HEADER OXIDOREDUCTASE 03-JUL-10 3NTB
TITLE STRUCTURE OF 6-METHYLTHIO NAPROXEN ANALOG BOUND TO MCOX-2.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 18-604, CATALYTIC DOMAIN;
COMPND 5 EC: 1.14.99.1;
COMPND 6 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 PGHS-B, MCG_5001, PTGS2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROSTAGLANDIN H2 SYNTHASE, CYCLOOXYGEANSE-2, NAPROXEN ANALOG,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.C.DUGGAN,J.MUSEE,M.J.WALTERS,J.M.HARP,J.R.KIEFER,J.A.OATES,
AUTHOR 2 L.J.MARNETT
REVDAT 2 17-NOV-10 3NTB 1 JRNL
REVDAT 1 01-SEP-10 3NTB 0
JRNL AUTH K.C.DUGGAN,M.J.WALTERS,J.MUSEE,J.M.HARP,J.R.KIEFER,
JRNL AUTH 2 J.A.OATES,L.J.MARNETT
JRNL TITL MOLECULAR BASIS FOR CYCLOOXYGENASE INHIBITION BY THE
JRNL TITL 2 NON-STEROIDAL ANTI-INFLAMMATORY DRUG NAPROXEN.
JRNL REF J.BIOL.CHEM. V. 285 34950 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20810665
JRNL DOI 10.1074/JBC.M110.162982
REMARK 2
REMARK 2 RESOLUTION. 2.27 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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 121009
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13517
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) : 2.27
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8277
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 903
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17887
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 640
REMARK 3 SOLVENT ATOMS : 1109
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.04000
REMARK 3 B22 (A**2) : 3.93000
REMARK 3 B33 (A**2) : 3.11000
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): 0.372
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.253
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.946
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19109 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 25994 ; 0.923 ; 2.011
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2203 ; 4.350 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 895 ;35.776 ;24.101
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3102 ;12.967 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;12.904 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2765 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14532 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 11029 ; 0.127 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17924 ; 0.251 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8080 ; 0.476 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8070 ; 0.903 ; 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 33 A 583
REMARK 3 ORIGIN FOR THE GROUP (A): -56.0870 38.1550 -8.9610
REMARK 3 T TENSOR
REMARK 3 T11: 0.3264 T22: 0.0387
REMARK 3 T33: 0.0198 T12: -0.0074
REMARK 3 T13: -0.0163 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.4879 L22: 0.9510
REMARK 3 L33: 1.1061 L12: 0.1895
REMARK 3 L13: 0.3877 L23: 0.6038
REMARK 3 S TENSOR
REMARK 3 S11: -0.0242 S12: 0.0091 S13: 0.2332
REMARK 3 S21: -0.0238 S22: -0.0921 S23: 0.1439
REMARK 3 S31: -0.0117 S32: -0.1470 S33: 0.1163
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 33 B 583
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6540 45.8870 -2.4240
REMARK 3 T TENSOR
REMARK 3 T11: 0.3175 T22: 0.1414
REMARK 3 T33: 0.0372 T12: -0.0237
REMARK 3 T13: -0.0057 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 1.4821 L22: 0.7908
REMARK 3 L33: 1.2981 L12: 0.1648
REMARK 3 L13: 0.0893 L23: 0.5717
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: 0.2356 S13: 0.0606
REMARK 3 S21: -0.0744 S22: 0.1062 S23: -0.1175
REMARK 3 S31: -0.0574 S32: 0.3778 S33: -0.0647
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 33 C 583
REMARK 3 ORIGIN FOR THE GROUP (A): -67.3610 21.8430 -63.3420
REMARK 3 T TENSOR
REMARK 3 T11: 0.3343 T22: 0.0595
REMARK 3 T33: -0.0034 T12: -0.0059
REMARK 3 T13: 0.0065 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 1.2574 L22: 0.6018
REMARK 3 L33: 1.0506 L12: 0.0152
REMARK 3 L13: 0.0754 L23: -0.4650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0154 S12: 0.1523 S13: -0.0183
REMARK 3 S21: -0.0366 S22: 0.0468 S23: 0.0667
REMARK 3 S31: 0.0111 S32: -0.2437 S33: -0.0314
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 33 D 583
REMARK 3 ORIGIN FOR THE GROUP (A): -28.8050 28.5340 -70.3040
REMARK 3 T TENSOR
REMARK 3 T11: 0.3330 T22: 0.0180
REMARK 3 T33: -0.0064 T12: -0.0064
REMARK 3 T13: 0.0067 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 1.3254 L22: 0.8668
REMARK 3 L33: 0.8917 L12: 0.0627
REMARK 3 L13: -0.1776 L23: -0.4364
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: 0.0535 S13: -0.1311
REMARK 3 S21: -0.0124 S22: -0.0588 S23: -0.1049
REMARK 3 S31: 0.0051 S32: 0.1291 S33: 0.0615
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 3NTB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 136496
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 20.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MMP550, MGCL2, PH 8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291.15K
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 90.59850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.11250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 90.59850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.11250
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 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: 12500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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: 12360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 584
REMARK 465 PRO A 585
REMARK 465 GLN A 586
REMARK 465 PRO A 587
REMARK 465 THR A 588
REMARK 465 LYS A 589
REMARK 465 THR A 590
REMARK 465 ALA A 591
REMARK 465 THR A 592
REMARK 465 ILE A 593
REMARK 465 ASN A 594
REMARK 465 ALA A 595
REMARK 465 SER A 596
REMARK 465 ALA A 597
REMARK 465 SER A 598
REMARK 465 HIS A 599
REMARK 465 SER A 600
REMARK 465 ARG A 601
REMARK 465 LEU A 602
REMARK 465 ASP A 603
REMARK 465 ASP A 604
REMARK 465 ILE A 605
REMARK 465 ASN A 606
REMARK 465 PRO A 607
REMARK 465 THR A 608
REMARK 465 VAL A 609
REMARK 465 LEU A 610
REMARK 465 ILE A 611
REMARK 465 LYS A 612
REMARK 465 ARG A 613
REMARK 465 ARG A 614
REMARK 465 SER A 615
REMARK 465 THR A 616
REMARK 465 GLU A 617
REMARK 465 LEU A 618
REMARK 465 GLN B 583
REMARK 465 ASP B 584
REMARK 465 PRO B 585
REMARK 465 GLN B 586
REMARK 465 PRO B 587
REMARK 465 THR B 588
REMARK 465 LYS B 589
REMARK 465 THR B 590
REMARK 465 ALA B 591
REMARK 465 THR B 592
REMARK 465 ILE B 593
REMARK 465 ASN B 594
REMARK 465 ALA B 595
REMARK 465 SER B 596
REMARK 465 ALA B 597
REMARK 465 SER B 598
REMARK 465 HIS B 599
REMARK 465 SER B 600
REMARK 465 ARG B 601
REMARK 465 LEU B 602
REMARK 465 ASP B 603
REMARK 465 ASP B 604
REMARK 465 ILE B 605
REMARK 465 ASN B 606
REMARK 465 PRO B 607
REMARK 465 THR B 608
REMARK 465 VAL B 609
REMARK 465 LEU B 610
REMARK 465 ILE B 611
REMARK 465 LYS B 612
REMARK 465 ARG B 613
REMARK 465 ARG B 614
REMARK 465 SER B 615
REMARK 465 THR B 616
REMARK 465 GLU B 617
REMARK 465 LEU B 618
REMARK 465 ASP C 584
REMARK 465 PRO C 585
REMARK 465 GLN C 586
REMARK 465 PRO C 587
REMARK 465 THR C 588
REMARK 465 LYS C 589
REMARK 465 THR C 590
REMARK 465 ALA C 591
REMARK 465 THR C 592
REMARK 465 ILE C 593
REMARK 465 ASN C 594
REMARK 465 ALA C 595
REMARK 465 SER C 596
REMARK 465 ALA C 597
REMARK 465 SER C 598
REMARK 465 HIS C 599
REMARK 465 SER C 600
REMARK 465 ARG C 601
REMARK 465 LEU C 602
REMARK 465 ASP C 603
REMARK 465 ASP C 604
REMARK 465 ILE C 605
REMARK 465 ASN C 606
REMARK 465 PRO C 607
REMARK 465 THR C 608
REMARK 465 VAL C 609
REMARK 465 LEU C 610
REMARK 465 ILE C 611
REMARK 465 LYS C 612
REMARK 465 ARG C 613
REMARK 465 ARG C 614
REMARK 465 SER C 615
REMARK 465 THR C 616
REMARK 465 GLU C 617
REMARK 465 LEU C 618
REMARK 465 ASP D 584
REMARK 465 PRO D 585
REMARK 465 GLN D 586
REMARK 465 PRO D 587
REMARK 465 THR D 588
REMARK 465 LYS D 589
REMARK 465 THR D 590
REMARK 465 ALA D 591
REMARK 465 THR D 592
REMARK 465 ILE D 593
REMARK 465 ASN D 594
REMARK 465 ALA D 595
REMARK 465 SER D 596
REMARK 465 ALA D 597
REMARK 465 SER D 598
REMARK 465 HIS D 599
REMARK 465 SER D 600
REMARK 465 ARG D 601
REMARK 465 LEU D 602
REMARK 465 ASP D 603
REMARK 465 ASP D 604
REMARK 465 ILE D 605
REMARK 465 ASN D 606
REMARK 465 PRO D 607
REMARK 465 THR D 608
REMARK 465 VAL D 609
REMARK 465 LEU D 610
REMARK 465 ILE D 611
REMARK 465 LYS D 612
REMARK 465 ARG D 613
REMARK 465 ARG D 614
REMARK 465 SER D 615
REMARK 465 THR D 616
REMARK 465 GLU D 617
REMARK 465 LEU D 618
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN B 410 C2 NAG B 681 2.17
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 ARG A 61 18.28 58.96
REMARK 500 THR A 129 -89.69 -116.21
REMARK 500 ARG A 185 -70.09 -88.27
REMARK 500 ASP A 249 19.20 59.44
REMARK 500 TRP A 387 52.97 -98.81
REMARK 500 GLU A 398 -119.80 58.58
REMARK 500 SER A 496 -46.75 73.56
REMARK 500 CYS A 575 64.92 38.19
REMARK 500 THR B 129 -87.88 -120.31
REMARK 500 TRP B 387 54.34 -93.03
REMARK 500 GLU B 398 -113.16 59.63
REMARK 500 TYR B 409 6.84 50.27
REMARK 500 ASN B 439 10.04 -142.30
REMARK 500 SER B 496 -50.22 70.97
REMARK 500 THR C 129 -93.90 -117.26
REMARK 500 ARG C 185 -71.23 -97.62
REMARK 500 HIS C 386 71.25 -69.71
REMARK 500 TRP C 387 51.70 -91.06
REMARK 500 GLU C 398 -117.83 56.03
REMARK 500 TYR C 409 9.24 56.12
REMARK 500 ASN C 410 77.02 -105.38
REMARK 500 ASN C 439 11.43 -140.53
REMARK 500 SER C 496 -50.53 71.00
REMARK 500 THR D 129 -88.05 -117.56
REMARK 500 ARG D 185 -76.64 -92.59
REMARK 500 ASP D 347 -51.89 -127.62
REMARK 500 TRP D 387 50.58 -96.93
REMARK 500 GLU D 398 -117.17 57.12
REMARK 500 ASN D 410 77.51 -119.67
REMARK 500 SER D 496 -56.65 72.66
REMARK 500
REMARK 500 REMARK: NULL
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 C 619 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 388 NE2
REMARK 620 2 HEM C 619 NA 90.7
REMARK 620 3 HEM C 619 NB 88.7 89.0
REMARK 620 4 HEM C 619 NC 92.4 176.7 89.9
REMARK 620 5 HEM C 619 ND 90.9 90.5 179.3 90.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 619 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 HEM A 619 NA 90.7
REMARK 620 3 HEM A 619 NB 92.7 89.0
REMARK 620 4 HEM A 619 NC 91.8 177.3 89.9
REMARK 620 5 HEM A 619 ND 86.8 90.7 179.4 90.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 619 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 388 NE2
REMARK 620 2 HEM D 619 NA 92.0
REMARK 620 3 HEM D 619 NB 94.4 89.3
REMARK 620 4 HEM D 619 NC 90.6 177.4 90.1
REMARK 620 5 HEM D 619 ND 85.4 90.2 179.5 90.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 619 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388 NE2
REMARK 620 2 HEM B 619 NA 91.4
REMARK 620 3 HEM B 619 NB 94.9 89.8
REMARK 620 4 HEM B 619 NC 90.8 177.6 89.2
REMARK 620 5 HEM B 619 ND 84.8 89.5 179.2 91.5
REMARK 620 6 HOH B 19 O 167.6 77.6 90.8 100.3 89.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N C 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N D 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PGH RELATED DB: PDB
REMARK 900 COX-2:FLURBIPROFEN
REMARK 900 RELATED ID: 1PXX RELATED DB: PDB
REMARK 900 COX-2:DICLOFENAC
REMARK 900 RELATED ID: 1CQE RELATED DB: PDB
REMARK 900 COX-1:FLURBIPROFEN
REMARK 900 RELATED ID: 3NT1 RELATED DB: PDB
REMARK 900 COX-2:NAPROXEN
DBREF 3NTB A 33 618 UNP Q543K3 Q543K3_MOUSE 18 604
DBREF 3NTB B 33 618 UNP Q543K3 Q543K3_MOUSE 18 604
DBREF 3NTB C 33 618 UNP Q543K3 Q543K3_MOUSE 18 604
DBREF 3NTB D 33 618 UNP Q543K3 Q543K3_MOUSE 18 604
SEQRES 1 A 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 A 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 A 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 A 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 A 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 A 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 A 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 A 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 A 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 A 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 A 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 A 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 A 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 A 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 A 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 A 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 A 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 A 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 A 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 A 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 A 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 A 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 A 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 A 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 A 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 A 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 A 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 A 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 A 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 A 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 A 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 A 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 A 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 A 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 A 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 A 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 A 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 A 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 A 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 A 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 A 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 A 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 A 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 A 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 A 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 A 587 GLU LEU
SEQRES 1 B 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 B 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 B 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 B 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 B 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 B 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 B 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 B 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 B 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 B 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 B 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 B 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 B 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 B 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 B 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 B 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 B 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 B 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 B 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 B 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 B 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 B 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 B 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 B 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 B 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 B 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 B 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 B 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 B 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 B 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 B 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 B 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 B 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 B 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 B 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 B 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 B 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 B 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 B 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 B 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 B 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 B 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 B 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 B 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 B 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 B 587 GLU LEU
SEQRES 1 C 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 C 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 C 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 C 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 C 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 C 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 C 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 C 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 C 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 C 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 C 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 C 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 C 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 C 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 C 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 C 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 C 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 C 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 C 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 C 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 C 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 C 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 C 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 C 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 C 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 C 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 C 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 C 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 C 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 C 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 C 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 C 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 C 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 C 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 C 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 C 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 C 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 C 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 C 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 C 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 C 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 C 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 C 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 C 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 C 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 C 587 GLU LEU
SEQRES 1 D 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 D 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 D 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 D 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 D 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 D 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 D 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 D 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 D 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 D 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 D 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 D 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 D 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 D 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 D 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 D 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 D 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 D 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 D 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 D 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 D 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 D 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 D 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 D 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 D 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 D 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 D 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 D 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 D 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 D 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 D 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 D 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 D 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 D 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 D 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 D 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 D 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 D 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 D 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 D 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 D 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 D 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 D 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 D 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 D 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 D 587 GLU LEU
MODRES 3NTB ASN C 410 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN D 410 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN B 410 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN D 68 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN A 410 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN B 144 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN A 68 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN B 68 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN D 144 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN C 68 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN A 144 ASN GLYCOSYLATION SITE
MODRES 3NTB ASN C 144 ASN GLYCOSYLATION SITE
HET HEM A 619 43
HET NAG A 661 14
HET NAG A 671 14
HET NAG A 672 14
HET NAG A 673 14
HET NAG A 681 14
HET BOG A 703 20
HET T1N A 3 17
HET BOG A 7 20
HET HEM B 619 43
HET NAG B 661 14
HET NAG B 671 14
HET NAG B 672 14
HET NAG B 673 14
HET NAG B 681 14
HET T1N B 1 17
HET BOG B 6 20
HET HEM C 619 43
HET NAG C 661 14
HET NAG C 671 14
HET NAG C 672 14
HET NAG C 673 14
HET NAG C 681 14
HET T1N C 2 17
HET BOG C 5 20
HET HEM D 619 43
HET NAG D 661 14
HET NAG D 671 14
HET NAG D 672 14
HET NAG D 673 14
HET NAG D 681 14
HET BOG D 703 20
HET T1N D 4 17
HET BOG D 8 20
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BOG B-OCTYLGLUCOSIDE
HETNAM T1N (2S)-2-[6-(METHYLSULFANYL)NAPHTHALEN-2-YL]PROPANOIC
HETNAM 2 T1N ACID
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 NAG 20(C8 H15 N O6)
FORMUL 9 BOG 6(C14 H28 O6)
FORMUL 10 T1N 4(C14 H14 O2 S)
FORMUL 31 HOH *1109(H2 O)
HELIX 1 1 GLU A 73 LYS A 83 1 11
HELIX 2 2 THR A 85 HIS A 95 1 11
HELIX 3 3 PHE A 96 ASN A 104 1 9
HELIX 4 4 ILE A 105A TYR A 122 1 18
HELIX 5 5 SER A 138 ASN A 144 1 7
HELIX 6 6 ASP A 173 LEU A 182 1 10
HELIX 7 7 ASN A 195 HIS A 207 1 13
HELIX 8 8 LEU A 230 GLY A 235 1 6
HELIX 9 9 THR A 237 ARG A 245 1 9
HELIX 10 10 THR A 265 GLN A 270 1 6
HELIX 11 11 PRO A 280 GLN A 284 5 5
HELIX 12 12 VAL A 295 HIS A 320 1 26
HELIX 13 13 GLY A 324 ASP A 347 1 24
HELIX 14 14 ASP A 347 GLY A 354 1 8
HELIX 15 15 ASP A 362 PHE A 367 5 6
HELIX 16 16 ALA A 378 TYR A 385 1 8
HELIX 17 17 TRP A 387 LEU A 391 5 5
HELIX 18 18 SER A 403 LEU A 408 1 6
HELIX 19 19 ASN A 411 GLN A 429 1 19
HELIX 20 20 PRO A 441 ALA A 443 5 3
HELIX 21 21 VAL A 444 MET A 458 1 15
HELIX 22 22 SER A 462 PHE A 470 1 9
HELIX 23 23 SER A 477 GLY A 483 1 7
HELIX 24 24 LYS A 485 SER A 496 1 12
HELIX 25 25 ASP A 497 MET A 501 5 5
HELIX 26 26 GLU A 502 GLU A 510 1 9
HELIX 27 27 GLY A 519 GLY A 536 1 18
HELIX 28 28 ASN A 537 SER A 541 5 5
HELIX 29 29 LYS A 546 GLY A 551 5 6
HELIX 30 30 GLY A 552 THR A 561 1 10
HELIX 31 31 SER A 563 VAL A 572 1 10
HELIX 32 32 GLU B 73 LYS B 83 1 11
HELIX 33 33 THR B 85 THR B 94 1 10
HELIX 34 34 PHE B 96 ASN B 104 1 9
HELIX 35 35 ILE B 105A TYR B 122 1 18
HELIX 36 36 SER B 138 ASN B 144 1 7
HELIX 37 37 ASP B 173 LEU B 182 1 10
HELIX 38 38 ASN B 195 HIS B 207 1 13
HELIX 39 39 LEU B 230 GLY B 235 1 6
HELIX 40 40 THR B 237 ARG B 245 1 9
HELIX 41 41 THR B 265 GLN B 270 1 6
HELIX 42 42 PRO B 280 GLN B 284 5 5
HELIX 43 43 VAL B 295 HIS B 320 1 26
HELIX 44 44 GLY B 324 ASP B 347 1 24
HELIX 45 45 ASP B 347 GLY B 354 1 8
HELIX 46 46 ASP B 362 PHE B 367 5 6
HELIX 47 47 ALA B 378 TYR B 385 1 8
HELIX 48 48 HIS B 386 LEU B 391 5 6
HELIX 49 49 SER B 403 LEU B 408 1 6
HELIX 50 50 ASN B 411 GLY B 418 1 8
HELIX 51 51 GLY B 418 GLN B 429 1 12
HELIX 52 52 PRO B 441 ALA B 443 5 3
HELIX 53 53 VAL B 444 MET B 458 1 15
HELIX 54 54 SER B 462 PHE B 470 1 9
HELIX 55 55 SER B 477 GLY B 483 1 7
HELIX 56 56 LYS B 485 SER B 496 1 12
HELIX 57 57 ASP B 497 MET B 501 5 5
HELIX 58 58 GLU B 502 GLU B 510 1 9
HELIX 59 59 GLY B 519 GLY B 536 1 18
HELIX 60 60 ASN B 537 SER B 541 5 5
HELIX 61 61 LYS B 546 GLY B 551 5 6
HELIX 62 62 GLY B 552 THR B 561 1 10
HELIX 63 63 SER B 563 VAL B 572 1 10
HELIX 64 64 GLU C 73 LYS C 83 1 11
HELIX 65 65 THR C 85 THR C 94 1 10
HELIX 66 66 PHE C 96 ASN C 105 1 10
HELIX 67 67 ILE C 105A TYR C 122 1 18
HELIX 68 68 SER C 138 ASN C 144 1 7
HELIX 69 69 ASP C 173 LEU C 182 1 10
HELIX 70 70 ASN C 195 HIS C 207 1 13
HELIX 71 71 LEU C 230 GLY C 235 1 6
HELIX 72 72 THR C 237 ARG C 245 1 9
HELIX 73 73 THR C 265 GLN C 270 1 6
HELIX 74 74 PRO C 280 GLN C 284 5 5
HELIX 75 75 VAL C 291 LEU C 294 5 4
HELIX 76 76 VAL C 295 HIS C 320 1 26
HELIX 77 77 GLY C 324 ASP C 347 1 24
HELIX 78 78 ASP C 347 GLY C 354 1 8
HELIX 79 79 ASP C 362 PHE C 367 5 6
HELIX 80 80 ALA C 378 TYR C 385 1 8
HELIX 81 81 HIS C 386 LEU C 391 5 6
HELIX 82 82 SER C 403 LEU C 408 1 6
HELIX 83 83 ASN C 411 GLY C 418 1 8
HELIX 84 84 GLY C 418 GLN C 429 1 12
HELIX 85 85 PRO C 441 ALA C 443 5 3
HELIX 86 86 VAL C 444 MET C 458 1 15
HELIX 87 87 SER C 462 PHE C 470 1 9
HELIX 88 88 SER C 477 GLY C 483 1 7
HELIX 89 89 LYS C 485 SER C 496 1 12
HELIX 90 90 ASP C 497 MET C 501 5 5
HELIX 91 91 GLU C 502 GLU C 510 1 9
HELIX 92 92 GLY C 519 GLY C 536 1 18
HELIX 93 93 ASN C 537 SER C 541 5 5
HELIX 94 94 LYS C 546 GLY C 551 5 6
HELIX 95 95 GLY C 552 THR C 561 1 10
HELIX 96 96 SER C 563 VAL C 572 1 10
HELIX 97 97 ASN D 34 ASN D 39 5 6
HELIX 98 98 GLU D 73 LYS D 83 1 11
HELIX 99 99 THR D 85 HIS D 95 1 11
HELIX 100 100 PHE D 96 ASN D 105 1 10
HELIX 101 101 ILE D 105A TYR D 122 1 18
HELIX 102 102 SER D 138 ASN D 144 1 7
HELIX 103 103 ASP D 173 LEU D 182 1 10
HELIX 104 104 ASN D 195 HIS D 207 1 13
HELIX 105 105 LEU D 230 GLY D 235 1 6
HELIX 106 106 THR D 237 ARG D 245 1 9
HELIX 107 107 THR D 265 GLN D 270 1 6
HELIX 108 108 PRO D 280 GLN D 284 5 5
HELIX 109 109 VAL D 295 HIS D 320 1 26
HELIX 110 110 GLY D 324 ASP D 347 1 24
HELIX 111 111 ASP D 347 GLY D 354 1 8
HELIX 112 112 ASP D 362 PHE D 367 5 6
HELIX 113 113 ALA D 378 TYR D 385 1 8
HELIX 114 114 TRP D 387 LEU D 391 5 5
HELIX 115 115 SER D 403 LEU D 408 1 6
HELIX 116 116 ASN D 411 GLY D 418 1 8
HELIX 117 117 GLY D 418 GLN D 429 1 12
HELIX 118 118 PRO D 441 ALA D 443 5 3
HELIX 119 119 VAL D 444 MET D 458 1 15
HELIX 120 120 SER D 462 PHE D 470 1 9
HELIX 121 121 SER D 477 GLY D 483 1 7
HELIX 122 122 LYS D 485 SER D 496 1 12
HELIX 123 123 ASP D 497 MET D 501 5 5
HELIX 124 124 GLU D 502 GLU D 510 1 9
HELIX 125 125 GLY D 519 GLY D 536 1 18
HELIX 126 126 ASN D 537 SER D 541 5 5
HELIX 127 127 LYS D 546 GLY D 551 5 6
HELIX 128 128 GLY D 552 THR D 561 1 10
HELIX 129 129 SER D 563 VAL D 572 1 10
SHEET 1 A 2 GLU A 46 SER A 49 0
SHEET 2 A 2 TYR A 55 ASP A 58 -1 O ASP A 58 N GLU A 46
SHEET 1 B 2 PHE A 64 TYR A 65 0
SHEET 2 B 2 THR A 71 PRO A 72 -1 O THR A 71 N TYR 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 VAL A 256 0
SHEET 2 D 2 VAL A 261 TYR A 262 -1 O TYR A 262 N GLN A 255
SHEET 1 E 2 PHE A 395 ILE A 397 0
SHEET 2 E 2 GLN A 400 TYR A 402 -1 O TYR A 402 N PHE A 395
SHEET 1 F 2 GLU B 46 SER B 49 0
SHEET 2 F 2 TYR B 55 ASP B 58 -1 O LYS B 56 N MET B 48
SHEET 1 G 2 PHE B 64 TYR B 65 0
SHEET 2 G 2 THR B 71 PRO B 72 -1 O THR B 71 N TYR 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 ILE 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 ILE B 397 0
SHEET 2 J 2 GLN B 400 TYR B 402 -1 O TYR B 402 N PHE B 395
SHEET 1 K 2 GLU C 46 SER C 49 0
SHEET 2 K 2 TYR C 55 ASP C 58 -1 O ASP C 58 N GLU C 46
SHEET 1 L 2 PHE C 64 TYR C 65 0
SHEET 2 L 2 THR C 71 PRO C 72 -1 O THR C 71 N TYR C 65
SHEET 1 M 2 TYR C 130 ASN C 131 0
SHEET 2 M 2 THR C 149 ARG C 150 -1 O ARG C 150 N TYR C 130
SHEET 1 N 2 GLN C 255 ILE C 257 0
SHEET 2 N 2 GLU C 260 TYR C 262 -1 O TYR C 262 N GLN C 255
SHEET 1 O 2 PHE C 395 ILE C 397 0
SHEET 2 O 2 GLN C 400 TYR C 402 -1 O TYR C 402 N PHE C 395
SHEET 1 P 2 GLU D 46 SER D 49 0
SHEET 2 P 2 TYR D 55 ASP D 58 -1 O LYS D 56 N MET D 48
SHEET 1 Q 2 PHE D 64 TYR D 65 0
SHEET 2 Q 2 THR D 71 PRO D 72 -1 O THR D 71 N TYR D 65
SHEET 1 R 2 GLN D 255 ILE D 257 0
SHEET 2 R 2 GLU D 260 TYR D 262 -1 O TYR D 262 N GLN D 255
SHEET 1 S 2 PHE D 395 ILE D 397 0
SHEET 2 S 2 GLN D 400 TYR D 402 -1 O TYR D 402 N PHE D 395
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.04
SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.03
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.03
SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.04
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.04
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.04
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.03
SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.03
SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.04
SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.03
SSBOND 11 CYS C 36 CYS C 47 1555 1555 2.04
SSBOND 12 CYS C 37 CYS C 159 1555 1555 2.03
SSBOND 13 CYS C 41 CYS C 57 1555 1555 2.03
SSBOND 14 CYS C 59 CYS C 69 1555 1555 2.04
SSBOND 15 CYS C 569 CYS C 575 1555 1555 2.04
SSBOND 16 CYS D 36 CYS D 47 1555 1555 2.04
SSBOND 17 CYS D 37 CYS D 159 1555 1555 2.04
SSBOND 18 CYS D 41 CYS D 57 1555 1555 2.03
SSBOND 19 CYS D 59 CYS D 69 1555 1555 2.04
SSBOND 20 CYS D 569 CYS D 575 1555 1555 2.04
LINK ND2 ASN C 410 C1 NAG C 681 1555 1555 1.44
LINK ND2 ASN D 410 C1 NAG D 681 1555 1555 1.44
LINK ND2 ASN B 410 C1 NAG B 681 1555 1555 1.44
LINK ND2 ASN D 68 C1 NAG D 661 1555 1555 1.44
LINK ND2 ASN A 410 C1 NAG A 681 1555 1555 1.44
LINK ND2 ASN B 144 C1 NAG B 671 1555 1555 1.44
LINK ND2 ASN A 68 C1 NAG A 661 1555 1555 1.45
LINK ND2 ASN B 68 C1 NAG B 661 1555 1555 1.45
LINK ND2 ASN D 144 C1 NAG D 671 1555 1555 1.45
LINK ND2 ASN C 68 C1 NAG C 661 1555 1555 1.45
LINK ND2 ASN A 144 C1 NAG A 671 1555 1555 1.45
LINK ND2 ASN C 144 C1 NAG C 671 1555 1555 1.45
LINK O4 NAG C 671 C1 NAG C 672 1555 1555 1.45
LINK O4 NAG A 671 C1 NAG A 672 1555 1555 1.45
LINK O4 NAG D 671 C1 NAG D 672 1555 1555 1.45
LINK O4 NAG B 671 C1 NAG B 672 1555 1555 1.45
LINK O4 NAG B 672 C1 NAG B 673 1555 1555 1.45
LINK O4 NAG C 672 C1 NAG C 673 1555 1555 1.45
LINK O4 NAG D 672 C1 NAG D 673 1555 1555 1.45
LINK O4 NAG A 672 C1 NAG A 673 1555 1555 1.46
LINK NE2 HIS C 388 FE HEM C 619 1555 1555 2.18
LINK NE2 HIS A 388 FE HEM A 619 1555 1555 2.25
LINK NE2 HIS D 388 FE HEM D 619 1555 1555 2.30
LINK NE2 HIS B 388 FE HEM B 619 1555 1555 2.33
LINK FE HEM B 619 O HOH B 19 1555 1555 2.35
CISPEP 1 SER A 126 PRO A 127 0 -0.70
CISPEP 2 SER B 126 PRO B 127 0 -0.12
CISPEP 3 SER C 126 PRO C 127 0 0.25
CISPEP 4 SER D 126 PRO D 127 0 -0.72
SITE 1 AC1 17 HOH A 10 ALA A 199 PHE A 200 ALA A 202
SITE 2 AC1 17 GLN A 203 HIS A 207 PHE A 210 LYS A 211
SITE 3 AC1 17 THR A 212 HIS A 214 VAL A 295 ASN A 382
SITE 4 AC1 17 TYR A 385 HIS A 386 HIS A 388 LEU A 391
SITE 5 AC1 17 VAL A 447
SITE 1 AC2 5 TYR A 55 GLU A 67 ASN A 68 HOH A4050
SITE 2 AC2 5 HOH A4063
SITE 1 AC3 8 GLU A 140 ASN A 144 TYR A 147 ARG A 216
SITE 2 AC3 8 NAG A 672 HOH A4017 HOH A4298 HOH A4799
SITE 1 AC4 3 ARG A 216 NAG A 671 NAG A 673
SITE 1 AC5 2 NAG A 672 HOH A4059
SITE 1 AC6 4 GLN A 406 ASN A 410 SER A 412 ILE A 413
SITE 1 AC7 10 GLU A 179 ARG A 184 ARG A 185 ILE A 442
SITE 2 AC7 10 GLN A 445 ARG B 184 ARG B 185 ARG B 438
SITE 3 AC7 10 GLU B 486 GLU B 490
SITE 1 AC8 9 ARG A 120 VAL A 349 LEU A 352 TYR A 355
SITE 2 AC8 9 TYR A 385 TRP A 387 VAL A 523 ALA A 527
SITE 3 AC8 9 LEU A 531
SITE 1 AC9 5 LYS A 83 PRO A 84 VAL A 89 SER A 119
SITE 2 AC9 5 ARG A 120
SITE 1 BC1 16 HOH B 19 ALA B 199 ALA B 202 GLN B 203
SITE 2 BC1 16 HIS B 207 PHE B 210 THR B 212 HIS B 214
SITE 3 BC1 16 VAL B 295 ASN B 382 TYR B 385 HIS B 386
SITE 4 BC1 16 HIS B 388 LEU B 391 LEU B 408 VAL B 447
SITE 1 BC2 5 TYR B 55 GLU B 67 ASN B 68 HOH B4018
SITE 2 BC2 5 HOH B4422
SITE 1 BC3 7 GLU B 140 ASN B 144 TYR B 147 ARG B 216
SITE 2 BC3 7 NAG B 672 HOH B4045 HOH B4370
SITE 1 BC4 4 ASP A 239 ARG B 216 NAG B 671 NAG B 673
SITE 1 BC5 1 NAG B 672
SITE 1 BC6 6 TYR B 402 GLN B 406 TYR B 409 ASN B 410
SITE 2 BC6 6 ILE B 413 HOH B4700
SITE 1 BC7 9 ARG B 120 VAL B 349 TYR B 355 TYR B 385
SITE 2 BC7 9 TRP B 387 VAL B 523 GLY B 526 ALA B 527
SITE 3 BC7 9 LEU B 531
SITE 1 BC8 7 LYS B 83 PRO B 84 PRO B 86 TYR B 115
SITE 2 BC8 7 SER B 119 ARG B 120 LEU B 123
SITE 1 BC9 17 ALA C 199 PHE C 200 ALA C 202 GLN C 203
SITE 2 BC9 17 HIS C 207 PHE C 210 THR C 212 HIS C 214
SITE 3 BC9 17 VAL C 295 ASN C 382 TYR C 385 HIS C 386
SITE 4 BC9 17 HIS C 388 LEU C 391 LEU C 408 ALA C 450
SITE 5 BC9 17 HOH C4061
SITE 1 CC1 4 TYR C 55 GLU C 67 ASN C 68 HOH C4349
SITE 1 CC2 7 ASN C 144 TYR C 147 ARG C 216 NAG C 672
SITE 2 CC2 7 HOH C4085 HOH C4331 HOH C4974
SITE 1 CC3 3 ARG C 216 NAG C 671 NAG C 673
SITE 1 CC4 1 NAG C 672
SITE 1 CC5 6 TYR C 402 GLN C 406 ASN C 410 SER C 412
SITE 2 CC5 6 ILE C 413 HOH C4055
SITE 1 CC6 8 VAL C 116 ARG C 120 VAL C 349 TYR C 355
SITE 2 CC6 8 TYR C 385 TRP C 387 VAL C 523 ALA C 527
SITE 1 CC7 4 LYS C 83 PRO C 84 SER C 119 ARG C 120
SITE 1 CC8 16 ALA D 199 PHE D 200 ALA D 202 GLN D 203
SITE 2 CC8 16 HIS D 207 PHE D 210 LYS D 211 THR D 212
SITE 3 CC8 16 HIS D 214 VAL D 295 ASN D 382 TYR D 385
SITE 4 CC8 16 HIS D 386 HIS D 388 LEU D 391 LEU D 408
SITE 1 CC9 5 TYR D 55 GLU D 67 ASN D 68 HOH D 654
SITE 2 CC9 5 HOH D 689
SITE 1 DC1 9 LEU C 238 GLU D 140 ASN D 144 TYR D 147
SITE 2 DC1 9 ARG D 216 HOH D 640 NAG D 672 HOH D4013
SITE 3 DC1 9 HOH D4295
SITE 1 DC2 3 ARG D 216 NAG D 671 NAG D 673
SITE 1 DC3 1 NAG D 672
SITE 1 DC4 8 GLN D 406 ASN D 410 SER D 412 ILE D 413
SITE 2 DC4 8 GLU D 416 HOH D 670 HOH D 688 HOH D4821
SITE 1 DC5 11 GLU C 179 LYS C 180 ARG C 184 ARG C 185
SITE 2 DC5 11 ARG C 438 GLU C 486 GLU C 490 GLU D 179
SITE 3 DC5 11 ARG D 185 ILE D 442 GLN D 445
SITE 1 DC6 7 ARG D 120 VAL D 349 TYR D 355 TYR D 385
SITE 2 DC6 7 TRP D 387 ALA D 527 LEU D 531
SITE 1 DC7 7 LYS D 83 PRO D 84 PRO D 86 SER D 119
SITE 2 DC7 7 ARG D 120 LEU D 123 GLU D 524
CRYST1 181.197 134.225 121.990 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 0.005519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007450 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
