HEADER OXIDOREDUCTASE 01-FEB-10 3LN0
TITLE STRUCTURE OF COMPOUND 5C-S BOUND AT THE ACTIVE SITE OF COX-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND 5 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND 6 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND 7 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND 8 2;
COMPND 9 EC: 1.14.99.1;
COMPND 10 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, PGHS-B, PROSTAGLANDIN H2 SYNTHASE 2, PTGS2,
SOURCE 6 TIS10;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 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.R.KIEFER,R.G.KURUMBAIL,W.C.STALLINGS,J.L.PAWLITZ
REVDAT 3 29-JUL-20 3LN0 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 01-DEC-10 3LN0 1 JRNL
REVDAT 1 27-OCT-10 3LN0 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.5
REMARK 3 NUMBER OF REFLECTIONS : 115927
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12935
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7800
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 844
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17896
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 568
REMARK 3 SOLVENT ATOMS : 1147
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.27000
REMARK 3 B22 (A**2) : 1.73000
REMARK 3 B33 (A**2) : 0.53000
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): 0.366
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.916
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19047 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 13014 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 25931 ; 1.137 ; 2.008
REMARK 3 BOND ANGLES OTHERS (DEGREES): 31529 ; 0.780 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2203 ; 5.156 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 896 ;40.284 ;24.107
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3104 ;17.516 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;19.290 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2746 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20797 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3835 ; 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): 11035 ; 0.428 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4416 ; 0.080 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17933 ; 0.859 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8012 ; 1.381 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7998 ; 2.387 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 25 A 550 1
REMARK 3 1 B 25 B 550 1
REMARK 3 1 C 25 C 550 1
REMARK 3 1 D 25 D 550 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 7326 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 7326 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 7326 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 7326 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 7326 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 7326 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 7326 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 7326 ; 0.06 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 : 1.20
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 3LN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-00
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 : NULL
REMARK 200 OPTICS : NULL
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 : 144570
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 (%) : 93.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
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 (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 (%): 56.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
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 90.50750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.60050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 90.50750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.60050
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: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H
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 570
REMARK 465 PRO A 571
REMARK 465 GLN A 572
REMARK 465 PRO A 573
REMARK 465 THR A 574
REMARK 465 LYS A 575
REMARK 465 THR A 576
REMARK 465 ALA A 577
REMARK 465 THR A 578
REMARK 465 ILE A 579
REMARK 465 ASN A 580
REMARK 465 ALA A 581
REMARK 465 SER A 582
REMARK 465 ALA A 583
REMARK 465 SER A 584
REMARK 465 HIS A 585
REMARK 465 SER A 586
REMARK 465 ARG A 587
REMARK 465 LEU A 588
REMARK 465 ASP A 589
REMARK 465 ASP A 590
REMARK 465 ILE A 591
REMARK 465 ASN A 592
REMARK 465 PRO A 593
REMARK 465 THR A 594
REMARK 465 VAL A 595
REMARK 465 LEU A 596
REMARK 465 ILE A 597
REMARK 465 LYS A 598
REMARK 465 ARG A 599
REMARK 465 ARG A 600
REMARK 465 SER A 601
REMARK 465 THR A 602
REMARK 465 GLU A 603
REMARK 465 LEU A 604
REMARK 465 ASP B 570
REMARK 465 PRO B 571
REMARK 465 GLN B 572
REMARK 465 PRO B 573
REMARK 465 THR B 574
REMARK 465 LYS B 575
REMARK 465 THR B 576
REMARK 465 ALA B 577
REMARK 465 THR B 578
REMARK 465 ILE B 579
REMARK 465 ASN B 580
REMARK 465 ALA B 581
REMARK 465 SER B 582
REMARK 465 ALA B 583
REMARK 465 SER B 584
REMARK 465 HIS B 585
REMARK 465 SER B 586
REMARK 465 ARG B 587
REMARK 465 LEU B 588
REMARK 465 ASP B 589
REMARK 465 ASP B 590
REMARK 465 ILE B 591
REMARK 465 ASN B 592
REMARK 465 PRO B 593
REMARK 465 THR B 594
REMARK 465 VAL B 595
REMARK 465 LEU B 596
REMARK 465 ILE B 597
REMARK 465 LYS B 598
REMARK 465 ARG B 599
REMARK 465 ARG B 600
REMARK 465 SER B 601
REMARK 465 THR B 602
REMARK 465 GLU B 603
REMARK 465 LEU B 604
REMARK 465 ASP C 570
REMARK 465 PRO C 571
REMARK 465 GLN C 572
REMARK 465 PRO C 573
REMARK 465 THR C 574
REMARK 465 LYS C 575
REMARK 465 THR C 576
REMARK 465 ALA C 577
REMARK 465 THR C 578
REMARK 465 ILE C 579
REMARK 465 ASN C 580
REMARK 465 ALA C 581
REMARK 465 SER C 582
REMARK 465 ALA C 583
REMARK 465 SER C 584
REMARK 465 HIS C 585
REMARK 465 SER C 586
REMARK 465 ARG C 587
REMARK 465 LEU C 588
REMARK 465 ASP C 589
REMARK 465 ASP C 590
REMARK 465 ILE C 591
REMARK 465 ASN C 592
REMARK 465 PRO C 593
REMARK 465 THR C 594
REMARK 465 VAL C 595
REMARK 465 LEU C 596
REMARK 465 ILE C 597
REMARK 465 LYS C 598
REMARK 465 ARG C 599
REMARK 465 ARG C 600
REMARK 465 SER C 601
REMARK 465 THR C 602
REMARK 465 GLU C 603
REMARK 465 LEU C 604
REMARK 465 ASP D 570
REMARK 465 PRO D 571
REMARK 465 GLN D 572
REMARK 465 PRO D 573
REMARK 465 THR D 574
REMARK 465 LYS D 575
REMARK 465 THR D 576
REMARK 465 ALA D 577
REMARK 465 THR D 578
REMARK 465 ILE D 579
REMARK 465 ASN D 580
REMARK 465 ALA D 581
REMARK 465 SER D 582
REMARK 465 ALA D 583
REMARK 465 SER D 584
REMARK 465 HIS D 585
REMARK 465 SER D 586
REMARK 465 ARG D 587
REMARK 465 LEU D 588
REMARK 465 ASP D 589
REMARK 465 ASP D 590
REMARK 465 ILE D 591
REMARK 465 ASN D 592
REMARK 465 PRO D 593
REMARK 465 THR D 594
REMARK 465 VAL D 595
REMARK 465 LEU D 596
REMARK 465 ILE D 597
REMARK 465 LYS D 598
REMARK 465 ARG D 599
REMARK 465 ARG D 600
REMARK 465 SER D 601
REMARK 465 THR D 602
REMARK 465 GLU D 603
REMARK 465 LEU D 604
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 O HOH B 4867 O HOH B 4991 2.17
REMARK 500 O LEU C 109 NH2 ARG C 455 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 25 C - N - CA ANGL. DEV. = 9.2 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 PRO A 113 151.44 -49.87
REMARK 500 THR A 115 -89.64 -121.23
REMARK 500 ARG A 171 -69.23 -94.08
REMARK 500 ASP A 235 15.58 59.57
REMARK 500 TRP A 373 44.62 -97.63
REMARK 500 GLU A 384 -120.53 58.27
REMARK 500 TYR A 395 27.36 49.36
REMARK 500 SER A 482 -47.87 71.54
REMARK 500 ARG B 29 8.72 80.38
REMARK 500 ASP B 38 17.67 -140.28
REMARK 500 THR B 115 -91.06 -122.43
REMARK 500 ARG B 171 -72.65 -93.93
REMARK 500 TRP B 373 45.17 -95.57
REMARK 500 GLU B 384 -119.97 57.48
REMARK 500 TYR B 395 27.66 49.65
REMARK 500 SER B 482 -48.31 72.08
REMARK 500 ARG C 46 18.14 59.40
REMARK 500 THR C 115 -90.45 -121.64
REMARK 500 ARG C 171 -72.85 -94.24
REMARK 500 TRP C 373 43.51 -95.78
REMARK 500 GLU C 384 -121.16 56.98
REMARK 500 TYR C 395 28.54 48.77
REMARK 500 SER C 482 -47.63 72.02
REMARK 500 ARG D 29 7.74 80.08
REMARK 500 ASP D 38 17.46 -140.28
REMARK 500 PRO D 113 151.67 -49.87
REMARK 500 THR D 115 -89.62 -122.53
REMARK 500 ARG D 171 -67.93 -94.80
REMARK 500 ASP D 235 14.71 59.72
REMARK 500 TRP D 373 45.88 -96.04
REMARK 500 GLU D 384 -122.06 57.90
REMARK 500 TYR D 395 29.87 48.90
REMARK 500 SER D 482 -48.93 72.10
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 A 605 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 374 NE2
REMARK 620 2 HEM A 605 NA 94.7
REMARK 620 3 HEM A 605 NB 95.6 87.1
REMARK 620 4 HEM A 605 NC 96.1 168.7 88.4
REMARK 620 5 HEM A 605 ND 90.5 91.1 173.7 92.3
REMARK 620 6 HOH A4121 O 176.3 88.8 83.3 80.4 90.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 605 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 374 NE2
REMARK 620 2 HEM B 605 NA 95.9
REMARK 620 3 HEM B 605 NB 93.7 86.9
REMARK 620 4 HEM B 605 NC 94.3 169.5 89.8
REMARK 620 5 HEM B 605 ND 92.4 89.6 173.2 92.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 605 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 374 NE2
REMARK 620 2 HEM C 605 NA 93.7
REMARK 620 3 HEM C 605 NB 91.7 87.8
REMARK 620 4 HEM C 605 NC 93.6 172.3 89.4
REMARK 620 5 HEM C 605 ND 91.6 90.7 176.5 91.6
REMARK 620 6 HOH C4116 O 177.7 87.9 90.0 84.8 86.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 605 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 374 NE2
REMARK 620 2 HEM D 605 NA 93.2
REMARK 620 3 HEM D 605 NB 95.6 83.9
REMARK 620 4 HEM D 605 NC 98.0 168.1 91.2
REMARK 620 5 HEM D 605 ND 90.3 92.2 173.1 91.6
REMARK 620 6 HOH D4018 O 174.2 81.4 81.8 87.2 92.0
REMARK 620 N 1 2 3 4 5
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE INHIBITOR
REMARK 630 MOLECULE NAME: 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 NAG A 661
REMARK 630 NAG A 681
REMARK 630 NAG B 661
REMARK 630 NAG B 681
REMARK 630 NAG C 661
REMARK 630 NAG C 681
REMARK 630 NAG D 661
REMARK 630 NAG D 681
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
DBREF 3LN0 A 18 604 UNP Q05769 PGH2_MOUSE 18 604
DBREF 3LN0 B 18 604 UNP Q05769 PGH2_MOUSE 18 604
DBREF 3LN0 C 18 604 UNP Q05769 PGH2_MOUSE 18 604
DBREF 3LN0 D 18 604 UNP Q05769 PGH2_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 3LN0 ASN B 396 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN A 53 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN D 396 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN A 396 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN C 396 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN B 53 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN D 53 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN A 130 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN C 53 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN B 130 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN D 130 ASN GLYCOSYLATION SITE
MODRES 3LN0 ASN C 130 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET NAG E 3 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG F 3 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG G 3 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG H 3 14
HET HEM A 605 43
HET NAG A 661 14
HET NAG A 681 14
HET 52B A 701 19
HET BOG A 703 20
HET HEM B 605 43
HET NAG B 661 14
HET NAG B 681 14
HET 52B B 701 19
HET HEM C 605 43
HET NAG C 661 14
HET NAG C 681 14
HET 52B C 701 19
HET HEM D 605 43
HET NAG D 661 14
HET NAG D 681 14
HET BOG D 703 20
HET 52B D 701 19
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 52B (2S)-6,8-DICHLORO-2-(TRIFLUOROMETHYL)-2H-CHROMENE-3-
HETNAM 2 52B CARBOXYLIC ACID
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETSYN HEM HEME
FORMUL 5 NAG 20(C8 H15 N O6)
FORMUL 9 HEM 4(C34 H32 FE N4 O4)
FORMUL 12 52B 4(C11 H5 CL2 F3 O3)
FORMUL 13 BOG 2(C14 H28 O6)
FORMUL 27 HOH *1147(H2 O)
HELIX 1 1 GLU A 58 LEU A 67 1 10
HELIX 2 2 THR A 70 THR A 79 1 10
HELIX 3 3 PHE A 81 ASN A 89 1 9
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 GLN A 415 1 19
HELIX 21 21 PRO A 427 ALA A 429 5 3
HELIX 22 22 VAL A 430 MET A 444 1 15
HELIX 23 23 SER A 448 PHE A 456 1 9
HELIX 24 24 SER A 463 GLY A 469 1 7
HELIX 25 25 LYS A 471 SER A 482 1 12
HELIX 26 26 ASP A 483 MET A 487 5 5
HELIX 27 27 GLU A 488 GLU A 496 1 9
HELIX 28 28 GLY A 505 GLY A 522 1 18
HELIX 29 29 ASN A 523 SER A 527 5 5
HELIX 30 30 LYS A 532 GLY A 537 5 6
HELIX 31 31 GLY A 538 THR A 547 1 10
HELIX 32 32 SER A 549 VAL A 558 1 10
HELIX 33 33 GLU B 58 LEU B 67 1 10
HELIX 34 34 THR B 70 THR B 79 1 10
HELIX 35 35 PHE B 81 ASN B 89 1 9
HELIX 36 36 ILE B 91 TYR B 108 1 18
HELIX 37 37 SER B 124 ASN B 130 1 7
HELIX 38 38 ASP B 159 LEU B 168 1 10
HELIX 39 39 ASN B 181 HIS B 193 1 13
HELIX 40 40 LEU B 216 GLY B 221 1 6
HELIX 41 41 THR B 223 ARG B 231 1 9
HELIX 42 42 THR B 251 GLN B 256 1 6
HELIX 43 43 PRO B 266 GLN B 270 5 5
HELIX 44 44 VAL B 277 LEU B 280 5 4
HELIX 45 45 VAL B 281 HIS B 306 1 26
HELIX 46 46 GLY B 310 ASP B 333 1 24
HELIX 47 47 ASP B 333 GLY B 340 1 8
HELIX 48 48 ASP B 348 PHE B 353 5 6
HELIX 49 49 ALA B 364 TYR B 371 1 8
HELIX 50 50 TRP B 373 LEU B 377 5 5
HELIX 51 51 SER B 389 LEU B 394 1 6
HELIX 52 52 ASN B 396 GLN B 415 1 20
HELIX 53 53 PRO B 427 ALA B 429 5 3
HELIX 54 54 VAL B 430 MET B 444 1 15
HELIX 55 55 SER B 448 PHE B 456 1 9
HELIX 56 56 SER B 463 GLY B 469 1 7
HELIX 57 57 LYS B 471 SER B 482 1 12
HELIX 58 58 ASP B 483 MET B 487 5 5
HELIX 59 59 GLU B 488 GLU B 496 1 9
HELIX 60 60 GLY B 505 GLY B 522 1 18
HELIX 61 61 ASN B 523 SER B 527 5 5
HELIX 62 62 LYS B 532 GLY B 537 5 6
HELIX 63 63 GLY B 538 THR B 547 1 10
HELIX 64 64 SER B 549 VAL B 558 1 10
HELIX 65 65 GLU C 58 LEU C 67 1 10
HELIX 66 66 THR C 70 THR C 79 1 10
HELIX 67 67 PHE C 81 ASN C 89 1 9
HELIX 68 68 ILE C 91 TYR C 108 1 18
HELIX 69 69 SER C 124 ASN C 130 1 7
HELIX 70 70 ASP C 159 LEU C 168 1 10
HELIX 71 71 ASN C 181 HIS C 193 1 13
HELIX 72 72 LEU C 216 GLY C 221 1 6
HELIX 73 73 THR C 223 ARG C 231 1 9
HELIX 74 74 THR C 251 GLN C 256 1 6
HELIX 75 75 PRO C 266 GLN C 270 5 5
HELIX 76 76 VAL C 281 HIS C 306 1 26
HELIX 77 77 GLY C 310 ASP C 333 1 24
HELIX 78 78 ASP C 333 GLY C 340 1 8
HELIX 79 79 ASP C 348 PHE C 353 5 6
HELIX 80 80 ALA C 364 TYR C 371 1 8
HELIX 81 81 TRP C 373 LEU C 377 5 5
HELIX 82 82 SER C 389 LEU C 394 1 6
HELIX 83 83 ASN C 397 GLN C 415 1 19
HELIX 84 84 PRO C 427 ALA C 429 5 3
HELIX 85 85 VAL C 430 MET C 444 1 15
HELIX 86 86 SER C 448 PHE C 456 1 9
HELIX 87 87 SER C 463 GLY C 469 1 7
HELIX 88 88 LYS C 471 SER C 482 1 12
HELIX 89 89 ASP C 483 MET C 487 5 5
HELIX 90 90 GLU C 488 GLU C 496 1 9
HELIX 91 91 GLY C 505 GLY C 522 1 18
HELIX 92 92 ASN C 523 SER C 527 5 5
HELIX 93 93 LYS C 532 GLY C 537 5 6
HELIX 94 94 GLY C 538 THR C 547 1 10
HELIX 95 95 SER C 549 VAL C 558 1 10
HELIX 96 96 GLU D 58 LEU D 67 1 10
HELIX 97 97 THR D 70 THR D 79 1 10
HELIX 98 98 PHE D 81 ASN D 89 1 9
HELIX 99 99 ILE D 91 TYR D 108 1 18
HELIX 100 100 SER D 124 ASN D 130 1 7
HELIX 101 101 ASP D 159 LEU D 168 1 10
HELIX 102 102 ASN D 181 HIS D 193 1 13
HELIX 103 103 LEU D 216 GLY D 221 1 6
HELIX 104 104 THR D 223 ARG D 231 1 9
HELIX 105 105 THR D 251 GLN D 256 1 6
HELIX 106 106 PRO D 266 GLN D 270 5 5
HELIX 107 107 VAL D 277 LEU D 280 5 4
HELIX 108 108 VAL D 281 HIS D 306 1 26
HELIX 109 109 GLY D 310 ASP D 333 1 24
HELIX 110 110 ASP D 333 GLY D 340 1 8
HELIX 111 111 ASP D 348 PHE D 353 5 6
HELIX 112 112 ALA D 364 TYR D 371 1 8
HELIX 113 113 HIS D 372 LEU D 377 5 6
HELIX 114 114 SER D 389 LEU D 394 1 6
HELIX 115 115 ASN D 396 GLN D 415 1 20
HELIX 116 116 PRO D 427 ALA D 429 5 3
HELIX 117 117 VAL D 430 MET D 444 1 15
HELIX 118 118 SER D 448 PHE D 456 1 9
HELIX 119 119 SER D 463 GLY D 469 1 7
HELIX 120 120 LYS D 471 SER D 482 1 12
HELIX 121 121 ASP D 483 MET D 487 5 5
HELIX 122 122 GLU D 488 GLU D 496 1 9
HELIX 123 123 GLY D 505 GLY D 522 1 18
HELIX 124 124 ASN D 523 SER D 527 5 5
HELIX 125 125 LYS D 532 GLY D 537 5 6
HELIX 126 126 GLY D 538 THR D 547 1 10
HELIX 127 127 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 SER B 34 0
SHEET 2 F 2 TYR B 40 ASP B 43 -1 O LYS B 41 N MET B 33
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 GLN B 241 ILE B 243 0
SHEET 2 H 2 GLU B 246 TYR B 248 -1 O TYR B 248 N GLN B 241
SHEET 1 I 2 PHE B 381 ILE B 383 0
SHEET 2 I 2 GLN B 386 TYR B 388 -1 O TYR B 388 N PHE B 381
SHEET 1 J 2 GLU C 31 SER C 34 0
SHEET 2 J 2 TYR C 40 ASP C 43 -1 O ASP C 43 N GLU C 31
SHEET 1 K 2 PHE C 49 TYR C 50 0
SHEET 2 K 2 THR C 56 PRO C 57 -1 O THR C 56 N TYR C 50
SHEET 1 L 2 GLN C 241 ILE C 243 0
SHEET 2 L 2 GLU C 246 TYR C 248 -1 O TYR C 248 N GLN C 241
SHEET 1 M 2 PHE C 381 ILE C 383 0
SHEET 2 M 2 GLN C 386 TYR C 388 -1 O TYR C 388 N PHE C 381
SHEET 1 N 2 GLU D 31 SER D 34 0
SHEET 2 N 2 TYR D 40 ASP D 43 -1 O ASP D 43 N GLU D 31
SHEET 1 O 2 PHE D 49 TYR D 50 0
SHEET 2 O 2 THR D 56 PRO D 57 -1 O THR D 56 N TYR D 50
SHEET 1 P 2 GLN D 241 ILE D 243 0
SHEET 2 P 2 GLU D 246 TYR D 248 -1 O TYR D 248 N GLN D 241
SHEET 1 Q 2 PHE D 381 ILE D 383 0
SHEET 2 Q 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 2.04
SSBOND 2 CYS A 22 CYS A 145 1555 1555 2.04
SSBOND 3 CYS A 26 CYS A 42 1555 1555 2.04
SSBOND 4 CYS A 44 CYS A 54 1555 1555 2.05
SSBOND 5 CYS A 555 CYS A 561 1555 1555 2.05
SSBOND 6 CYS B 21 CYS B 32 1555 1555 2.03
SSBOND 7 CYS B 22 CYS B 145 1555 1555 2.04
SSBOND 8 CYS B 26 CYS B 42 1555 1555 2.04
SSBOND 9 CYS B 44 CYS B 54 1555 1555 2.05
SSBOND 10 CYS B 555 CYS B 561 1555 1555 2.06
SSBOND 11 CYS C 21 CYS C 32 1555 1555 2.04
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 2.07
SSBOND 16 CYS D 21 CYS D 32 1555 1555 2.05
SSBOND 17 CYS D 22 CYS D 145 1555 1555 2.05
SSBOND 18 CYS D 26 CYS D 42 1555 1555 2.04
SSBOND 19 CYS D 44 CYS D 54 1555 1555 2.04
SSBOND 20 CYS D 555 CYS D 561 1555 1555 2.04
LINK ND2 ASN A 53 C1 NAG A 661 1555 1555 1.43
LINK ND2 ASN A 130 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 396 C1 NAG A 681 1555 1555 1.44
LINK ND2 ASN B 53 C1 NAG B 661 1555 1555 1.44
LINK ND2 ASN B 130 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN B 396 C1 NAG B 681 1555 1555 1.43
LINK ND2 ASN C 53 C1 NAG C 661 1555 1555 1.45
LINK ND2 ASN C 130 C1 NAG G 1 1555 1555 1.46
LINK ND2 ASN C 396 C1 NAG C 681 1555 1555 1.44
LINK ND2 ASN D 53 C1 NAG D 661 1555 1555 1.44
LINK ND2 ASN D 130 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN D 396 C1 NAG D 681 1555 1555 1.43
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 NAG E 3 1555 1555 1.46
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG F 2 C1 NAG F 3 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG G 2 C1 NAG G 3 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG H 2 C1 NAG H 3 1555 1555 1.45
LINK NE2 HIS A 374 FE HEM A 605 1555 1555 2.07
LINK FE HEM A 605 O HOH A4121 1555 1555 2.28
LINK NE2 HIS B 374 FE HEM B 605 1555 1555 2.17
LINK NE2 HIS C 374 FE HEM C 605 1555 1555 2.20
LINK FE HEM C 605 O HOH C4116 1555 1555 2.09
LINK NE2 HIS D 374 FE HEM D 605 1555 1555 2.08
LINK FE HEM D 605 O HOH D4018 1555 1555 2.39
CISPEP 1 SER A 112 PRO A 113 0 -0.82
CISPEP 2 SER B 112 PRO B 113 0 -0.30
CISPEP 3 SER C 112 PRO C 113 0 0.90
CISPEP 4 SER D 112 PRO D 113 0 -0.63
CRYST1 181.015 135.201 124.291 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 0.005524 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007396 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008046 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
