113 ASN D  427  ARG D  435  5                                   9
HELIX  114 114 SER D  498  GLY D  502  5                                   5
HELIX  115 115 TYR D  505  GLN D  515  1                                  11
HELIX  116 116 THR D  516  LYS D  533  1                                  18
HELIX  117 117 ARG D  536  HIS D  549  1                                  14
HELIX  118 118 ASP D  551  LEU D  562  1                                  12
HELIX  119 119 THR D  567  ASN D  572  1                                   6
HELIX  120 120 ASP D  585  SER D  589  5                                   5
HELIX  121 121 ARG D  612  LYS D  626  1                                  15
HELIX  122 122 PRO D  658  VAL D  662  5                                   5
HELIX  123 123 ASN D  671  ILE D  675  5                                   5
HELIX  124 124 ASN D  678  HIS D  691  1                                  14
HELIX  125 125 ASP D  700  ILE D  708  5                                   9
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  GLN A 368   N  PHE A 338
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  TYR A 190   N  PRO A 161
SHEET    9   C11 GLY A 194  ASN A 201 -1  O  PHE A 196   N  PHE A 189
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 LEU C  95  ALA C  97  0
SHEET    2   E 4 ARG B 488  ARG B 495 -1  N  VAL B 494   O  ARG C  96
SHEET    3   E 4 ARG A 488  ARG A 495 -1  N  GLY A 491   O  VAL B 489
SHEET    4   E 4 LEU D  95  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  ILE A 695
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  VAL B 289   N  PHE B 277
SHEET    4   I11 GLU B 333  PRO B 342 -1  O  GLY B 337   N  HIS B 292
SHEET    5   I11 GLN B 368  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 665
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  GLY C 337   N  HIS C 292
SHEET    5   M11 GLN C 368  ARG C 377 -1  O  VAL C 370   N  LEU C 336
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  THR C 160   N  PHE C 138
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  GLN D 339   N  ARG D 290
SHEET    5   P11 GLN D 368  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  PHE D 166   N  SER D 132
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  LYS D 631
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         OH  TYR B 415                FE  AHDD B 760     1555   1555  1.84
LINK         OH  TYR D 415                FE  AHDD D 760     1555   1555  1.90
LINK         OH  TYR C 415                FE  AHDD C 760     1555   1555  1.91
LINK         OH  TYR A 415                FE  AHDD A 760     1555   1555  1.92
LINK        FE  BHDE B 761                 O   HOH B3593     1555   1555  1.99
LINK         OH  TYR A 415                FE  BHDE A 761     1555   1555  2.11
LINK        FE  BHDE A 761                 O   HOH A3592     1555   1555  2.14
LINK         OH  TYR B 415                FE  BHDE B 761     1555   1555  2.17
LINK        FE  BHDE C 761                 O   HOH C3277     1555   1555  2.17
LINK         OH  TYR D 415                FE  BHDE D 761     1555   1555  2.18
LINK        FE  BHDE D 761                 O   HOH D3252     1555   1555  2.18
LINK         OH  TYR C 415                FE  BHDE C 761     1555   1555  2.19
LINK        FE  AHDD A 760                 O   HOH A3592     1555   1555  2.22
LINK        FE  AHDD B 760                 O   HOH B3593     1555   1555  2.36
LINK        FE  AHDD C 760                 O   HOH C3277     1555   1555  2.45
LINK        FE  AHDD D 760                 O   HOH D3252     1555   1555  2.49
LINK         ND1 HIS A 392                 CB  TYR A 415     1555   1555  1.57
LINK         ND1 HIS B 392                 CB  TYR B 415     1555   1555  1.58
LINK         ND1 HIS C 392                 CB  TYR C 415     1555   1555  1.54
LINK         ND1 HIS D 392                 CB  TYR D 415     1555   1555  1.54
CISPEP   1 ILE A  229    PRO A  230          0         7.91
CISPEP   2 GLU A  461    PRO A  462          0         9.61
CISPEP   3 TRP A  469    PRO A  470          0        -2.78
CISPEP   4 ILE B  229    PRO B  230          0         6.66
CISPEP   5 GLU B  461    PRO B  462          0         3.11
CISPEP   6 TRP B  469    PRO B  470          0        -7.30
CISPEP   7 ILE C  229    PRO C  230          0        -0.11
CISPEP   8 GLU C  461    PRO C  462          0        -0.54
CISPEP   9 TRP C  469    PRO C  470          0        -0.50
CISPEP  10 ILE D  229    PRO D  230          0         0.47
CISPEP  11 GLU D  461    PRO D  462          0         5.60
CISPEP  12 TRP D  469    PRO D  470          0        -3.40
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  CYS 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 H2S A 754  HOH A 792  HOH A 849  HOH A 877
SITE     7 AC1 25 HOH A3592
SITE     1 AC2 22 ARG A 125  VAL A 127  HIS A 128  ARG A 165
SITE     2 AC2 22 VAL A 199  GLY A 200  ASN A 201  ALA A 211
SITE     3 AC2 22 PHE A 214  CYS A 274  PHE A 391  LEU A 407
SITE     4 AC2 22 ARG A 411  SER A 414  TYR A 415  THR A 418
SITE     5 AC2 22 GLN A 419  ARG A 422  H2S A 754  HOH A 792
SITE     6 AC2 22 HOH A 849  HOH A3592
SITE     1 AC3  4 CYS A 274  HDD A 760  HDE A 761  HOH A3466
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 PHE B 206  PHE B 214  CYS B 274  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  H2S B 754  HOH B 847
SITE     6 AC4 23 HOH B 898  HOH B 928  HOH B3593
SITE     1 AC5 24 ARG B 125  VAL B 127  HIS B 128  ARG B 165
SITE     2 AC5 24 GLY B 184  PHE B 185  VAL B 199  GLY B 200
SITE     3 AC5 24 ASN B 201  ALA B 211  PHE B 214  CYS B 274
SITE     4 AC5 24 HIS B 275  PHE B 391  LEU B 407  ARG B 411
SITE     5 AC5 24 SER B 414  TYR B 415  THR B 418  GLN B 419
SITE     6 AC5 24 H2S B 754  HOH B 847  HOH B 898  HOH B3593
SITE     1 AC6  3 CYS B 274  HDD B 760  HDE B 761
SITE     1 AC7 24 ARG C 125  VAL C 127  HIS C 128  ARG C 165
SITE     2 AC7 24 GLY C 184  VAL C 199  GLY C 200  ASN C 201
SITE     3 AC7 24 PHE C 206  PHE C 214  CYS C 274  PHE C 391
SITE     4 AC7 24 LEU C 407  ARG C 411  SER C 414  TYR C 415
SITE     5 AC7 24 THR C 418  GLN C 419  ARG C 422  H2S C 754
SITE     6 AC7 24 HOH C 871  HOH C 929  HOH C 964  HOH C3277
SITE     1 AC8 21 ARG C 125  VAL C 127  HIS C 128  ARG C 165
SITE     2 AC8 21 VAL C 199  GLY C 200  ASN C 201  ALA C 211
SITE     3 AC8 21 PHE C 214  CYS C 274  PHE C 391  LEU C 407
SITE     4 AC8 21 ARG C 411  SER C 414  TYR C 415  THR C 418
SITE     5 AC8 21 GLN C 419  H2S C 754  HOH C 871  HOH C 929
SITE     6 AC8 21 HOH C3277
SITE     1 AC9  4 PHE C 206  CYS C 274  HDD C 760  HDE C 761
SITE     1 BC1 23 ARG D 125  VAL D 127  HIS D 128  ARG D 165
SITE     2 BC1 23 GLY D 184  VAL D 199  GLY D 200  ASN D 201
SITE     3 BC1 23 PHE D 214  CYS D 274  HIS D 275  PHE D 391
SITE     4 BC1 23 LEU D 407  ARG D 411  SER D 414  TYR D 415
SITE     5 BC1 23 THR D 418  GLN D 419  H2S D 754  HOH D1295
SITE     6 BC1 23 HOH D1353  HOH D1388  HOH D3252
SITE     1 BC2 24 ARG D 125  VAL D 127  HIS D 128  ARG D 165
SITE     2 BC2 24 GLY D 184  PHE D 185  ALA D 186  VAL D 199
SITE     3 BC2 24 GLY D 200  ASN D 201  ALA D 211  PHE D 214
SITE     4 BC2 24 CYS D 274  PHE D 391  LEU D 407  ARG D 411
SITE     5 BC2 24 SER D 414  TYR D 415  THR D 418  GLN D 419
SITE     6 BC2 24 H2S D 754  HOH D1295  HOH D1353  HOH D3252
SITE     1 BC3  3 CYS D 274  HDD D 760  HDE D 761
CRYST1   93.660  133.020  122.590  90.00 109.59  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      0.010677  0.000000  0.003800        0.00000
SCALE2      0.000000  0.007518  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008658        0.00000
      
PROCHECK
Go to PROCHECK summary
 References