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PDBsum entry 3kk6

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3kk6
Jmol
Contents
Protein chains
553 a.a.
Ligands
HEM ×2
NAG-NAG-MAN-BMA-
MAN
NAG-NDG ×3
CEL ×2
BOG ×4
FLC
NAG-NAG-MAN-BMA
Waters ×105
HEADER    OXIDOREDUCTASE                          04-NOV-09   3KK6
TITLE     CRYSTAL STRUCTURE OF CYCLOOXYGENASE-1 IN COMPLEX WITH CELECOXIB
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: DOMESTIC SHEEP,LAMBS,WILD SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 GENE: COX1, PTGS1;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
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, CELECOXIB,
KEYWDS   2 MEROHEDRAL TWINNED, DIOXYGENASE, DISULFIDE BOND, EGF-LIKE DOMAIN,
KEYWDS   3 ENDOPLASMIC RETICULUM, FATTY ACID BIOSYNTHESIS, GLYCOPROTEIN, IRON,
KEYWDS   4 LIPID SYNTHESIS, MEMBRANE, METAL-BINDING, MICROSOME, OXIDOREDUCTASE,
KEYWDS   5 PROSTAGLANDIN BIOSYNTHESIS, TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.SIDHU
REVDAT   7   13-MAR-13 3KK6    1       REMARK
REVDAT   6   13-JUL-11 3KK6    1       VERSN
REVDAT   5   02-MAR-10 3KK6    1       MTRIX1 MTRIX2 MTRIX3
REVDAT   4   09-FEB-10 3KK6    1       JRNL
REVDAT   3   29-DEC-09 3KK6    1       MTRIX1 MTRIX2 MTRIX3
REVDAT   2   22-DEC-09 3KK6    1       CAVEAT
REVDAT   1   15-DEC-09 3KK6    0
JRNL        AUTH   G.RIMON,R.S.SIDHU,D.A.LAUVER,J.Y.LEE,N.P.SHARMA,C.YUAN,
JRNL        AUTH 2 R.A.FRIELER,R.C.TRIEVEL,B.R.LUCCHESI,W.L.SMITH
JRNL        TITL   COXIBS INTERFERE WITH THE ACTION OF ASPIRIN BY BINDING
JRNL        TITL 2 TIGHTLY TO ONE MONOMER OF CYCLOOXYGENASE-1.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107    28 2010
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   19955429
JRNL        DOI    10.1073/PNAS.0909765106
REMARK   2
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.41
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.140
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4
REMARK   3   NUMBER OF REFLECTIONS             : 48593
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208
REMARK   3   R VALUE            (WORKING SET) : 0.207
REMARK   3   FREE R VALUE                     : 0.242
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1992
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 41.4200 -  7.4510    0.98     2453   103  0.1977 0.2478
REMARK   3     2  7.4510 -  5.9196    0.98     2421   103  0.2157 0.2703
REMARK   3     3  5.9196 -  5.1729    0.98     2399   103  0.1894 0.1792
REMARK   3     4  5.1729 -  4.7007    0.98     2402    99  0.1550 0.2212
REMARK   3     5  4.7007 -  4.3642    0.98     2411   103  0.1594 0.1652
REMARK   3     6  4.3642 -  4.1071    0.98     2375    99  0.1576 0.2068
REMARK   3     7  4.1071 -  3.9016    0.98     2385   101  0.1791 0.2150
REMARK   3     8  3.9016 -  3.7319    0.98     2379    97  0.1943 0.1975
REMARK   3     9  3.7319 -  3.5883    0.98     2371   101  0.1962 0.2903
REMARK   3    10  3.5883 -  3.4645    0.98     2378    99  0.2165 0.2400
REMARK   3    11  3.4645 -  3.3562    0.98     2349    99  0.2360 0.2875
REMARK   3    12  3.3562 -  3.2603    0.98     2371    96  0.2480 0.2341
REMARK   3    13  3.2603 -  3.1745    0.98     2336   101  0.2580 0.2561
REMARK   3    14  3.1745 -  3.0971    0.98     2323    95  0.2545 0.2693
REMARK   3    15  3.0971 -  3.0267    0.98     2319    97  0.2597 0.2834
REMARK   3    16  3.0267 -  2.9623    0.98     2324    97  0.2743 0.3070
REMARK   3    17  2.9623 -  2.9031    0.98     2300   101  0.2748 0.3278
REMARK   3    18  2.9031 -  2.8483    0.98     2231    91  0.2804 0.4040
REMARK   3    19  2.8483 -  2.7975    0.98     2154    93  0.2869 0.3220
REMARK   3    20  2.7975 -  2.7500    0.98     1953    81  0.3050 0.3790
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.30
REMARK   3   B_SOL              : 52.41
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.430
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.52
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -13.52800
REMARK   3    B22 (A**2) : -13.52800
REMARK   3    B33 (A**2) : -13.13000
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  TWINNING INFORMATION.
REMARK   3   FRACTION: 0.5010
REMARK   3   OPERATOR: H,-H-K,-L
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.009          18307
REMARK   3   ANGLE     :  1.013          32834
REMARK   3   CHIRALITY :  0.092           1414
REMARK   3   PLANARITY :  0.007           2764
REMARK   3   DIHEDRAL  : 18.604           4574
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (CHAIN A AND (RESID 32:584 OR RESID 601:900 ) )
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0177  52.0151  -1.2038
REMARK   3    T TENSOR
REMARK   3      T11:   0.4133 T22:   0.2565
REMARK   3      T33:   0.2780 T12:   0.2410
REMARK   3      T13:  -0.0689 T23:  -0.0325
REMARK   3    L TENSOR
REMARK   3      L11:   0.1627 L22:   0.1579
REMARK   3      L33:   0.4631 L12:   0.1784
REMARK   3      L13:   0.0370 L23:   0.1191
REMARK   3    S TENSOR
REMARK   3      S11:   0.0101 S12:   0.0385 S13:  -0.1231
REMARK   3      S21:  -0.1581 S22:  -0.0741 S23:   0.0431
REMARK   3      S31:  -0.2704 S32:  -0.0970 S33:   0.0000
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (CHAIN B AND (RESID 32:584 OR RESID 601:1752 ) )
REMARK   3    ORIGIN FOR THE GROUP (A): -25.8399  57.3222  36.8645
REMARK   3    T TENSOR
REMARK   3      T11:   0.3871 T22:   0.2278
REMARK   3      T33:   0.2394 T12:   0.2200
REMARK   3      T13:  -0.0652 T23:  -0.0573
REMARK   3    L TENSOR
REMARK   3      L11:   0.3230 L22:   0.0898
REMARK   3      L33:   0.1611 L12:   0.0845
REMARK   3      L13:   0.0718 L23:   0.0370
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0782 S12:  -0.1017 S13:   0.0670
REMARK   3      S21:   0.1530 S22:   0.0906 S23:  -0.1688
REMARK   3      S31:  -0.0860 S32:  -0.1039 S33:   0.0278
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : 1
REMARK   3   NCS GROUP : 1
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain A and (resseq 32:278 or resseq 282:
REMARK   3                          584 ) and (not element H)
REMARK   3     SELECTION          : chain B and (resseq 32:278 or resseq 282:
REMARK   3                          584 ) and (not element H)
REMARK   3     ATOM PAIRS NUMBER  : 4207
REMARK   3     RMSD               : 0.238
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: USED TWIN OPERATOR (H,-H-K,-L)
REMARK   4
REMARK   4 3KK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056093.
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-D
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                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49685
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 7.400
REMARK 200  R MERGE                    (I) : 0.07900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.4000
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) : 2.85
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.54700
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   (%): 67.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, LITHIUM CHLORIDE,
REMARK 280  SODIUM AZIDE, N-OCTYL GLUCOSIDE, PH 6.5, VAPOR DIFFUSION,
REMARK 280  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       68.46533
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       34.23267
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       51.34900
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       17.11633
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       85.58167
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: 21710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 78.0 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     TRP A  75    CG   CD1  CD2  NE1  CE2  CE3  CZ2
REMARK 470     TRP A  75    CZ3  CH2
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  97    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     GLN A 170    CG   CD   OE1  NE2
REMARK 470     ASP A 173    CG   OD1  OD2
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     LYS A 215    CG   CD   CE   NZ
REMARK 470     LYS A 222    CG   CD   CE   NZ
REMARK 470     GLU A 239    CG   CD   OE1  OE2
REMARK 470     GLU A 267    CG   CD   OE1  OE2
REMARK 470     GLU A 268    CG   CD   OE1  OE2
REMARK 470     ARG A 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 282    CG   CD   OE1  NE2
REMARK 470     LYS A 317    CG   CD   CE   NZ
REMARK 470     LEU A 422    CG   CD1  CD2
REMARK 470     LYS A 453    CG   CD   CE   NZ
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     LYS A 485    CG   CD   CE   NZ
REMARK 470     GLU A 492    CG   CD   OE1  OE2
REMARK 470     GLU A 493    CG   CD   OE1  OE2
REMARK 470     LYS A 511    CG   CD   CE   NZ
REMARK 470     LYS A 573    CG   CD   CE   NZ
REMARK 470     GLU B  73    CG   CD   OE1  OE2
REMARK 470     LEU B  78    CG   CD1  CD2
REMARK 470     ARG B  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR B  80    OG1  CG2
REMARK 470     ARG B 157    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     ARG B 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 185    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     LYS B 222    CG   CD   CE   NZ
REMARK 470     GLU B 239    CG   CD   OE1  OE2
REMARK 470     GLU B 267    CG   CD   OE1  OE2
REMARK 470     ARG B 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN B 282    CG   CD   OE1  NE2
REMARK 470     LYS B 317    CG   CD   CE   NZ
REMARK 470     ARG B 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN B 406    CG   CD   OE1  NE2
REMARK 470     LYS B 453    CG   CD   CE   NZ
REMARK 470     LYS B 473    CG   CD   CE   NZ
REMARK 470     GLN B 479    CG   CD   OE1  NE2
REMARK 470     LYS B 485    CG   CD   CE   NZ
REMARK 470     GLU B 490    CG   CD   OE1  OE2
REMARK 470     LYS B 532    CG   CD   CE   NZ
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     CYS B   69   N
REMARK 480     ASN B  122   N
REMARK 480     LEU B  123   N
REMARK 480     PRO B  127   N
REMARK 480     TYR B  130   O
REMARK 480     LEU B  171   CG   CD1  CD2
REMARK 480     GLN B  243   CB   CG   CD   OE1  NE2
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   HG   CYS B    36     SG   CYS B    47              0.73
REMARK 500   O    VAL B   349     HG   SER B   353              0.80
REMARK 500   SG   CYS A    41     HG   CYS A    57              0.89
REMARK 500  HD21  ASN A   144     C1   NAG A   671              0.90
REMARK 500   SG   CYS A    36     HG   CYS A    47              1.25
REMARK 500   O    LEU A   352    HN31  CEL A   701              1.27
REMARK 500   SG   CYS B    36     HG   CYS B    47              1.28
REMARK 500   HG1  THR B   212     O1D  HEM B   601              1.45
REMARK 500   O6   MAN B  1673     H62  BMA B  1674              1.53
REMARK 500   O    VAL B   349     OG   SER B   353              1.53
REMARK 500   OE1  GLN A   192    HN32  CEL A   701              1.57
REMARK 500   ND2  ASN A   144     C1   NAG A   671              1.80
REMARK 500   O4   BMA A   674     C2   MAN A   675              1.81
REMARK 500   O4   BMA A   674     O5   MAN A   675              1.86
REMARK 500   NH2  ARG B    83     O3   BOG B  1751              1.86
REMARK 500   OH   TYR B   147     O6   NAG B  1671              1.91
REMARK 500   OD1  ASN B   410     C1   NAG B  1681              1.92
REMARK 500   O4   BMA A   674     C5   MAN A   675              1.92
REMARK 500   OD1  ASN B   144     C1   NAG B  1671              1.97
REMARK 500   O4   BMA A   674     C1   MAN A   675              2.01
REMARK 500   ND2  ASN A   144     O5   NAG A   671              2.16
REMARK 500   OE1  GLN B   243     C3   MAN A   675              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    ILE B   279     H83  NAG A   681     4565     1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 180   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 180   NE  -  CZ  -  NH2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    PRO A 280   C   -  N   -  CD  ANGL. DEV. = -18.6 DEGREES
REMARK 500    ARG A 459   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG A 459   NE  -  CZ  -  NH2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    PRO A 514   C   -  N   -  CD  ANGL. DEV. = -16.3 DEGREES
REMARK 500    ARG B  97   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B 180   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG B 180   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ARG B 459   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG B 459   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A  53       28.63   -145.42
REMARK 500    CYS A  59       36.74    -98.99
REMARK 500    LEU A 117      -72.04    -71.49
REMARK 500    SER A 146        0.28    -64.65
REMARK 500    ASP A 158       30.95    -90.49
REMARK 500    ARG A 185      -67.35    -98.34
REMARK 500    THR A 194      142.82    -39.67
REMARK 500    LYS A 253      154.75    -47.48
REMARK 500    HIS A 274       39.61    -99.40
REMARK 500    SER A 283       -0.57    108.39
REMARK 500    VAL A 291       26.52     46.33
REMARK 500    GLU A 347      -50.76   -133.58
REMARK 500    TYR A 373       54.04    -90.29
REMARK 500    PRO A 392     -167.17    -77.49
REMARK 500    SER A 394     -158.76   -145.74
REMARK 500    PRO A 462     -177.19    -55.74
REMARK 500    PRO A 514      -39.48    -37.18
REMARK 500    TRP A 545       44.72    -87.63
REMARK 500    GLN B  44       42.76     71.47
REMARK 500    ASP B  53       28.66   -145.51
REMARK 500    CYS B  59       36.85    -98.75
REMARK 500    CYS B  69       43.13     72.26
REMARK 500    LEU B 117      -72.06    -71.59
REMARK 500    PRO B 128      173.75    -45.09
REMARK 500    THR B 129      -55.03   -127.76
REMARK 500    SER B 146        0.03    -64.52
REMARK 500    ARG B 157        5.45    -68.23
REMARK 500    ARG B 185      -67.09    -98.79
REMARK 500    THR B 194      142.32    -39.89
REMARK 500    LYS B 215      -72.73    -35.96
REMARK 500    LYS B 253      154.67    -47.26
REMARK 500    HIS B 274       39.48    -99.22
REMARK 500    ARG B 277     -149.97     57.60
REMARK 500    ILE B 279      167.92     82.03
REMARK 500    GLU B 347      -51.39   -126.36
REMARK 500    TYR B 373       53.74    -90.68
REMARK 500    PRO B 392     -167.05    -77.57
REMARK 500    SER B 394     -158.78   -145.65
REMARK 500    PRO B 462     -177.03    -56.05
REMARK 500    TRP B 545       44.89    -87.42
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  27        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH A 603        DISTANCE =  5.86 ANGSTROMS
REMARK 525    HOH B   5        DISTANCE =  6.72 ANGSTROMS
REMARK 525    HOH B 591        DISTANCE =  6.28 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615   M RES C  SSEQI
REMARK 615     BOG A   751
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 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 675
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CEL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 1662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1674
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 1682
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CEL B 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1751
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1752
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 MET TO LEU CONFLICT IN UNP ENTRY  P05979
DBREF  3KK6 A   32   584  UNP    P05979   PGH1_SHEEP      32    584
DBREF  3KK6 B   32   584  UNP    P05979   PGH1_SHEEP      32    584
SEQADV 3KK6 LEU A   92  UNP  P05979    MET    92 SEE REMARK 999
SEQADV 3KK6 LEU B   92  UNP  P05979    MET    92 SEE REMARK 999
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
HET    HEM  A 601      73
HET    NAG  A 671      26
HET    NAG  A 672      26
HET    MAN  A 673      11
HET    BMA  A 674      20
HET    MAN  A 675      11
HET    NAG  A 681      26
HET    NDG  A 682      27
HET    CEL  A 701      40
HET    BOG  A 751      47
HET    BOG  A 754      48
HET    FLC  A 900      18
HET    HEM  B 601      73
HET    NAG  B1661      26
HET    NDG  B1662      27
HET    NAG  B1671      26
HET    NAG  B1672      26
HET    MAN  B1673      17
HET    BMA  B1674      21
HET    NAG  B1681      26
HET    NDG  B1682      27
HET    CEL  B1701      40
HET    BOG  B1751      48
HET    BOG  B1752      48
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     CEL 4-[5-(4-METHYLPHENYL)-3-(TRIFLUOROMETHYL)-1H-PYRAZOL-1-
HETNAM   2 CEL  YL]BENZENESULFONAMIDE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     FLC CITRATE ANION
HETSYN     HEM HEME
HETSYN     CEL CELECOXIB
FORMUL   3  HEM    2(C34 H32 FE N4 O4)
FORMUL   4  NAG    7(C8 H15 N O6)
FORMUL   4  MAN    3(C6 H12 O6)
FORMUL   4  BMA    2(C6 H12 O6)
FORMUL   5  NDG    3(C8 H15 N O6)
FORMUL   6  CEL    2(C17 H14 F3 N3 O2 S)
FORMUL   7  BOG    4(C14 H28 O6)
FORMUL   9  FLC    C6 H5 O7 3-
FORMUL  17  HOH   *105(H2 O)
HELIX    1   1 ASN A   34  TYR A   38  5                                   5
HELIX    2   2 GLU A   73  LEU A   82  1                                  10
HELIX    3   3 SER A   85  LEU A   93  1                                   9
HELIX    4   4 GLY A   96  ASN A  104  1                                   9
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  ARG A  179  1                                   7
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 LEU A  295  HIS A  320  1                                  26
HELIX   11  11 GLY A  324  GLU A  346  1                                  23
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 VAL A  419  SER A  427  1                                   9
HELIX   19  19 ILE A  444  ARG A  459  1                                  16
HELIX   20  20 PRO A  462  PHE A  470  1                                   9
HELIX   21  21 SER A  477  GLY A  483  1                                   7
HELIX   22  22 GLU A  484  TYR A  495  1                                  12
HELIX   23  23 ASP A  497  LEU A  501  5                                   5
HELIX   24  24 GLU A  502  GLU A  510  1                                   9
HELIX   25  25 GLY A  519  GLY A  536  1                                  18
HELIX   26  26 ASN A  537  SER A  541  5                                   5
HELIX   27  27 ALA A  547  GLY A  551  5                                   5
HELIX   28  28 GLY A  552  THR A  561  1                                  10
HELIX   29  29 LYS A  565  LEU A  570  1                                   6
HELIX   30  30 ASN B   34  TYR B   39  5                                   6
HELIX   31  31 GLU B   73  LEU B   82  1                                  10
HELIX   32  32 SER B   85  LEU B   93  1                                   9
HELIX   33  33 GLY B   96  ASN B  104  1                                   9
HELIX   34  34 PHE B  107  ASN B  122  1                                  16
HELIX   35  35 SER B  138  ASN B  144  1                                   7
HELIX   36  36 ASP B  173  ARG B  179  1                                   7
HELIX   37  37 ASN B  195  HIS B  207  1                                  13
HELIX   38  38 ASN B  237  ARG B  245  1                                   9
HELIX   39  39 PRO B  280  GLN B  284  5                                   5
HELIX   40  40 LEU B  295  HIS B  320  1                                  26
HELIX   41  41 GLY B  324  GLU B  347  1                                  24
HELIX   42  42 GLU B  347  GLY B  354  1                                   8
HELIX   43  43 ASP B  362  PHE B  367  5                                   6
HELIX   44  44 ALA B  378  TYR B  385  1                                   8
HELIX   45  45 TRP B  387  MET B  391  5                                   5
HELIX   46  46 SER B  403  LEU B  408  1                                   6
HELIX   47  47 SER B  412  GLY B  418  1                                   7
HELIX   48  48 VAL B  419  SER B  427  1                                   9
HELIX   49  49 ILE B  444  ARG B  459  1                                  16
HELIX   50  50 PRO B  462  PHE B  470  1                                   9
HELIX   51  51 SER B  477  GLY B  483  1                                   7
HELIX   52  52 GLU B  484  GLU B  493  1                                  10
HELIX   53  53 ASP B  497  LEU B  501  5                                   5
HELIX   54  54 GLU B  502  GLU B  510  1                                   9
HELIX   55  55 GLY B  519  GLY B  536  1                                  18
HELIX   56  56 ASN B  537  SER B  541  5                                   5
HELIX   57  57 ALA B  547  GLY B  551  5                                   5
HELIX   58  58 GLY B  552  THR B  561  1                                  10
HELIX   59  59 LYS B  565  LEU B  570  1                                   6
SHEET    1   A 2 ILE A  46  PHE A  50  0
SHEET    2   A 2 ARG A  54  ASP A  58 -1  O  ASP A  58   N  ILE A  46
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  GLN A 400   N  VAL A 397
SHEET    1   F 2 ILE B  46  PHE B  50  0
SHEET    2   F 2 ARG B  54  ASP B  58 -1  O  ASP B  58   N  ILE B  46
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 TYR B 130  ASN B 131  0
SHEET    2   H 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130
SHEET    1   I 2 GLN B 255  LEU B 257  0
SHEET    2   I 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   J 2 PHE B 395  VAL B 397  0
SHEET    2   J 2 GLN B 400  TYR B 402 -1  O  GLN B 400   N  VAL B 397
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.03
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  2.03
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  1.56
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         O4  NAG B1671                 C1  NAG B1672     1555   1555  1.44
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44
LINK         O4  NAG B1672                 C1  MAN B1673     1555   1555  1.44
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.45
LINK         O4  NAG B1661                 C1  NDG B1662     1555   1555  1.42
LINK         O4  NAG A 681                 C1  NDG A 682     1555   1555  1.42
LINK         O6  MAN B1673                 C1  BMA B1674     1555   1555  1.43
LINK         O4  MAN A 673                 C1  BMA A 674     1555   1555  1.44
LINK         O3  BMA A 674                 C1  MAN A 675     1555   1555  1.44
LINK         O4  NAG B1681                 C1  NDG B1682     1555   1555  1.45
CISPEP   1 SER A  126    PRO A  127          0        -7.92
CISPEP   2 GLY A  235    ASP A  236          0         3.22
CISPEP   3 PRO A  281    GLN A  282          0         8.67
CISPEP   4 GLY A  437    ARG A  438          0         0.66
CISPEP   5 SER B  126    PRO B  127          0        13.82
CISPEP   6 GLY B  235    ASP B  236          0         3.77
CISPEP   7 ARG B  277    GLY B  278          0        -0.09
CISPEP   8 GLY B  437    ARG B  438          0         0.67
SITE     1 AC1 16 TYR A 148  GLN A 203  HIS A 207  PHE A 210
SITE     2 AC1 16 LYS A 211  THR A 212  LEU A 295  ASN A 382
SITE     3 AC1 16 TYR A 385  HIS A 386  TRP A 387  HIS A 388
SITE     4 AC1 16 MET A 391  VAL A 447  ASP A 450  FLC A 900
SITE     1 AC2  3 ASN A 144  TYR A 147  NAG A 672
SITE     1 AC3  3 NAG A 671  MAN A 673  LEU B 238
SITE     1 AC4  2 NAG A 672  BMA A 674
SITE     1 AC5  2 MAN A 673  MAN A 675
SITE     1 AC6  2 BMA A 674  HOH B 592
SITE     1 AC7  8 TYR A 402  GLN A 406  ASN A 410  MET A 413
SITE     2 AC7  8 ASP A 416  NDG A 682  ILE B 279  PRO B 281
SITE     1 AC8  6 GLN A 400  TYR A 402  GLN A 406  ASP A 416
SITE     2 AC8  6 HOH A 599  NAG A 681
SITE     1 AC9 16 HIS A  90  VAL A 116  GLN A 192  VAL A 349
SITE     2 AC9 16 LEU A 352  SER A 353  TYR A 355  LEU A 359
SITE     3 AC9 16 TRP A 387  SER A 516  ILE A 517  PHE A 518
SITE     4 AC9 16 MET A 522  ILE A 523  GLY A 526  ALA A 527
SITE     1 BC1  5 PRO A  86  LEU A 115  VAL A 119  ARG A 120
SITE     2 BC1  5 GLU A 524
SITE     1 BC2  5 PRO A  84  SER A  85  SER A  87  PHE A  88
SITE     2 BC2  5 PHE A  91
SITE     1 BC3  3 LYS A 211  THR A 212  HEM A 601
SITE     1 BC4 15 ALA B 199  GLN B 203  THR B 206  HIS B 207
SITE     2 BC4 15 PHE B 210  LYS B 211  THR B 212  ASN B 382
SITE     3 BC4 15 TYR B 385  HIS B 386  TRP B 387  HIS B 388
SITE     4 BC4 15 MET B 391  VAL B 447  ASP B 450
SITE     1 BC5  3 TYR B  55  ASN B  68  NDG B1662
SITE     1 BC6  3 HOH B  31  TYR B  38  NAG B1661
SITE     1 BC7  3 ASN B 144  TYR B 147  NAG B1672
SITE     1 BC8  4 MET B 216  HOH B 588  NAG B1671  MAN B1673
SITE     1 BC9  3 HOH B 589  NAG B1672  BMA B1674
SITE     1 CC1  1 MAN B1673
SITE     1 CC2  7 PRO A 281  TYR B 402  GLN B 406  ASN B 410
SITE     2 CC2  7 MET B 413  ASP B 416  NDG B1682
SITE     1 CC3  3 HOH B   4  TYR B 402  NAG B1681
SITE     1 CC4 17 HIS B  90  VAL B 116  GLN B 192  VAL B 349
SITE     2 CC4 17 LEU B 352  SER B 353  TYR B 355  LEU B 359
SITE     3 CC4 17 TRP B 387  SER B 516  ILE B 517  PHE B 518
SITE     4 CC4 17 MET B 522  ILE B 523  GLY B 526  ALA B 527
SITE     5 CC4 17 SER B 530
SITE     1 CC5  6 ARG B  83  ILE B  89  ARG B 120  GLY B 471
SITE     2 CC5  6 GLU B 524  HOH B 617
SITE     1 CC6  4 TRP B  77  GLY B  96  ARG B  97  TRP B  98
CRYST1  181.035  181.035  102.698  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      0.005524  0.003189  0.000000        0.00000
SCALE2      0.000000  0.006378  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009737        0.00000
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1
MTRIX1   2 -0.521844 -0.853041 -0.000040        0.00336    1
MTRIX2   2 -0.853023  0.521834 -0.006415        0.20183    1
MTRIX3   2  0.005493 -0.003314 -0.999979       36.11250    1
      
PROCHECK
Go to PROCHECK summary
 References