HEADER OXIDOREDUCTASE 04-JUL-10 3NTG
TITLE CRYSTAL STRUCTURE OF COX-2 WITH SELECTIVE COMPOUND 23D-(R)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: MCOX-2 C DELTA (UNP RESIDUES 18 TO 604);
COMPND 5 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED
COMPND 6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-
COMPND 7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2
COMPND 8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE
COMPND 9 SYNTHASE 2, TIS10 PROTEIN;
COMPND 10 EC: 1.14.99.1;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: COX-2, COX2, MCG_5001, PGHS-B, PTGS2, TIS10;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS COX2, COX-2, PGH2S-2, CYCLOOXYGENASE-2, DIOXYGENASE, DISULFIDE BOND,
KEYWDS 2 ENDOPLASMIC RETICULUM, FATTY ACID BIOSYNTHESIS, GLYCOPROTEIN, HEME,
KEYWDS 3 IRON, LIPID SYNTHESIS, MEMBRANE, METAL-BINDING, MICROSOME,
KEYWDS 4 OXIDOREDUCTASE, PEROXIDASE, PHOSPHOPROTEIN, PROSTAGLANDIN
KEYWDS 5 BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.WANG,D.LIMBURG,M.J.GRANETO,J.C.CARTER,J.J.TALLEY,J.R.KIEFER
REVDAT 3 23-MAR-11 3NTG 1 COMPND DBREF SOURCE
REVDAT 2 01-DEC-10 3NTG 1 JRNL
REVDAT 1 27-OCT-10 3NTG 0
JRNL AUTH J.L.WANG,D.LIMBURG,M.J.GRANETO,J.SPRINGER,J.R.HAMPER,S.LIAO,
JRNL AUTH 2 J.L.PAWLITZ,R.G.KURUMBAIL,T.MAZIASZ,J.J.TALLEY,J.R.KIEFER,
JRNL AUTH 3 J.CARTER
JRNL TITL THE NOVEL BENZOPYRAN CLASS OF SELECTIVE CYCLOOXYGENASE-2
JRNL TITL 2 INHIBITORS. PART 2: THE SECOND CLINICAL CANDIDATE HAVING A
JRNL TITL 3 SHORTER AND FAVORABLE HUMAN HALF-LIFE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 7159 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20709553
JRNL DOI 10.1016/J.BMCL.2010.07.054
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 3 NUMBER OF REFLECTIONS : 120646
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13440
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8199
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 888
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17900
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 476
REMARK 3 SOLVENT ATOMS : 1077
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.63000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : 1.57000
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): 0.330
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.243
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.270
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 18966 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 12911 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 25818 ; 1.232 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 31375 ; 0.870 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2208 ; 5.590 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 897 ;38.275 ;24.114
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3107 ;16.750 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;17.099 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2713 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20864 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3852 ; 0.001 ; 0.020
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): 11048 ; 0.371 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4420 ; 0.077 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17959 ; 0.709 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7918 ; 1.202 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7859 ; 1.979 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 18 A 569
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7730 28.8900 9.2420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0050 T22: 0.0096
REMARK 3 T33: 0.0206 T12: 0.0004
REMARK 3 T13: 0.0028 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.0221 L22: 0.8460
REMARK 3 L33: 0.9009 L12: 0.0677
REMARK 3 L13: -0.0248 L23: 0.5016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: -0.0584 S13: -0.0780
REMARK 3 S21: 0.0025 S22: -0.0279 S23: 0.1016
REMARK 3 S31: 0.0189 S32: -0.0696 S33: 0.0466
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 18 B 569
REMARK 3 ORIGIN FOR THE GROUP (A): 67.2030 22.0290 2.1100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0140 T22: 0.0329
REMARK 3 T33: 0.0115 T12: 0.0018
REMARK 3 T13: -0.0002 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.0829 L22: 0.7138
REMARK 3 L33: 0.9328 L12: 0.0608
REMARK 3 L13: 0.1457 L23: 0.4267
REMARK 3 S TENSOR
REMARK 3 S11: 0.0099 S12: -0.0483 S13: -0.0186
REMARK 3 S21: 0.0421 S22: 0.0104 S23: -0.0742
REMARK 3 S31: -0.0004 S32: 0.1337 S33: -0.0203
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 18 C 569
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5260 45.4940 63.5120
REMARK 3 T TENSOR
REMARK 3 T11: 0.0364 T22: 0.0820
REMARK 3 T33: 0.0265 T12: 0.0318
REMARK 3 T13: -0.0038 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 1.0855 L22: 0.7424
REMARK 3 L33: 1.1008 L12: -0.0440
REMARK 3 L13: -0.0659 L23: -0.4917
REMARK 3 S TENSOR
REMARK 3 S11: -0.0179 S12: -0.0926 S13: 0.0566
REMARK 3 S21: 0.0755 S22: 0.0523 S23: 0.0986
REMARK 3 S31: -0.0698 S32: -0.2180 S33: -0.0344
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 18 D 569
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8480 37.9770 70.2690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0179 T22: 0.0323
REMARK 3 T33: 0.0328 T12: -0.0016
REMARK 3 T13: -0.0107 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 1.1640 L22: 0.8529
REMARK 3 L33: 1.1535 L12: -0.0073
REMARK 3 L13: 0.1290 L23: -0.5574
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: -0.0137 S13: 0.1118
REMARK 3 S21: 0.0135 S22: -0.0538 S23: -0.1263
REMARK 3 S31: -0.0439 S32: 0.1011 S33: 0.0865
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 3NTG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
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 : CRYSTAL
REMARK 200 OPTICS : CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134127
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.51100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 90.13400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.13650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 90.13400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.13650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMER OF DIMERS
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: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 10800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 C 362 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 455 NE - CZ - NH2 ANGL. DEV. = -3.2 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 THR A 45 121.02 -38.96
REMARK 500 THR A 115 -88.44 -125.53
REMARK 500 TRP A 373 44.31 -97.57
REMARK 500 GLU A 384 -125.06 54.33
REMARK 500 SER A 482 -61.45 69.47
REMARK 500 ASP B 38 30.45 -141.33
REMARK 500 THR B 115 -90.06 -120.40
REMARK 500 ARG B 171 -65.30 -96.70
REMARK 500 ASP B 333 -52.33 -120.01
REMARK 500 HIS B 372 79.39 -69.94
REMARK 500 TRP B 373 47.29 -99.23
REMARK 500 GLU B 384 -130.15 57.97
REMARK 500 ASN B 425 22.46 -143.04
REMARK 500 SER B 482 -49.47 65.12
REMARK 500 ASP B 501 29.43 49.76
REMARK 500 CYS B 561 66.32 38.35
REMARK 500 THR C 115 -92.23 -115.96
REMARK 500 ARG C 171 -76.48 -93.20
REMARK 500 LYS C 197 69.05 -150.02
REMARK 500 TRP C 373 46.22 -96.21
REMARK 500 GLU C 384 -125.42 60.58
REMARK 500 TYR C 395 11.73 58.81
REMARK 500 ASN C 396 74.85 -117.36
REMARK 500 ASN C 425 16.61 -144.87
REMARK 500 SER C 482 -50.33 65.66
REMARK 500 THR D 115 -87.43 -126.23
REMARK 500 ASP D 333 -50.29 -123.05
REMARK 500 TRP D 373 48.73 -94.58
REMARK 500 GLU D 384 -119.66 58.05
REMARK 500 ASN D 425 18.95 -140.16
REMARK 500 SER D 482 -59.91 77.74
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 C4349 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B4422 DISTANCE = 5.90 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 374 NE2
REMARK 620 2 HEM B 601 NA 91.0
REMARK 620 3 HEM B 601 NB 91.6 90.9
REMARK 620 4 HEM B 601 NC 91.2 177.7 88.1
REMARK 620 5 HEM B 601 ND 89.4 89.2 179.0 91.7
REMARK 620 6 HOH B5274 O 170.7 80.6 84.8 97.2 94.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 374 NE2
REMARK 620 2 HEM A 601 NA 93.3
REMARK 620 3 HEM A 601 NB 96.0 88.9
REMARK 620 4 HEM A 601 NC 89.8 176.9 91.0
REMARK 620 5 HEM A 601 ND 84.8 89.6 178.3 90.6
REMARK 620 6 HOH A4121 O 172.0 81.2 89.8 95.6 89.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 374 NE2
REMARK 620 2 HEM D 601 NA 89.6
REMARK 620 3 HEM D 601 NB 92.8 87.0
REMARK 620 4 HEM D 601 NC 92.5 177.4 91.4
REMARK 620 5 HEM D 601 ND 87.1 92.1 179.1 89.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 374 NE2
REMARK 620 2 HEM C 601 NA 87.6
REMARK 620 3 HEM C 601 NB 91.7 90.3
REMARK 620 4 HEM C 601 NC 94.9 177.5 89.4
REMARK 620 5 HEM C 601 ND 89.1 89.2 179.0 91.1
REMARK 620 6 HOH C4116 O 169.2 81.7 90.1 95.7 89.0
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 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 NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D72 D 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PXX RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH DICLOFENAC
REMARK 900 RELATED ID: 3LN1 RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH CELECOXIB
REMARK 900 RELATED ID: 3MQE RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH SC-75416
REMARK 900 RELATED ID: 3LN0 RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH COMPOUND 5C-(S)
REMARK 900 RELATED ID: 3PGH RELATED DB: PDB
REMARK 900 STRUCTURE OF COX-2 WITH FLURBIPROFEN
DBREF 3NTG A 18 569 UNP Q05769 PGH2_MOUSE 18 569
DBREF 3NTG B 18 569 UNP Q05769 PGH2_MOUSE 18 569
DBREF 3NTG C 18 569 UNP Q05769 PGH2_MOUSE 18 569
DBREF 3NTG D 18 569 UNP Q05769 PGH2_MOUSE 18 569
SEQRES 1 A 552 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 A 552 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 A 552 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 A 552 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 A 552 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 A 552 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 A 552 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 A 552 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 A 552 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 A 552 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 A 552 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 A 552 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 A 552 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 A 552 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 A 552 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 A 552 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 A 552 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 A 552 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 A 552 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 A 552 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 A 552 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 A 552 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 A 552 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 A 552 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 A 552 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 A 552 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 A 552 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 A 552 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 A 552 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 A 552 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 A 552 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 A 552 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 A 552 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 A 552 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 A 552 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 A 552 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 A 552 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 A 552 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 A 552 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 A 552 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 A 552 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 A 552 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 A 552 THR SER PHE ASN VAL GLN
SEQRES 1 B 552 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 B 552 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 B 552 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 B 552 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 B 552 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 B 552 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 B 552 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 B 552 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 B 552 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 B 552 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 B 552 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 B 552 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 B 552 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 B 552 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 B 552 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 B 552 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 B 552 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 B 552 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 B 552 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 B 552 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 B 552 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 B 552 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 B 552 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 B 552 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 B 552 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 B 552 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 B 552 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 B 552 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 B 552 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 B 552 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 B 552 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 B 552 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 B 552 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 B 552 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 B 552 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 B 552 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 B 552 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 B 552 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 B 552 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 B 552 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 B 552 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 B 552 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 B 552 THR SER PHE ASN VAL GLN
SEQRES 1 C 552 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 C 552 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 C 552 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 C 552 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 C 552 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 C 552 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 C 552 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 C 552 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 C 552 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 C 552 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 C 552 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 C 552 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 C 552 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 C 552 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 C 552 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 C 552 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 C 552 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 C 552 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 C 552 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 C 552 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 C 552 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 C 552 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 C 552 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 C 552 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 C 552 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 C 552 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 C 552 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 C 552 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 C 552 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 C 552 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 C 552 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 C 552 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 C 552 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 C 552 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 C 552 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 C 552 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 C 552 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 C 552 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 C 552 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 C 552 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 C 552 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 C 552 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 C 552 THR SER PHE ASN VAL GLN
SEQRES 1 D 552 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 D 552 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 D 552 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 D 552 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 D 552 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 D 552 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 D 552 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 D 552 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 D 552 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 D 552 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 D 552 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 D 552 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 D 552 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 D 552 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 D 552 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 D 552 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 D 552 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 D 552 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 D 552 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 D 552 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 D 552 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 D 552 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 D 552 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 D 552 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 D 552 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 D 552 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 D 552 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 D 552 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 D 552 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 D 552 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 D 552 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 D 552 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 D 552 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 D 552 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 D 552 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 D 552 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 D 552 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 D 552 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 D 552 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 D 552 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 D 552 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 D 552 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 D 552 THR SER PHE ASN VAL GLN
MODRES 3NTG ASN B 130 ASN GLYCOSYLATION SITE
MODRES 3NTG ASN C 396 ASN GLYCOSYLATION SITE
MODRES 3NTG ASN A 396 ASN GLYCOSYLATION SITE
MODRES 3NTG ASN B 396 ASN GLYCOSYLATION SITE
MODRES 3NTG ASN A 130 ASN GLYCOSYLATION SITE
MODRES 3NTG ASN D 130 ASN GLYCOSYLATION SITE
MODRES 3NTG ASN C 130 ASN GLYCOSYLATION SITE
MODRES 3NTG ASN D 396 ASN GLYCOSYLATION SITE
HET HEM A 601 43
HET NAG A 671 14
HET NAG A 672 14
HET NAG A 681 14
HET BOG A 703 20
HET D72 A 701 24
HET HEM B 601 43
HET NAG B 671 14
HET NAG B 672 14
HET NAG B 681 14
HET D72 B 701 24
HET HEM C 601 43
HET NAG C 671 14
HET NAG C 672 14
HET NAG C 681 14
HET D72 C 701 24
HET HEM D 601 43
HET NAG D 671 14
HET NAG D 672 14
HET NAG D 681 14
HET BOG D 703 20
HET D72 D 701 24
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BOG B-OCTYLGLUCOSIDE
HETNAM D72 (2R)-6,8-DICHLORO-7-(2-METHYLPROPOXY)-2-
HETNAM 2 D72 (TRIFLUOROMETHYL)-2H-CHROMENE-3-CARBOXYLIC ACID
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 NAG 12(C8 H15 N O6)
FORMUL 8 BOG 2(C14 H28 O6)
FORMUL 9 D72 4(C15 H13 CL2 F3 O4)
FORMUL 23 HOH *1077(H2 O)
HELIX 1 1 GLU A 58 LYS A 68 1 11
HELIX 2 2 THR A 70 THR A 79 1 10
HELIX 3 3 PHE A 81 ASN A 90 1 10
HELIX 4 4 ILE A 91 TYR A 108 1 18
HELIX 5 5 SER A 124 ASN A 130 1 7
HELIX 6 6 ASP A 159 LEU A 168 1 10
HELIX 7 7 ASN A 181 HIS A 193 1 13
HELIX 8 8 LEU A 216 GLY A 221 1 6
HELIX 9 9 THR A 223 ARG A 231 1 9
HELIX 10 10 THR A 251 GLN A 256 1 6
HELIX 11 11 PRO A 266 GLN A 270 5 5
HELIX 12 12 VAL A 277 LEU A 280 5 4
HELIX 13 13 VAL A 281 HIS A 306 1 26
HELIX 14 14 GLY A 310 ASP A 333 1 24
HELIX 15 15 ASP A 333 GLY A 340 1 8
HELIX 16 16 ASP A 348 PHE A 353 5 6
HELIX 17 17 ALA A 364 TYR A 371 1 8
HELIX 18 18 TRP A 373 LEU A 377 5 5
HELIX 19 19 SER A 389 LEU A 394 1 6
HELIX 20 20 ASN A 397 GLY A 404 1 8
HELIX 21 21 GLY A 404 GLN A 415 1 12
HELIX 22 22 PRO A 427 ALA A 429 5 3
HELIX 23 23 VAL A 430 MET A 444 1 15
HELIX 24 24 SER A 448 PHE A 456 1 9
HELIX 25 25 SER A 463 GLY A 469 1 7
HELIX 26 26 LYS A 471 SER A 482 1 12
HELIX 27 27 ASP A 483 MET A 487 5 5
HELIX 28 28 GLU A 488 GLU A 496 1 9
HELIX 29 29 GLY A 505 GLY A 522 1 18
HELIX 30 30 ASN A 523 SER A 527 5 5
HELIX 31 31 LYS A 532 GLY A 537 5 6
HELIX 32 32 GLY A 538 THR A 547 1 10
HELIX 33 33 SER A 549 VAL A 558 1 10
HELIX 34 34 GLU B 58 LEU B 67 1 10
HELIX 35 35 THR B 70 HIS B 80 1 11
HELIX 36 36 PHE B 81 ASN B 90 1 10
HELIX 37 37 ILE B 91 TYR B 108 1 18
HELIX 38 38 SER B 124 ASN B 130 1 7
HELIX 39 39 ASP B 159 LEU B 168 1 10
HELIX 40 40 ASN B 181 HIS B 193 1 13
HELIX 41 41 LEU B 216 GLY B 221 1 6
HELIX 42 42 THR B 223 ARG B 231 1 9
HELIX 43 43 THR B 251 GLN B 256 1 6
HELIX 44 44 PRO B 266 GLN B 270 5 5
HELIX 45 45 VAL B 277 LEU B 280 5 4
HELIX 46 46 VAL B 281 HIS B 306 1 26
HELIX 47 47 GLY B 310 ASP B 333 1 24
HELIX 48 48 ASP B 333 GLY B 340 1 8
HELIX 49 49 ASP B 348 PHE B 353 5 6
HELIX 50 50 ALA B 364 TYR B 371 1 8
HELIX 51 51 HIS B 372 LEU B 377 5 6
HELIX 52 52 SER B 389 LEU B 394 1 6
HELIX 53 53 ASN B 397 GLN B 415 1 19
HELIX 54 54 PRO B 427 ALA B 429 5 3
HELIX 55 55 VAL B 430 MET B 444 1 15
HELIX 56 56 SER B 448 PHE B 456 1 9
HELIX 57 57 SER B 463 GLY B 469 1 7
HELIX 58 58 LYS B 471 SER B 482 1 12
HELIX 59 59 ASP B 483 MET B 487 5 5
HELIX 60 60 GLU B 488 GLU B 496 1 9
HELIX 61 61 GLY B 505 GLY B 522 1 18
HELIX 62 62 ASN B 523 SER B 527 5 5
HELIX 63 63 LYS B 532 GLY B 537 5 6
HELIX 64 64 GLY B 538 THR B 547 1 10
HELIX 65 65 SER B 549 VAL B 558 1 10
HELIX 66 66 GLU C 58 LYS C 68 1 11
HELIX 67 67 THR C 70 THR C 79 1 10
HELIX 68 68 PHE C 81 ASN C 90 1 10
HELIX 69 69 ILE C 91 TYR C 108 1 18
HELIX 70 70 SER C 124 ASN C 130 1 7
HELIX 71 71 ASP C 159 LEU C 168 1 10
HELIX 72 72 ASN C 181 HIS C 193 1 13
HELIX 73 73 LEU C 216 GLY C 221 1 6
HELIX 74 74 THR C 223 ARG C 231 1 9
HELIX 75 75 THR C 251 GLN C 256 1 6
HELIX 76 76 PRO C 266 GLN C 270 5 5
HELIX 77 77 VAL C 277 LEU C 280 5 4
HELIX 78 78 VAL C 281 HIS C 306 1 26
HELIX 79 79 GLY C 310 ASP C 333 1 24
HELIX 80 80 ASP C 333 GLY C 340 1 8
HELIX 81 81 ASP C 348 PHE C 353 5 6
HELIX 82 82 ALA C 364 TYR C 371 1 8
HELIX 83 83 HIS C 372 LEU C 377 5 6
HELIX 84 84 SER C 389 LEU C 394 1 6
HELIX 85 85 ASN C 397 GLN C 415 1 19
HELIX 86 86 PRO C 427 ALA C 429 5 3
HELIX 87 87 VAL C 430 MET C 444 1 15
HELIX 88 88 SER C 448 PHE C 456 1 9
HELIX 89 89 SER C 463 GLY C 469 1 7
HELIX 90 90 LYS C 471 SER C 482 1 12
HELIX 91 91 ASP C 483 MET C 487 5 5
HELIX 92 92 GLU C 488 GLU C 496 1 9
HELIX 93 93 GLY C 505 GLY C 522 1 18
HELIX 94 94 ASN C 523 SER C 527 5 5
HELIX 95 95 LYS C 532 GLY C 537 5 6
HELIX 96 96 GLY C 538 THR C 547 1 10
HELIX 97 97 SER C 549 VAL C 558 1 10
HELIX 98 98 ASN D 19 ASN D 24 5 6
HELIX 99 99 GLU D 58 LYS D 68 1 11
HELIX 100 100 THR D 70 THR D 79 1 10
HELIX 101 101 PHE D 81 ASN D 90 1 10
HELIX 102 102 ILE D 91 TYR D 108 1 18
HELIX 103 103 SER D 124 ASN D 130 1 7
HELIX 104 104 ASP D 159 LEU D 168 1 10
HELIX 105 105 ASN D 181 HIS D 193 1 13
HELIX 106 106 LEU D 216 GLY D 221 1 6
HELIX 107 107 THR D 223 ARG D 231 1 9
HELIX 108 108 THR D 251 GLN D 256 1 6
HELIX 109 109 VAL D 281 HIS D 306 1 26
HELIX 110 110 GLY D 310 ASP D 333 1 24
HELIX 111 111 ASP D 333 GLY D 340 1 8
HELIX 112 112 ASP D 348 PHE D 353 5 6
HELIX 113 113 ALA D 364 TYR D 371 1 8
HELIX 114 114 HIS D 372 LEU D 377 5 6
HELIX 115 115 SER D 389 LEU D 394 1 6
HELIX 116 116 ASN D 396 GLY D 404 1 9
HELIX 117 117 GLY D 404 GLN D 415 1 12
HELIX 118 118 PRO D 427 ALA D 429 5 3
HELIX 119 119 VAL D 430 MET D 444 1 15
HELIX 120 120 SER D 448 PHE D 456 1 9
HELIX 121 121 SER D 463 GLY D 469 1 7
HELIX 122 122 LYS D 471 SER D 482 1 12
HELIX 123 123 ASP D 483 MET D 487 5 5
HELIX 124 124 GLU D 488 GLU D 496 1 9
HELIX 125 125 GLY D 505 GLY D 522 1 18
HELIX 126 126 ASN D 523 SER D 527 5 5
HELIX 127 127 LYS D 532 GLY D 537 5 6
HELIX 128 128 GLY D 538 THR D 547 1 10
HELIX 129 129 SER D 549 VAL D 558 1 10
SHEET 1 A 2 GLU A 31 SER A 34 0
SHEET 2 A 2 TYR A 40 ASP A 43 -1 O ASP A 43 N GLU A 31
SHEET 1 B 2 PHE A 49 TYR A 50 0
SHEET 2 B 2 THR A 56 PRO A 57 -1 O THR A 56 N TYR A 50
SHEET 1 C 2 TYR A 116 ASN A 117 0
SHEET 2 C 2 THR A 135 ARG A 136 -1 O ARG A 136 N TYR A 116
SHEET 1 D 2 GLN A 241 ILE A 243 0
SHEET 2 D 2 GLU A 246 TYR A 248 -1 O TYR A 248 N GLN A 241
SHEET 1 E 2 PHE A 381 ILE A 383 0
SHEET 2 E 2 GLN A 386 TYR A 388 -1 O TYR A 388 N PHE A 381
SHEET 1 F 2 GLU B 31 GLY B 36 0
SHEET 2 F 2 GLN B 39 ASP B 43 -1 O ASP B 43 N GLU B 31
SHEET 1 G 2 PHE B 49 TYR B 50 0
SHEET 2 G 2 THR B 56 PRO B 57 -1 O THR B 56 N TYR B 50
SHEET 1 H 2 TYR B 116 ASN B 117 0
SHEET 2 H 2 THR B 135 ARG B 136 -1 O ARG B 136 N TYR B 116
SHEET 1 I 2 GLN B 241 ILE B 243 0
SHEET 2 I 2 GLU B 246 TYR B 248 -1 O TYR B 248 N GLN B 241
SHEET 1 J 2 PHE B 381 ILE B 383 0
SHEET 2 J 2 GLN B 386 TYR B 388 -1 O TYR B 388 N PHE B 381
SHEET 1 K 2 GLU C 31 GLY C 36 0
SHEET 2 K 2 GLN C 39 ASP C 43 -1 O LYS C 41 N MET C 33
SHEET 1 L 2 PHE C 49 TYR C 50 0
SHEET 2 L 2 THR C 56 PRO C 57 -1 O THR C 56 N TYR C 50
SHEET 1 M 2 GLN C 241 ILE C 243 0
SHEET 2 M 2 GLU C 246 TYR C 248 -1 O TYR C 248 N GLN C 241
SHEET 1 N 2 PHE C 381 ILE C 383 0
SHEET 2 N 2 GLN C 386 TYR C 388 -1 O TYR C 388 N PHE C 381
SHEET 1 O 2 GLU D 31 SER D 34 0
SHEET 2 O 2 TYR D 40 ASP D 43 -1 O ASP D 43 N GLU D 31
SHEET 1 P 2 PHE D 49 TYR D 50 0
SHEET 2 P 2 THR D 56 PRO D 57 -1 O THR D 56 N TYR D 50
SHEET 1 Q 2 TYR D 116 ASN D 117 0
SHEET 2 Q 2 THR D 135 ARG D 136 -1 O ARG D 136 N TYR D 116
SHEET 1 R 2 GLN D 241 ILE D 243 0
SHEET 2 R 2 GLU D 246 TYR D 248 -1 O TYR D 248 N GLN D 241
SHEET 1 S 2 PHE D 381 ILE D 383 0
SHEET 2 S 2 GLN D 386 TYR D 388 -1 O TYR D 388 N PHE D 381
SSBOND 1 CYS A 21 CYS A 32 1555 1555 2.06
SSBOND 2 CYS A 22 CYS A 145 1555 1555 2.05
SSBOND 3 CYS A 26 CYS A 42 1555 1555 2.05
SSBOND 4 CYS A 44 CYS A 54 1555 1555 2.06
SSBOND 5 CYS A 555 CYS A 561 1555 1555 2.06
SSBOND 6 CYS B 21 CYS B 32 1555 1555 2.06
SSBOND 7 CYS B 22 CYS B 145 1555 1555 2.05
SSBOND 8 CYS B 26 CYS B 42 1555 1555 2.03
SSBOND 9 CYS B 44 CYS B 54 1555 1555 2.05
SSBOND 10 CYS B 555 CYS B 561 1555 1555 2.04
SSBOND 11 CYS C 21 CYS C 32 1555 1555 2.06
SSBOND 12 CYS C 22 CYS C 145 1555 1555 2.05
SSBOND 13 CYS C 26 CYS C 42 1555 1555 2.03
SSBOND 14 CYS C 44 CYS C 54 1555 1555 2.05
SSBOND 15 CYS C 555 CYS C 561 1555 1555 2.05
SSBOND 16 CYS D 21 CYS D 32 1555 1555 2.05
SSBOND 17 CYS D 22 CYS D 145 1555 1555 2.03
SSBOND 18 CYS D 26 CYS D 42 1555 1555 2.04
SSBOND 19 CYS D 44 CYS D 54 1555 1555 2.05
SSBOND 20 CYS D 555 CYS D 561 1555 1555 2.06
LINK ND2 ASN B 130 C1 NAG B 671 1555 1555 1.43
LINK ND2 ASN C 396 C1 NAG C 681 1555 1555 1.44
LINK ND2 ASN A 396 C1 NAG A 681 1555 1555 1.44
LINK ND2 ASN B 396 C1 NAG B 681 1555 1555 1.44
LINK ND2 ASN A 130 C1 NAG A 671 1555 1555 1.44
LINK ND2 ASN D 130 C1 NAG D 671 1555 1555 1.44
LINK ND2 ASN C 130 C1 NAG C 671 1555 1555 1.44
LINK O4 NAG B 671 C1 NAG B 672 1555 1555 1.44
LINK O4 NAG A 671 C1 NAG A 672 1555 1555 1.44
LINK O4 NAG D 671 C1 NAG D 672 1555 1555 1.44
LINK O4 NAG C 671 C1 NAG C 672 1555 1555 1.44
LINK ND2 ASN D 396 C1 NAG D 681 1555 1555 1.45
LINK NE2 HIS B 374 FE HEM B 601 1555 1555 2.09
LINK NE2 HIS A 374 FE HEM A 601 1555 1555 2.16
LINK NE2 HIS D 374 FE HEM D 601 1555 1555 2.22
LINK NE2 HIS C 374 FE HEM C 601 1555 1555 2.34
LINK FE HEM A 601 O HOH A4121 1555 1555 2.39
LINK FE HEM C 601 O HOH C4116 1555 1555 2.45
LINK FE HEM B 601 O HOH B5274 1555 1555 2.54
CISPEP 1 SER A 112 PRO A 113 0 0.42
CISPEP 2 SER B 112 PRO B 113 0 -0.46
CISPEP 3 SER C 112 PRO C 113 0 1.63
CISPEP 4 SER D 112 PRO D 113 0 3.31
SITE 1 AC1 16 ALA A 185 PHE A 186 GLN A 189 HIS A 193
SITE 2 AC1 16 PHE A 196 LYS A 197 THR A 198 HIS A 200
SITE 3 AC1 16 VAL A 281 ASN A 368 TYR A 371 HIS A 372
SITE 4 AC1 16 HIS A 374 LEU A 377 VAL A 433 HOH A4121
SITE 1 AC2 7 GLU A 126 ASN A 130 TYR A 133 ARG A 202
SITE 2 AC2 7 NAG A 672 HOH A4017 HOH A4298
SITE 1 AC3 3 ARG A 202 NAG A 671 ASP B 225
SITE 1 AC4 4 ASN A 396 SER A 398 ILE A 399 GLU A 402
SITE 1 AC5 10 GLU A 165 ARG A 170 ILE A 428 GLN A 431
SITE 2 AC5 10 HOH A5372 ARG B 170 ARG B 171 ARG B 424
SITE 3 AC5 10 GLU B 472 GLU B 476
SITE 1 AC6 8 ARG A 106 VAL A 335 TYR A 341 LEU A 345
SITE 2 AC6 8 VAL A 509 ALA A 513 SER A 516 LEU A 517
SITE 1 AC7 14 ALA B 185 PHE B 186 GLN B 189 HIS B 193
SITE 2 AC7 14 PHE B 196 LYS B 197 THR B 198 HIS B 200
SITE 3 AC7 14 ASN B 368 TYR B 371 HIS B 372 HIS B 374
SITE 4 AC7 14 LEU B 377 HOH B5274
SITE 1 AC8 9 LEU A 224 GLU B 126 ASN B 130 TYR B 133
SITE 2 AC8 9 ARG B 202 NAG B 672 HOH B4045 HOH B4370
SITE 3 AC8 9 HOH B4889
SITE 1 AC9 3 ARG B 202 NAG B 671 HOH B4882
SITE 1 BC1 3 GLN B 392 ASN B 396 ILE B 399
SITE 1 BC2 10 ARG B 106 VAL B 335 TYR B 341 LEU B 345
SITE 2 BC2 10 MET B 508 VAL B 509 GLY B 512 ALA B 513
SITE 3 BC2 10 SER B 516 LEU B 517
SITE 1 BC3 16 ALA C 185 PHE C 186 ALA C 188 GLN C 189
SITE 2 BC3 16 HIS C 193 PHE C 196 LYS C 197 THR C 198
SITE 3 BC3 16 HIS C 200 VAL C 281 ASN C 368 TYR C 371
SITE 4 BC3 16 HIS C 372 HIS C 374 LEU C 377 HOH C4116
SITE 1 BC4 8 GLU C 126 ASN C 130 TYR C 133 ARG C 202
SITE 2 BC4 8 NAG C 672 HOH C4085 HOH C4331 HOH C4757
SITE 1 BC5 3 ARG C 202 NAG C 671 ASP D 225
SITE 1 BC6 4 LYS C 391 GLN C 392 ASN C 396 ILE C 399
SITE 1 BC7 8 ARG C 106 VAL C 335 TYR C 341 LEU C 345
SITE 2 BC7 8 VAL C 509 GLY C 512 ALA C 513 LEU C 517
SITE 1 BC8 15 ALA D 185 PHE D 186 GLN D 189 HIS D 193
SITE 2 BC8 15 PHE D 196 LYS D 197 THR D 198 HIS D 200
SITE 3 BC8 15 ASN D 368 TYR D 371 HIS D 372 HIS D 374
SITE 4 BC8 15 LEU D 377 LEU D 394 VAL D 433
SITE 1 BC9 7 GLU D 126 ASN D 130 TYR D 133 ARG D 202
SITE 2 BC9 7 NAG D 672 HOH D4013 HOH D4295
SITE 1 CC1 2 ARG D 202 NAG D 671
SITE 1 CC2 4 GLN D 392 ASN D 396 SER D 398 ILE D 399
SITE 1 CC3 11 LYS C 166 ARG C 170 ARG C 171 ARG C 424
SITE 2 CC3 11 GLU C 472 GLU C 476 GLU D 165 ARG D 170
SITE 3 CC3 11 ARG D 171 ILE D 428 GLN D 431
SITE 1 CC4 10 ARG D 106 VAL D 335 TYR D 341 LEU D 345
SITE 2 CC4 10 TRP D 373 PHE D 504 VAL D 509 GLY D 512
SITE 3 CC4 10 ALA D 513 LEU D 517
CRYST1 180.268 134.273 122.615 90.00 90.00 90.00 P 21 21 2 16
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 0.005547 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007448 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008156 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
