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PDBsum entry 3n8z

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3n8z
Jmol
Contents
Protein chains
553 a.a.
Ligands
HEM ×2
NAG-NDG
NAG-NAG ×3
BOG ×5
FLP ×2
NAG-NAG-BMA-BMA-
MAN
Waters ×135
HEADER    OXIDOREDUCTASE                          28-MAY-10   3N8Z
TITLE     CRYSTAL STRUCTURE OF CYCLOOXYGENASE-1 IN COMPLEX WITH FLURBIPROFEN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CYCLOOXYGENASE-1, COX-1, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 1, PROSTAGLANDIN H2 SYNTHASE 1, PGH SYNTHASE 1, PGHS-1, PHS 1;
COMPND   6 EC: 1.14.99.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE   3 ORGANISM_COMMON: SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 STRAIN: SHEEP;
SOURCE   6 GENE: COX1, PTGS1;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-HTOCOX-1
KEYWDS    COX-1, CYCLOOXYGENASE, PEROXIDASE, PROSTAGLANDIN, HEME, FLURBIPROFEN,
KEYWDS   2 MEROHEDRAL TWINNED, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.SIDHU
REVDAT   2   01-SEP-10 3N8Z    1       JRNL
REVDAT   1   28-JUL-10 3N8Z    0
JRNL        AUTH   R.S.SIDHU,J.Y.LEE,C.YUAN,W.L.SMITH
JRNL        TITL   COMPARISON OF CYCLOOXYGENASE-1 CRYSTAL STRUCTURES:
JRNL        TITL 2 CROSS-TALK BETWEEN MONOMERS COMPRISING CYCLOOXYGENASE-1
JRNL        TITL 3 HOMODIMERS
JRNL        REF    BIOCHEMISTRY                  V.  49  7069 2010
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   20669977
JRNL        DOI    10.1021/BI1003298
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
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) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.63
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 41602
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) : 0.177
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : 0.207
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 1545
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) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2983
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.48
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610
REMARK   3   BIN FREE R VALUE SET COUNT          : 110
REMARK   3   BIN FREE R VALUE                    : 0.2910
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8889
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 388
REMARK   3   SOLVENT ATOMS            : 135
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.22
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -19.42000
REMARK   3    B22 (A**2) : -19.42000
REMARK   3    B33 (A**2) : 38.85000
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : -0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.062
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.272
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.570
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9618 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13129 ; 0.910 ; 2.018
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1110 ; 4.100 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   438 ;35.218 ;23.242
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1448 ;16.277 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;13.918 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1404 ; 0.058 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7369 ; 0.004 ; 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):  5545 ; 0.086 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8970 ; 0.162 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4073 ; 0.219 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4158 ; 0.389 ; 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
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   LOOSE POSITIONAL   1    A    (A):   4383 ;  0.34 ;  5.00
REMARK   3   LOOSE THERMAL      1    A (A**2):   4383 ;  0.47 ; 10.00
REMARK   3
REMARK   3  TWIN DETAILS
REMARK   3   NUMBER OF TWIN DOMAINS  : 2
REMARK   3      TWIN DOMAIN   : 1
REMARK   3      TWIN OPERATOR : H, K, L
REMARK   3      TWIN FRACTION : 0.502
REMARK   3      TWIN DOMAIN   : 2
REMARK   3      TWIN OPERATOR : H+K, -K, -L
REMARK   3      TWIN FRACTION : 0.498
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
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): -25.9370  57.8710   8.2960
REMARK   3    T TENSOR
REMARK   3      T11:   0.3693 T22:   0.2383
REMARK   3      T33:   0.0175 T12:   0.1931
REMARK   3      T13:  -0.0261 T23:  -0.0796
REMARK   3    L TENSOR
REMARK   3      L11:   1.3953 L22:   0.8068
REMARK   3      L33:   0.9359 L12:   0.3820
REMARK   3      L13:   0.0174 L23:   0.0239
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0245 S12:  -0.3516 S13:   0.1726
REMARK   3      S21:   0.1773 S22:  -0.0438 S23:   0.0135
REMARK   3      S31:  -0.1202 S32:  -0.1402 S33:   0.0683
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): -36.1413  52.2878 -30.2750
REMARK   3    T TENSOR
REMARK   3      T11:   0.3611 T22:   0.1443
REMARK   3      T33:   0.0126 T12:   0.1866
REMARK   3      T13:  -0.0517 T23:  -0.0024
REMARK   3    L TENSOR
REMARK   3      L11:   1.6848 L22:   0.7804
REMARK   3      L33:   1.3545 L12:   0.6528
REMARK   3      L13:   0.0257 L23:   0.0398
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0995 S12:   0.1609 S13:   0.1477
REMARK   3      S21:  -0.2170 S22:  -0.0086 S23:   0.0777
REMARK   3      S31:  -0.2241 S32:  -0.1193 S33:   0.1082
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
REMARK   4
REMARK   4 3N8Z COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059530.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 5ID-B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR225
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43176
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.630
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 9.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10500
REMARK 200   FOR THE DATA SET  : 6.2690
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1Q46
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, LITHIUM CHLORIDE,
REMARK 280  SODIUM AZIDE, N-OCTYL GLUCOSIDE, PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.10733
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.55367
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.83050
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       17.27683
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       86.38417
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 157    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 168    CG   CD   CE   NZ
REMARK 470     LYS A 169    CG   CD   CE   NZ
REMARK 470     GLU A 175    CG   CD   OE1  OE2
REMARK 470     ARG A 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 186    CG   CD   CE   NZ
REMARK 470     ARG A 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 317    CG   CD   CE   NZ
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     LYS A 485    CG   CD   CE   NZ
REMARK 470     MET A 487    CG   SD   CE
REMARK 470     LYS B 169    CG   CD   CE   NZ
REMARK 470     GLN B 170    CG   CD   OE1  NE2
REMARK 470     LYS B 186    CG   CD   CE   NZ
REMARK 470     GLU B 239    CG   CD   OE1  OE2
REMARK 470     LYS B 248    CG   CD   CE   NZ
REMARK 470     ARG B 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 453    CG   CD   CE   NZ
REMARK 470     ARG B 459    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 573    CG   CD   CE   NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     LYS B  222   CD   CE   NZ
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    THR A 129      -68.47   -104.74
REMARK 500    ASP A 135       41.80    -98.30
REMARK 500    ASN A 144       90.93    -69.37
REMARK 500    ARG A 185      -88.63    -82.60
REMARK 500    ASP A 249       17.26     57.62
REMARK 500    TRP A 387       56.10    -94.71
REMARK 500    PRO A 514      108.77    -39.42
REMARK 500    THR B 129      -80.52   -104.74
REMARK 500    ASP B 135       33.43    -93.54
REMARK 500    ASP B 158       33.49    -99.96
REMARK 500    ARG B 185      -65.44    -98.18
REMARK 500    PRO B 270       79.75    -67.41
REMARK 500    GLU B 347      -51.86   -134.51
REMARK 500    ASN B 439       37.45   -141.17
REMARK 500    TRP B 545       65.42    -67.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 588        DISTANCE =  5.01 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     BOG A  752
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                             HEM B 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 HEM B 601   NA   85.9
REMARK 620 3 HEM B 601   NB   70.1  89.4
REMARK 620 4 HEM B 601   NC   95.6 177.8  89.6
REMARK 620 5 HEM B 601   ND  109.4  90.1 179.3  91.0
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 HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 675
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1750
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1751
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLP B 1701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N8V   RELATED DB: PDB
REMARK 900 RELATED ID: 3N8W   RELATED DB: PDB
REMARK 900 RELATED ID: 3N8X   RELATED DB: PDB
REMARK 900 RELATED ID: 3N8Y   RELATED DB: PDB
DBREF  3N8Z A   32   584  UNP    P05979   PGH1_SHEEP      32    584
DBREF  3N8Z B   32   584  UNP    P05979   PGH1_SHEEP      32    584
SEQADV 3N8Z LEU A   92  UNP  P05979    MET    92 CONFLICT
SEQADV 3N8Z LEU B   92  UNP  P05979    MET    92 CONFLICT
SEQRES   1 A  553  PRO VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN
SEQRES   2 A  553  GLY ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS
SEQRES   3 A  553  ASP CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR
SEQRES   4 A  553  ILE PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG
SEQRES   5 A  553  PRO SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY
SEQRES   6 A  553  ARG TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG
SEQRES   7 A  553  ASP THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN
SEQRES   8 A  553  LEU ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP
SEQRES   9 A  553  TYR ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR
SEQRES  10 A  553  THR ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR
SEQRES  11 A  553  PRO MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA
SEQRES  12 A  553  GLU PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE
SEQRES  13 A  553  ILE PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE
SEQRES  14 A  553  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER
SEQRES  15 A  553  GLY LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS
SEQRES  16 A  553  GLY VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU
SEQRES  17 A  553  ARG GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  553  LYS TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER
SEQRES  19 A  553  VAL GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY
SEQRES  20 A  553  ILE PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL
SEQRES  21 A  553  PHE GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE
SEQRES  22 A  553  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP LEU LEU LYS
SEQRES  23 A  553  ALA GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  553  THR ALA ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  553  VAL ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE
SEQRES  26 A  553  LEU GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA
SEQRES  27 A  553  GLN PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN
SEQRES  28 A  553  GLN LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE
SEQRES  29 A  553  ARG VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU
SEQRES  30 A  553  PHE ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA
SEQRES  31 A  553  LEU VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE
SEQRES  32 A  553  GLY GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL
SEQRES  33 A  553  ALA VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU
SEQRES  34 A  553  GLN PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS
SEQRES  35 A  553  PRO TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  553  MET ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP
SEQRES  37 A  553  ALA LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS
SEQRES  38 A  553  HIS PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET
SEQRES  39 A  553  GLY ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO
SEQRES  40 A  553  ILE CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY
SEQRES  41 A  553  GLY GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU
SEQRES  42 A  553  LYS LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR
SEQRES  43 A  553  VAL SER PHE HIS VAL PRO ASP
SEQRES   1 B  553  PRO VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN
SEQRES   2 B  553  GLY ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS
SEQRES   3 B  553  ASP CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR
SEQRES   4 B  553  ILE PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG
SEQRES   5 B  553  PRO SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY
SEQRES   6 B  553  ARG TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG
SEQRES   7 B  553  ASP THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN
SEQRES   8 B  553  LEU ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP
SEQRES   9 B  553  TYR ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR
SEQRES  10 B  553  THR ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR
SEQRES  11 B  553  PRO MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA
SEQRES  12 B  553  GLU PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE
SEQRES  13 B  553  ILE PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE
SEQRES  14 B  553  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER
SEQRES  15 B  553  GLY LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS
SEQRES  16 B  553  GLY VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU
SEQRES  17 B  553  ARG GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 B  553  LYS TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER
SEQRES  19 B  553  VAL GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY
SEQRES  20 B  553  ILE PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL
SEQRES  21 B  553  PHE GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE
SEQRES  22 B  553  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP LEU LEU LYS
SEQRES  23 B  553  ALA GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 B  553  THR ALA ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 B  553  VAL ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE
SEQRES  26 B  553  LEU GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA
SEQRES  27 B  553  GLN PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN
SEQRES  28 B  553  GLN LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE
SEQRES  29 B  553  ARG VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU
SEQRES  30 B  553  PHE ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA
SEQRES  31 B  553  LEU VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE
SEQRES  32 B  553  GLY GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL
SEQRES  33 B  553  ALA VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU
SEQRES  34 B  553  GLN PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS
SEQRES  35 B  553  PRO TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU
SEQRES  36 B  553  MET ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP
SEQRES  37 B  553  ALA LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS
SEQRES  38 B  553  HIS PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET
SEQRES  39 B  553  GLY ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO
SEQRES  40 B  553  ILE CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY
SEQRES  41 B  553  GLY GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU
SEQRES  42 B  553  LYS LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR
SEQRES  43 B  553  VAL SER PHE HIS VAL PRO ASP
MODRES 3N8Z ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3N8Z ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3N8Z ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3N8Z ASN A   68  ASN  GLYCOSYLATION SITE
HET    HEM  A 601      43
HET    NAG  A 661      14
HET    NDG  A 662      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    NAG  A 681      14
HET    NAG  A 682      14
HET    BOG  A 750      20
HET    BOG  A 751      20
HET    BOG  A 752      13
HET    FLP  A 701      18
HET    HEM  B 601      43
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    BMA  B 673      11
HET    BMA  B 674      11
HET    MAN  B 675      11
HET    NAG  B 681      14
HET    NAG  B 682      14
HET    BOG  B1750      20
HET    BOG  B1751      20
HET    FLP  B1701      18
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     FLP FLURBIPROFEN
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETSYN     HEM HEME
FORMUL   3  HEM    2(C34 H32 FE N4 O4)
FORMUL   4  NAG    9(C8 H15 N O6)
FORMUL   4  NDG    C8 H15 N O6
FORMUL   7  BOG    5(C14 H28 O6)
FORMUL  10  FLP    2(C15 H13 F O2)
FORMUL  12  BMA    2(C6 H12 O6)
FORMUL  12  MAN    C6 H12 O6
FORMUL  17  HOH   *135(H2 O)
HELIX    1   1 ASN A   34  TYR A   39  5                                   6
HELIX    2   2 GLU A   73  THR A   81  1                                   9
HELIX    3   3 SER A   85  THR A   94  1                                  10
HELIX    4   4 GLY A   96  ALA A  105  1                                  10
HELIX    5   5 PHE A  107  ASN A  122  1                                  16
HELIX    6   6 SER A  138  ASN A  144  1                                   7
HELIX    7   7 ASP A  173  LEU A  182  1                                  10
HELIX    8   8 ASN A  195  HIS A  207  1                                  13
HELIX    9   9 ASN A  237  ARG A  245  1                                   9
HELIX   10  10 GLY A  297  HIS A  320  1                                  24
HELIX   11  11 GLY A  324  GLU A  347  1                                  24
HELIX   12  12 GLU A  347  GLY A  354  1                                   8
HELIX   13  13 ASP A  362  PHE A  367  5                                   6
HELIX   14  14 ALA A  378  TYR A  385  1                                   8
HELIX   15  15 TRP A  387  MET A  391  5                                   5
HELIX   16  16 SER A  403  LEU A  408  1                                   6
HELIX   17  17 SER A  412  GLY A  418  1                                   7
HELIX   18  18 GLY A  418  SER A  427  1                                  10
HELIX   19  19 ASP A  441  HIS A  443  5                                   3
HELIX   20  20 ILE A  444  ARG A  459  1                                  16
HELIX   21  21 PRO A  462  PHE A  470  1                                   9
HELIX   22  22 SER A  477  GLY A  483  1                                   7
HELIX   23  23 LYS A  485  GLY A  496  1                                  12
HELIX   24  24 ASP A  497  LEU A  501  5                                   5
HELIX   25  25 GLU A  502  GLU A  510  1                                   9
HELIX   26  26 GLY A  519  ASN A  537  1                                  19
HELIX   27  27 PRO A  538  SER A  541  5                                   4
HELIX   28  28 LYS A  546  PHE A  550  5                                   5
HELIX   29  29 GLY A  551  THR A  561  1                                  11
HELIX   30  30 THR A  563  LEU A  570  1                                   8
HELIX   31  31 ASN B   34  TYR B   39  5                                   6
HELIX   32  32 GLU B   73  ARG B   83  1                                  11
HELIX   33  33 SER B   85  THR B   94  1                                  10
HELIX   34  34 GLY B   96  THR B  106  1                                  11
HELIX   35  35 PHE B  107  ASN B  122  1                                  16
HELIX   36  36 SER B  138  ASN B  144  1                                   7
HELIX   37  37 ASP B  173  LEU B  182  1                                  10
HELIX   38  38 ASN B  195  HIS B  207  1                                  13
HELIX   39  39 ASN B  237  ARG B  245  1                                   9
HELIX   40  40 PRO B  280  GLN B  284  5                                   5
HELIX   41  41 GLN B  289  LEU B  294  5                                   6
HELIX   42  42 LEU B  295  HIS B  320  1                                  26
HELIX   43  43 GLY B  324  GLU B  347  1                                  24
HELIX   44  44 GLU B  347  GLY B  354  1                                   8
HELIX   45  45 ASP B  362  PHE B  367  5                                   6
HELIX   46  46 ALA B  378  TYR B  385  1                                   8
HELIX   47  47 HIS B  386  MET B  391  5                                   6
HELIX   48  48 SER B  403  LEU B  408  1                                   6
HELIX   49  49 SER B  412  GLY B  418  1                                   7
HELIX   50  50 GLY B  418  SER B  427  1                                  10
HELIX   51  51 ASP B  441  HIS B  443  5                                   3
HELIX   52  52 ILE B  444  LEU B  458  1                                  15
HELIX   53  53 PRO B  462  PHE B  470  1                                   9
HELIX   54  54 SER B  477  GLY B  483  1                                   7
HELIX   55  55 LYS B  485  GLY B  496  1                                  12
HELIX   56  56 ASP B  497  LEU B  501  5                                   5
HELIX   57  57 GLU B  502  GLU B  510  1                                   9
HELIX   58  58 GLY B  519  GLY B  536  1                                  18
HELIX   59  59 ASN B  537  SER B  541  5                                   5
HELIX   60  60 ALA B  547  GLY B  551  5                                   5
HELIX   61  61 GLY B  552  THR B  561  1                                  10
HELIX   62  62 THR B  563  LEU B  570  1                                   8
SHEET    1   A 2 ILE A  46  PHE A  50  0
SHEET    2   A 2 ARG A  54  ASP A  58 -1  O  GLN A  56   N  VAL A  48
SHEET    1   B 2 TYR A  64  SER A  65  0
SHEET    2   B 2 ILE A  71  PRO A  72 -1  O  ILE A  71   N  SER A  65
SHEET    1   C 2 TYR A 130  ASN A 131  0
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130
SHEET    1   D 2 GLN A 255  LEU A 257  0
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   E 2 PHE A 395  VAL A 397  0
SHEET    2   E 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   F 2 ILE B  46  PHE B  50  0
SHEET    2   F 2 ARG B  54  ASP B  58 -1  O  GLN B  56   N  VAL B  48
SHEET    1   G 2 TYR B  64  SER B  65  0
SHEET    2   G 2 ILE B  71  PRO B  72 -1  O  ILE B  71   N  SER B  65
SHEET    1   H 2 GLN B 255  LEU B 257  0
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   I 2 PHE B 395  VAL B 397  0
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.03
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44
LINK         O4  NAG B 681                 C1  NAG B 682     1555   1555  1.44
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45
LINK         O4  NAG A 681                 C1  NAG A 682     1555   1555  1.45
LINK         O4  NAG A 661                 C1  NDG A 662     1555   1555  1.45
LINK         NE2 HIS B 388                FE   HEM B 601     1555   1555  2.78
LINK         O4  BMA B 674                 C1  MAN B 675     1555   1555  1.44
LINK         O4  BMA B 673                 C1  BMA B 674     1555   1555  1.45
LINK         O4  NAG B 672                 C1  BMA B 673     1555   1555  1.45
CISPEP   1 SER A  126    PRO A  127          0         2.81
CISPEP   2 SER B  126    PRO B  127          0        -1.10
SITE     1 AC1 15 HOH A  20  ALA A 199  ALA A 202  GLN A 203
SITE     2 AC1 15 THR A 206  PHE A 210  LYS A 211  THR A 212
SITE     3 AC1 15 LEU A 295  HIS A 386  HIS A 388  MET A 391
SITE     4 AC1 15 ILE A 444  HIS A 446  VAL A 447
SITE     1 AC2  5 PRO A  40  TYR A  55  ASN A  68  HOH A 631
SITE     2 AC2  5 NDG A 662
SITE     1 AC3  3 HOH A 605  HOH A 631  NAG A 661
SITE     1 AC4  5 ASN A 144  TYR A 147  HOH A 623  NAG A 672
SITE     2 AC4  5 HOH B 591
SITE     1 AC5  1 NAG A 671
SITE     1 AC6  9 TYR A 402  ASN A 410  MET A 413  ASP A 416
SITE     2 AC6  9 HOH A 597  NAG A 682  PRO B 280  GLN B 282
SITE     3 AC6  9 SER B 283
SITE     1 AC7  5 GLN A 400  GLN A 406  ASP A 416  HOH A 595
SITE     2 AC7  5 NAG A 681
SITE     1 AC8  6 THR A  81  LEU A  82  PRO A  84  PHE A  88
SITE     2 AC8  6 HOH A 598  HOH A 644
SITE     1 AC9  5 ARG A  83  ILE A  89  VAL A 119  ARG A 120
SITE     2 AC9  5 GLU A 524
SITE     1 BC1  3 SER A  85  SER A  87  PHE A  91
SITE     1 BC2 11 VAL A 116  ARG A 120  VAL A 349  LEU A 352
SITE     2 BC2 11 TYR A 355  TYR A 385  TRP A 387  GLY A 526
SITE     3 BC2 11 ALA A 527  SER A 530  LEU A 531
SITE     1 BC3 13 ALA B 202  GLN B 203  HIS B 207  PHE B 210
SITE     2 BC3 13 THR B 212  LEU B 295  ASN B 382  HIS B 386
SITE     3 BC3 13 TRP B 387  HIS B 388  MET B 391  VAL B 447
SITE     4 BC3 13 HOH B 613
SITE     1 BC4  5 GLU B 140  ASN B 144  TYR B 147  PHE B 220
SITE     2 BC4  5 NAG B 672
SITE     1 BC5  4 MET B 216  HOH B 610  NAG B 671  BMA B 673
SITE     1 BC6  3 HOH B 610  NAG B 672  BMA B 674
SITE     1 BC7  3 GLN A 243  BMA B 673  MAN B 675
SITE     1 BC8  2 GLN A 243  BMA B 674
SITE     1 BC9  9 PRO A 281  TYR B 402  GLN B 406  ASN B 410
SITE     2 BC9  9 SER B 412  MET B 413  ASP B 416  TYR B 417
SITE     3 BC9  9 NAG B 682
SITE     1 CC1  4 HOH B  13  ASP B 416  HOH B 588  NAG B 681
SITE     1 CC2  4 SER B  85  SER B  87  PHE B  88  PHE B  91
SITE     1 CC3  6 ARG B  83  PRO B  86  ILE B  89  VAL B 119
SITE     2 CC3  6 ARG B 120  GLU B 524
SITE     1 CC4 10 ARG B 120  VAL B 349  LEU B 352  TYR B 355
SITE     2 CC4 10 TYR B 385  TRP B 387  ILE B 523  GLY B 526
SITE     3 CC4 10 ALA B 527  SER B 530
CRYST1  181.490  181.490  103.661  90.00  90.00 120.00 P 65         12
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      0.005510  0.003181  0.000000        0.00000
SCALE2      0.000000  0.006362  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009647        0.00000
      
PROCHECK
Go to PROCHECK summary
 References