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PDBsum entry 3n8w

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3n8w
Jmol
Contents
Protein chains
553 a.a.
Ligands
HEM ×2
FLP
NAG-NDG ×2
NAG-NAG-BMA
NAG-NDG-BMA-MAN-
MAN
BOG ×3
NDG-NAG-MAN
NAG-NDG-BMA
Waters ×213
HEADER    OXIDOREDUCTASE                          28-MAY-10   3N8W
TITLE     CRYSTAL STRUCTURE OF R120Q/NATIVE CYCLOOXYGENASE-1 HETERODIMER MUTANT
TITLE    2 IN COMPLEX WITH FLURBIPROFEN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CHAIN B;
COMPND   5 SYNONYM: CYCLOOXYGENASE-1, COX-1, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   6 1, PROSTAGLANDIN H2 SYNTHASE 1, PGH SYNTHASE 1, PGHS-1, PHS 1;
COMPND   7 EC: 1.14.99.1;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES;
COMPND  10 MOL_ID: 2;
COMPND  11 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1;
COMPND  12 CHAIN: B;
COMPND  13 SYNONYM: CYCLOOXYGENASE-1, COX-1, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND  14 1, PROSTAGLANDIN H2 SYNTHASE 1, PGH SYNTHASE 1, PGHS-1, PHS 1;
COMPND  15 EC: 1.14.99.1;
COMPND  16 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;
SOURCE  12 MOL_ID: 2;
SOURCE  13 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE  14 ORGANISM_COMMON: SHEEP;
SOURCE  15 ORGANISM_TAXID: 9940;
SOURCE  16 GENE: PTGS1, COX1;
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-HTOCOX-1
KEYWDS    COX-1, CYCLOOXYGENASE, PEROXIDASE, PROSTAGLANDIN, HEME, FLURBIPROFEN,
KEYWDS   2 MEROHEDRAL TWINNED, HETERODIMER MUTANT, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.SIDHU
REVDAT   2   01-SEP-10 3N8W    1       JRNL
REVDAT   1   28-JUL-10 3N8W    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.    2.75 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) : 2.75
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.91
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0
REMARK   3   NUMBER OF REFLECTIONS             : 48759
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) : 0.179
REMARK   3   R VALUE            (WORKING SET) : 0.178
REMARK   3   FREE R VALUE                     : 0.201
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.400
REMARK   3   FREE R VALUE TEST SET COUNT      : 1705
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) : 2.75
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3165
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.36
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440
REMARK   3   BIN FREE R VALUE SET COUNT          : 97
REMARK   3   BIN FREE R VALUE                    : 0.2990
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8850
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 383
REMARK   3   SOLVENT ATOMS            : 213
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.78
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -4.23000
REMARK   3    B22 (A**2) : -4.23000
REMARK   3    B33 (A**2) : 8.47000
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): 0.053
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.241
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.211
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9617 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13144 ; 1.131 ; 2.020
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1113 ; 4.693 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   430 ;36.358 ;23.326
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1436 ;16.880 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;16.564 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1425 ; 0.071 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7362 ; 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):  5567 ; 0.153 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9000 ; 0.307 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4050 ; 0.704 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4143 ; 1.309 ; 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   MEDIUM POSITIONAL  1    A    (A):   4324 ;  0.25 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   4324 ;  0.15 ;  2.00
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 : 0.532
REMARK   3      TWIN DOMAIN   : 2
REMARK   3      TWIN OPERATOR : -H-K, K, -L
REMARK   3      TWIN FRACTION : 0.468
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):  36.2730 -52.1969   3.0999
REMARK   3    T TENSOR
REMARK   3      T11:   0.2550 T22:   0.0790
REMARK   3      T33:   0.1055 T12:   0.1257
REMARK   3      T13:  -0.0089 T23:  -0.0193
REMARK   3    L TENSOR
REMARK   3      L11:   1.5886 L22:   0.6676
REMARK   3      L33:   1.4894 L12:   0.5739
REMARK   3      L13:  -0.2616 L23:  -0.0851
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1183 S12:   0.1683 S13:  -0.0314
REMARK   3      S21:  -0.2129 S22:   0.0272 S23:  -0.0347
REMARK   3      S31:   0.0897 S32:   0.0297 S33:   0.0911
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):  25.6489 -58.1763  41.4865
REMARK   3    T TENSOR
REMARK   3      T11:   0.2553 T22:   0.1720
REMARK   3      T33:   0.1081 T12:   0.1596
REMARK   3      T13:  -0.0181 T23:   0.0368
REMARK   3    L TENSOR
REMARK   3      L11:   1.5311 L22:   0.7924
REMARK   3      L33:   1.2134 L12:   0.7135
REMARK   3      L13:   0.0125 L23:  -0.0809
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0024 S12:  -0.3450 S13:  -0.0599
REMARK   3      S21:   0.1768 S22:  -0.0381 S23:   0.0261
REMARK   3      S31:  -0.0215 S32:   0.0467 S33:   0.0404
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 3N8W 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 RCSB059527.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-08
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                       : 21-ID-F
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872
REMARK 200  MONOCHROMATOR                  : C(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50497
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.910
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 7.200
REMARK 200  R MERGE                    (I) : 0.07500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 24.3330
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.82
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.4
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 1Q4G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89
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       68.73000
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       34.36500
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       51.54750
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       17.18250
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       85.91250
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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  83    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     GLN A 170    CG   CD   OE1  NE2
REMARK 470     LYS A 186    CG   CD   CE   NZ
REMARK 470     GLU A 239    CG   CD   OE1  OE2
REMARK 470     LYS A 248    CG   CD   CE   NZ
REMARK 470     ARG A 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A 294    CG   CD1  CD2
REMARK 470     LYS A 485    CG   CD   CE   NZ
REMARK 470     GLU A 486    CG   CD   OE1  OE2
REMARK 470     GLU A 490    CG   CD   OE1  OE2
REMARK 470     LYS A 573    CG   CD   CE   NZ
REMARK 470     ARG B  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 168    CG   CD   CE   NZ
REMARK 470     LYS B 169    CG   CD   CE   NZ
REMARK 470     GLN B 170    CG   CD   OE1  NE2
REMARK 470     GLU B 175    CG   CD   OE1  OE2
REMARK 470     PHE B 176    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ARG B 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 180    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 186    CG   CD   CE   NZ
REMARK 470     LYS B 215    CG   CD   CE   NZ
REMARK 470     ARG B 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 438    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 485    CG   CD   CE   NZ
REMARK 470     GLU B 486    CG   CD   OE1  OE2
REMARK 470     MET B 487    CG   SD   CE
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   ND2  ASN A   410     O5   NAG A   681              1.55
REMARK 500   ND2  ASN B   410     N2   NDG B  1681              1.96
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    THR A  60      121.72    -38.96
REMARK 500    ARG A  61       18.71     55.41
REMARK 500    THR A 129      -81.64    -95.21
REMARK 500    ASP A 135       36.32    -95.51
REMARK 500    ARG A 185      -90.06   -108.73
REMARK 500    ASN A 258        9.07     59.45
REMARK 500    PRO A 270       91.78    -63.93
REMARK 500    GLN A 358       96.32    -69.10
REMARK 500    TRP A 387       45.99    -94.91
REMARK 500    ASN A 439       26.48   -144.23
REMARK 500    GLN B  44       22.61     81.02
REMARK 500    SER B 126      113.43   -174.26
REMARK 500    THR B 129      -77.94   -112.43
REMARK 500    ASP B 135       43.71    -98.52
REMARK 500    ASP B 158       55.24    -94.77
REMARK 500    ARG B 185      -84.69    -99.24
REMARK 500    HIS B 204      -76.02    -54.20
REMARK 500    ASP B 249       15.10     52.53
REMARK 500    TRP B 387       40.30    -98.95
REMARK 500    PHE B 409       -6.22     65.66
REMARK 500    GLU B 486      -72.35    -63.01
REMARK 500
REMARK 500 REMARK: NULL
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 B 1750
REMARK 610     BOG B 1751
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 HOH B 607   O
REMARK 620 2 HEM B 601   NA   92.2
REMARK 620 3 HEM B 601   NB   99.3  89.6
REMARK 620 4 HEM B 601   NC   86.6 178.6  91.2
REMARK 620 5 HEM B 601   ND   82.9  89.3 177.6  90.0
REMARK 620 6 HIS B 388   NE2 174.3  87.5  86.4  93.7  91.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 801  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 594   O
REMARK 620 2 HEM A 801   NA   79.9
REMARK 620 3 HEM A 801   NB  103.5  88.9
REMARK 620 4 HEM A 801   NC   97.9 177.8  91.6
REMARK 620 5 HEM A 801   ND   78.1  90.5 178.1  89.1
REMARK 620 6 HIS A 388   NE2 165.1  91.5  88.5  90.6  89.8
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 683
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 675
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 1662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 1681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1682
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1683
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 1672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1750
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1751
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N8V   RELATED DB: PDB
REMARK 900 RELATED ID: 3N8X   RELATED DB: PDB
REMARK 900 RELATED ID: 3N8Y   RELATED DB: PDB
REMARK 900 RELATED ID: 3N8Z   RELATED DB: PDB
DBREF  3N8W A   32   584  UNP    P05979   PGH1_SHEEP      32    584
DBREF  3N8W B   32   584  UNP    P05979   PGH1_SHEEP      32    584
SEQADV 3N8W LEU A   92  UNP  P05979    MET    92 CONFLICT
SEQADV 3N8W LEU B   92  UNP  P05979    MET    92 CONFLICT
SEQADV 3N8W GLN B  120  UNP  P05979    ARG   120 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 GLN 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 3N8W ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 3N8W ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3N8W ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3N8W ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3N8W ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3N8W ASN A   68  ASN  GLYCOSYLATION SITE
HET    HEM  A 801      43
HET    FLP  A 701      18
HET    NAG  A 661      14
HET    NDG  A 662      14
HET    NAG  A 681      14
HET    NAG  A 682      14
HET    BMA  A 683      11
HET    NAG  A 671      14
HET    NDG  A 672      14
HET    BMA  A 673      11
HET    MAN  A 674      11
HET    MAN  A 675      11
HET    BOG  A 751      20
HET    HEM  B 601      43
HET    NAG  B1661      14
HET    NDG  B1662      14
HET    NDG  B1681      14
HET    NAG  B1682      14
HET    MAN  B1683      11
HET    NAG  B1671      14
HET    NDG  B1672      14
HET    BMA  B1673      11
HET    BOG  B1750      13
HET    BOG  B1751      12
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     FLP FLURBIPROFEN
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETSYN     HEM HEME
FORMUL   3  HEM    2(C34 H32 FE N4 O4)
FORMUL   4  FLP    C15 H13 F O2
FORMUL   5  NAG    7(C8 H15 N O6)
FORMUL   5  NDG    5(C8 H15 N O6)
FORMUL   6  BMA    3(C6 H12 O6)
FORMUL   7  MAN    3(C6 H12 O6)
FORMUL   8  BOG    3(C14 H28 O6)
FORMUL  15  HOH   *213(H2 O)
HELIX    1   1 ASN A   34  TYR A   39  5                                   6
HELIX    2   2 GLU A   73  ARG A   83  1                                  11
HELIX    3   3 SER A   85  HIS A   95  1                                  11
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 VAL A  291  LEU A  294  5                                   4
HELIX   11  11 LEU A  295  HIS A  320  1                                  26
HELIX   12  12 GLY A  324  GLU A  347  1                                  24
HELIX   13  13 GLU A  347  GLY A  354  1                                   8
HELIX   14  14 ASP A  362  PHE A  367  5                                   6
HELIX   15  15 ALA A  378  TYR A  385  1                                   8
HELIX   16  16 HIS A  386  MET A  391  5                                   6
HELIX   17  17 SER A  403  LEU A  408  1                                   6
HELIX   18  18 SER A  412  GLY A  418  1                                   7
HELIX   19  19 GLY A  418  GLN A  429  1                                  12
HELIX   20  20 ASP A  441  HIS A  443  5                                   3
HELIX   21  21 ILE A  444  LEU A  458  1                                  15
HELIX   22  22 PRO A  462  PHE A  470  1                                   9
HELIX   23  23 SER A  477  GLY A  483  1                                   7
HELIX   24  24 LYS A  485  GLY A  496  1                                  12
HELIX   25  25 ASP A  497  LEU A  501  5                                   5
HELIX   26  26 GLU A  502  GLU A  510  1                                   9
HELIX   27  27 GLY A  519  GLY A  536  1                                  18
HELIX   28  28 ASN A  537  SER A  541  5                                   5
HELIX   29  29 LYS A  546  GLY A  551  5                                   6
HELIX   30  30 GLY A  552  THR A  561  1                                  10
HELIX   31  31 THR A  563  LEU A  570  1                                   8
HELIX   32  32 ASN B   34  TYR B   39  5                                   6
HELIX   33  33 GLU B   73  ARG B   83  1                                  11
HELIX   34  34 SER B   85  HIS B   95  1                                  11
HELIX   35  35 GLY B   96  ALA B  105  1                                  10
HELIX   36  36 PHE B  107  ASN B  122  1                                  16
HELIX   37  37 SER B  138  ASN B  144  1                                   7
HELIX   38  38 ASP B  173  LEU B  182  1                                  10
HELIX   39  39 ASN B  195  HIS B  207  1                                  13
HELIX   40  40 ASN B  237  ARG B  245  1                                   9
HELIX   41  41 PRO B  280  GLN B  284  5                                   5
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  ALA B  369  5                                   8
HELIX   46  46 ALA B  378  TYR B  385  1                                   8
HELIX   47  47 TRP B  387  MET B  391  5                                   5
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  GLN B  429  1                                  12
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 GLN A 255  LEU A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   D 2 PHE A 395  VAL A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   E 2 ILE B  46  PHE B  50  0
SHEET    2   E 2 ARG B  54  ASP B  58 -1  O  GLN B  56   N  VAL B  48
SHEET    1   F 2 TYR B  64  SER B  65  0
SHEET    2   F 2 ILE B  71  PRO B  72 -1  O  ILE B  71   N  SER B  65
SHEET    1   G 2 TYR B 130  ASN B 131  0
SHEET    2   G 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130
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  2.04
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.01
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.00
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.03
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.04
LINK         ND2 ASN B 410                 C2  NDG B1681     1555   1555  1.30
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.36
LINK         ND2 ASN B 410                 C1  NDG B1681     1555   1555  1.44
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B1671     1555   1555  1.44
LINK         ND2 ASN B  68                 C1  NAG B1661     1555   1555  1.44
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         O4  NDG B1681                 C1  NAG B1682     1555   1555  1.45
LINK         O4  NAG B1682                 C1  MAN B1683     1555   1555  1.45
LINK         O6  MAN A 674                 C1  MAN A 675     1555   1555  1.45
LINK         O4  NAG A 681                 C1  NAG A 682     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NDG A 672     1555   1555  1.45
LINK         O4  NAG B1661                 C1  NDG B1662     1555   1555  1.45
LINK         O4  NAG A 661                 C1  NDG A 662     1555   1555  1.46
LINK         O4  NAG B1671                 C1  NDG B1672     1555   1555  1.46
LINK        FE   HEM B 601                 O   HOH B 607     1555   1555  2.09
LINK        FE   HEM A 801                 O   HOH A 594     1555   1555  2.17
LINK         NE2 HIS B 388                FE   HEM B 601     1555   1555  2.23
LINK         NE2 HIS A 388                FE   HEM A 801     1555   1555  2.34
LINK         O6  BMA A 673                 C1  MAN A 674     1555   1555  1.45
LINK         O4  NAG A 682                 C1  BMA A 683     1555   1555  1.45
LINK         O4  NDG A 672                 C1  BMA A 673     1555   1555  1.46
LINK         O4  NDG B1672                 C1  BMA B1673     1555   1555  1.46
CISPEP   1 SER A  126    PRO A  127          0         3.71
CISPEP   2 SER B  126    PRO B  127          0         1.76
SITE     1 AC1 15 ALA A 199  ALA A 202  GLN A 203  HIS A 207
SITE     2 AC1 15 PHE A 210  LYS A 211  THR A 212  LEU A 295
SITE     3 AC1 15 ASN A 382  TYR A 385  HIS A 386  HIS A 388
SITE     4 AC1 15 MET A 391  ASP A 450  HOH A 594
SITE     1 AC2  9 ARG A 120  VAL A 349  LEU A 352  TYR A 355
SITE     2 AC2  9 TYR A 385  TRP A 387  GLY A 526  ALA A 527
SITE     3 AC2  9 SER A 530
SITE     1 AC3  4 TYR A  55  PRO A  67  ASN A  68  NDG A 662
SITE     1 AC4  2 NAG A 661  HOH A 668
SITE     1 AC5  9 TYR A 402  GLN A 406  ASN A 410  SER A 412
SITE     2 AC5  9 MET A 413  ASP A 416  NAG A 682  ILE B 279
SITE     3 AC5  9 PRO B 281
SITE     1 AC6  7 TYR A 402  GLN A 406  ASP A 416  NAG A 681
SITE     2 AC6  7 BMA A 683  GLN B 282  HOH B 639
SITE     1 AC7  4 GLN A 400  HOH A 586  HOH A 632  NAG A 682
SITE     1 AC8  5 GLU A 140  ASN A 144  TYR A 147  NDG A 672
SITE     2 AC8  5 HOH B 600
SITE     1 AC9  3 MET A 216  NAG A 671  BMA A 673
SITE     1 BC1  2 NDG A 672  MAN A 674
SITE     1 BC2  3 BMA A 673  MAN A 675  GLN B 243
SITE     1 BC3  3 MAN A 674  GLN B 243  PRO B 270
SITE     1 BC4  6 PRO A  86  ILE A  89  VAL A 119  ARG A 120
SITE     2 BC4  6 LEU A 123  GLU A 524
SITE     1 BC5 14 ALA B 199  ALA B 202  GLN B 203  THR B 206
SITE     2 BC5 14 HIS B 207  PHE B 210  THR B 212  ASN B 382
SITE     3 BC5 14 TYR B 385  HIS B 386  HIS B 388  MET B 391
SITE     4 BC5 14 VAL B 447  HOH B 607
SITE     1 BC6  4 TYR B  55  ASN B  68  HOH B 677  NDG B1662
SITE     1 BC7  1 NAG B1661
SITE     1 BC8 10 PRO A 280  GLN A 282  TYR B 402  GLN B 406
SITE     2 BC8 10 ASN B 410  SER B 412  MET B 413  ASP B 416
SITE     3 BC8 10 TYR B 417  NAG B1682
SITE     1 BC9  6 GLN B 400  GLN B 406  ASP B 416  HOH B 664
SITE     2 BC9  6 NDG B1681  MAN B1683
SITE     1 CC1  1 NAG B1682
SITE     1 CC2  6 GLU B 140  ASN B 144  TYR B 147  HOH B 598
SITE     2 CC2  6 HOH B 621  NDG B1672
SITE     1 CC3  4 LEU A 238  MET B 216  NAG B1671  BMA B1673
SITE     1 CC4  1 NDG B1672
SITE     1 CC5  2 SER B  87  PHE B  88
SITE     1 CC6  8 HOH B  14  ARG B  83  PRO B  86  ILE B  89
SITE     2 CC6  8 VAL B 119  GLN B 120  LEU B 123  GLU B 524
CRYST1  182.483  182.483  103.095  90.00  90.00 120.00 P 65          6
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      0.005480  0.003164  0.000000        0.00000
SCALE2      0.000000  0.006328  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009700        0.00000
      
PROCHECK
Go to PROCHECK summary
 References