HEADER OXIDOREDUCTASE 15-NOV-99 1QOM
TITLE MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH
TITLE 2 SWAPPED N-TERMINAL HOOK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: OXYGENASE DOMAIN, RESIDUES 65-498;
COMPND 5 EC: 1.14.13.39;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: MURINE INDUCIBLE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL: MACROPHAGE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS OXIDOREDUCTASE, NITRIC OXIDE MONOOXYGENASE, HEME, DIMER, NOS, SWAPPED
KEYWDS 2 N- TERMINAL HOOK, DISULFIDE (OXIDOREDUCTASE/SUBSTRATE)
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.CRANE,R.A.ROSENFELD,A.S.ARVAI,J.A.TAINER,D.J.STUEHR,E.D.GETZOFF
REVDAT 6 09-OCT-19 1QOM 1 REMARK
REVDAT 5 16-JUN-09 1QOM 1 REMARK
REVDAT 4 24-FEB-09 1QOM 1 VERSN
REVDAT 3 30-APR-00 1QOM 1 REMARK
REVDAT 2 10-APR-00 1QOM 1 REMARK
REVDAT 1 15-DEC-99 1QOM 0
JRNL AUTH B.R.CRANE,R.A.ROSENFELD,A.S.ARVAI,D.K.GHOSH,S.GHOSH,
JRNL AUTH 2 J.A.TAINER,D.J.STUEHR,E.D.GETZOFF
JRNL TITL N-TERMINAL DOMAIN SWAPPING AND METAL ION BINDING IN NITRIC
JRNL TITL 2 OXIDE SYNTHASE DIMERIZATION
JRNL REF EMBO J. V. 18 6271 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10562539
JRNL DOI 10.1093/EMBOJ/18.22.6271
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.K.GHOSH,B.R.CRANE,S.GHOSH,D.WOLAN,R.GACHHUI,C.CROOKS,
REMARK 1 AUTH 2 A.PRESTA,J.A.TAINER,E.D.GETZOFF,D.J.STUEHR
REMARK 1 TITL INDUCIBLE NITRIC OXIDE SYNTHASE: ROLE OF THE N-TERMINAL
REMARK 1 TITL 2 BETA-HAIRPIN HOOK AND PTERIN-BINDING SEGMENT IN DIMERIZATION
REMARK 1 TITL 3 AND TETRAHYDROBIOPTERIN INTERACTION
REMARK 1 REF EMBO J. V. 18 6260 1999
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 10562538
REMARK 1 DOI 10.1093/EMBOJ/18.22.6260
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.R.CRANE,A.S.ARVAI,D.K.GHOSH,C.WU,E.D.GETZOFF,D.J.STUEHR,
REMARK 1 AUTH 2 J.A.TAINER
REMARK 1 TITL STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DIMER WITH
REMARK 1 TITL 2 PTERIN AND SUBSTRATE
REMARK 1 REF SCIENCE V. 279 2121 1998
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 9516116
REMARK 1 DOI 10.1126/SCIENCE.279.5359.2121
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.R.CRANE,A.S.ARVAI,R.GACHHUI,C.WU,D.K.GHOSH,E.D.GETZOFF,
REMARK 1 AUTH 2 D.J.STUEHR,J.A.TAINER
REMARK 1 TITL THE STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN AND
REMARK 1 TITL 2 INHIBITOR COMPLEXES
REMARK 1 REF SCIENCE V. 278 425 1997
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 9334294
REMARK 1 DOI 10.1126/SCIENCE.278.5337.425
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 11313090.240
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 39200
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 SET) : 0.236
REMARK 3 FREE R VALUE : 0.306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1967
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6096
REMARK 3 BIN R VALUE (WORKING SET) : 0.3850
REMARK 3 BIN FREE R VALUE : 0.4360
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 329
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6848
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 394
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -22.73000
REMARK 3 B22 (A**2) : -22.73000
REMARK 3 B33 (A**2) : 45.46000
REMARK 3 B12 (A**2) : -7.37000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.66
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.74
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.210
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.840 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.640 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.830 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.720 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.04 ; 100
REMARK 3 GROUP 1 B-FACTOR (A**2) : 2.1 ; 0.95
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.
REMARK 3 TOPOLOGY FILE 2 : TOPH19X.H
REMARK 3 TOPOLOGY FILE 3 : TOPH19X.H
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QOM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1290004363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-97
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : PT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39200
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.00, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.06667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.13333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.10000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 95.16667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.03333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 38.06667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 76.13333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 95.16667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 57.10000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 19.03333
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 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -1.000000 0.000000 0.000000 212.98000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 57.10000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -0.500000 -0.866025 0.000000 319.47000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 184.44609
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 190.33333
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2148 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2170 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2080 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2163 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2185 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2186 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 PROTEIN WAS EXPRESSED WITH A COOH-TERMINAL HIS6 TAG.
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 SER A 65
REMARK 465 LEU A 66
REMARK 465 ASP A 67
REMARK 465 LYS A 68
REMARK 465 LEU A 69
REMARK 465 HIS A 70
REMARK 465 VAL A 71
REMARK 465 THR A 72
REMARK 465 SER A 73
REMARK 465 THR A 74
REMARK 465 ARG A 75
REMARK 465 PRO A 76
REMARK 465 ASN A 497
REMARK 465 GLU A 498
REMARK 465 HIS A 499
REMARK 465 HIS A 500
REMARK 465 HIS A 501
REMARK 465 HIS A 502
REMARK 465 HIS A 503
REMARK 465 HIS A 504
REMARK 465 SER B 65
REMARK 465 LEU B 66
REMARK 465 ASP B 67
REMARK 465 LYS B 68
REMARK 465 LEU B 69
REMARK 465 HIS B 70
REMARK 465 VAL B 71
REMARK 465 THR B 72
REMARK 465 SER B 73
REMARK 465 THR B 74
REMARK 465 ARG B 75
REMARK 465 PRO B 76
REMARK 465 ASN B 497
REMARK 465 GLU B 498
REMARK 465 HIS B 499
REMARK 465 HIS B 500
REMARK 465 HIS B 501
REMARK 465 HIS B 502
REMARK 465 HIS B 503
REMARK 465 HIS B 504
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 A 123 C - N - CA ANGL. DEV. = 11.0 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 TRP A 84 -0.52 -56.86
REMARK 500 THR A 99 -107.37 -65.74
REMARK 500 SER A 100 -111.31 -112.04
REMARK 500 PHE A 102 -134.27 -88.20
REMARK 500 THR A 103 -105.78 -66.95
REMARK 500 SER A 106 -72.31 -64.57
REMARK 500 SER A 108 127.28 173.19
REMARK 500 LEU A 110 34.98 -94.65
REMARK 500 ASN A 115 77.92 -112.30
REMARK 500 PRO A 123 -179.90 -52.73
REMARK 500 ASP A 125 -34.43 -149.98
REMARK 500 SER A 147 -73.12 -68.26
REMARK 500 PHE A 148 138.71 -38.67
REMARK 500 ARG A 197 -6.48 -55.69
REMARK 500 SER A 212 -10.61 -151.70
REMARK 500 GLN A 243 -178.42 -61.29
REMARK 500 SER A 245 -89.28 -102.64
REMARK 500 THR A 277 43.93 -93.28
REMARK 500 TYR A 293 79.49 30.97
REMARK 500 ASP A 306 55.47 34.89
REMARK 500 LYS A 329 -46.96 -135.11
REMARK 500 ASN A 348 32.25 -74.45
REMARK 500 CYS A 361 65.75 -165.38
REMARK 500 ARG A 382 -138.45 -116.27
REMARK 500 ALA A 447 -73.72 -70.87
REMARK 500 CYS A 451 103.92 -161.65
REMARK 500 LEU A 479 -155.62 -106.17
REMARK 500 PRO A 489 -31.82 -39.56
REMARK 500 THR B 99 -101.77 -73.64
REMARK 500 SER B 100 -123.57 -117.00
REMARK 500 PHE B 102 -138.78 -82.94
REMARK 500 THR B 103 -107.36 -61.40
REMARK 500 SER B 106 -88.80 -77.99
REMARK 500 SER B 108 134.36 162.84
REMARK 500 LEU B 110 39.84 -85.29
REMARK 500 ASN B 115 63.78 -115.97
REMARK 500 ASP B 125 -38.40 -143.67
REMARK 500 THR B 128 106.31 -52.79
REMARK 500 LYS B 149 -74.70 -43.62
REMARK 500 THR B 172 -167.29 -70.71
REMARK 500 ARG B 197 -8.96 -50.27
REMARK 500 TRP B 200 -35.75 -34.51
REMARK 500 ASP B 207 94.35 -69.55
REMARK 500 SER B 212 -6.79 -150.75
REMARK 500 SER B 245 -75.57 -93.91
REMARK 500 LEU B 258 -71.07 -48.43
REMARK 500 ARG B 260 141.13 -174.59
REMARK 500 ASP B 268 24.85 -68.91
REMARK 500 THR B 277 37.46 -98.25
REMARK 500 LEU B 287 21.22 -75.98
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 194 SG
REMARK 620 2 HEM A 901 NA 98.4
REMARK 620 3 HEM A 901 NB 87.8 90.2
REMARK 620 4 HEM A 901 NC 91.6 169.9 88.6
REMARK 620 5 HEM A 901 ND 94.3 89.9 177.9 91.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 194 SG
REMARK 620 2 HEM B 901 NA 96.2
REMARK 620 3 HEM B 901 NB 80.2 90.9
REMARK 620 4 HEM B 901 NC 87.5 176.3 89.3
REMARK 620 5 HEM B 901 ND 95.3 89.4 175.4 90.7
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: KABSCH AND SANDER
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DWV RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER N-
REMARK 900 HYDROXYARGININE AND 4-AMINO TETRAHYDROBIOPTERIN
REMARK 900 RELATED ID: 1DWW RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER N-
REMARK 900 HYDROXYARGININE AND DIHYDROBIOPTERIN
REMARK 900 RELATED ID: 1DWX RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER N-
REMARK 900 HYDROXYARGININE AND TETRAHYDROBIOPTERIN
REMARK 900 RELATED ID: 1NOC RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114)
REMARK 900 COMPLEXED WITH TYPE I E. COLI CHLORAMPHENICOL ACETYL TRANSFERASE
REMARK 900 AND IMIDAZOLE
REMARK 900 RELATED ID: 1NOS RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114),
REMARK 900 IMIDAZOLE COMPLEX
REMARK 900 RELATED ID: 2NOS RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114),
REMARK 900 AMINOGUANIDINE COMPLEX
REMARK 900 RELATED ID: 1NOD RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65)
REMARK 900 WITH TETRAHYDROBIOPTERIN AND SUBSTRATE L-ARGININE
REMARK 900 RELATED ID: 2NOD RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65)
REMARK 900 WITH TETRAHYDROBIOPTERIN AND WATER BOUND IN ACTIVE CENTER
REMARK 900 RELATED ID: 3NOD RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65)
REMARK 900 WITH TETRAHYDROBIOPTERIN AND PRODUCT ANALOGUE L-THIOCITRULLINE
DBREF 1QOM A 65 498 UNP P29477 NOS2_MOUSE 77 498
DBREF 1QOM A 499 504 PDB 1QOM 1QOM 499 504
DBREF 1QOM B 65 498 UNP P29477 NOS2_MOUSE 77 498
DBREF 1QOM B 499 504 PDB 1QOM 1QOM 499 504
SEQRES 1 A 440 SER LEU ASP LYS LEU HIS VAL THR SER THR ARG PRO GLN
SEQRES 2 A 440 TYR VAL ARG ILE LYS ASN TRP GLY SER GLY GLU ILE LEU
SEQRES 3 A 440 HIS ASP THR LEU HIS HIS LYS ALA THR SER ASP PHE THR
SEQRES 4 A 440 CYS LYS SER LYS SER CYS LEU GLY SER ILE MET ASN PRO
SEQRES 5 A 440 LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO THR PRO
SEQRES 6 A 440 LEU GLU GLU LEU LEU PRO HIS ALA ILE GLU PHE ILE ASN
SEQRES 7 A 440 GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE GLU GLU
SEQRES 8 A 440 HIS LEU ALA ARG LEU GLU ALA VAL THR LYS GLU ILE GLU
SEQRES 9 A 440 THR THR GLY THR TYR GLN LEU THR LEU ASP GLU LEU ILE
SEQRES 10 A 440 PHE ALA THR LYS MET ALA TRP ARG ASN ALA PRO ARG CYS
SEQRES 11 A 440 ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL PHE ASP
SEQRES 12 A 440 ALA ARG ASN CYS SER THR ALA GLN GLU MET PHE GLN HIS
SEQRES 13 A 440 ILE CYS ARG HIS ILE LEU TYR ALA THR ASN ASN GLY ASN
SEQRES 14 A 440 ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG SER ASP
SEQRES 15 A 440 GLY LYS HIS ASP PHE ARG LEU TRP ASN SER GLN LEU ILE
SEQRES 16 A 440 ARG TYR ALA GLY TYR GLN MET PRO ASP GLY THR ILE ARG
SEQRES 17 A 440 GLY ASP ALA ALA THR LEU GLU PHE THR GLN LEU CYS ILE
SEQRES 18 A 440 ASP LEU GLY TRP LYS PRO ARG TYR GLY ARG PHE ASP VAL
SEQRES 19 A 440 LEU PRO LEU VAL LEU GLN ALA ASP GLY GLN ASP PRO GLU
SEQRES 20 A 440 VAL PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU VAL THR
SEQRES 21 A 440 MET GLU HIS PRO LYS TYR GLU TRP PHE GLN GLU LEU GLY
SEQRES 22 A 440 LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN MET LEU
SEQRES 23 A 440 LEU GLU VAL GLY GLY LEU GLU PHE PRO ALA CYS PRO PHE
SEQRES 24 A 440 ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG ASP
SEQRES 25 A 440 PHE CYS ASP THR GLN ARG TYR ASN ILE LEU GLU GLU VAL
SEQRES 26 A 440 GLY ARG ARG MET GLY LEU GLU THR HIS THR LEU ALA SER
SEQRES 27 A 440 LEU TRP LYS ASP ARG ALA VAL THR GLU ILE ASN VAL ALA
SEQRES 28 A 440 VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR ILE MET
SEQRES 29 A 440 ASP HIS HIS THR ALA SER GLU SER PHE MET LYS HIS MET
SEQRES 30 A 440 GLN ASN GLU TYR ARG ALA ARG GLY GLY CYS PRO ALA ASP
SEQRES 31 A 440 TRP ILE TRP LEU VAL PRO PRO VAL SER GLY SER ILE THR
SEQRES 32 A 440 PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL LEU SER
SEQRES 33 A 440 PRO PHE TYR TYR TYR GLN ILE GLU PRO TRP LYS THR HIS
SEQRES 34 A 440 ILE TRP GLN ASN GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 440 SER LEU ASP LYS LEU HIS VAL THR SER THR ARG PRO GLN
SEQRES 2 B 440 TYR VAL ARG ILE LYS ASN TRP GLY SER GLY GLU ILE LEU
SEQRES 3 B 440 HIS ASP THR LEU HIS HIS LYS ALA THR SER ASP PHE THR
SEQRES 4 B 440 CYS LYS SER LYS SER CYS LEU GLY SER ILE MET ASN PRO
SEQRES 5 B 440 LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO THR PRO
SEQRES 6 B 440 LEU GLU GLU LEU LEU PRO HIS ALA ILE GLU PHE ILE ASN
SEQRES 7 B 440 GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE GLU GLU
SEQRES 8 B 440 HIS LEU ALA ARG LEU GLU ALA VAL THR LYS GLU ILE GLU
SEQRES 9 B 440 THR THR GLY THR TYR GLN LEU THR LEU ASP GLU LEU ILE
SEQRES 10 B 440 PHE ALA THR LYS MET ALA TRP ARG ASN ALA PRO ARG CYS
SEQRES 11 B 440 ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL PHE ASP
SEQRES 12 B 440 ALA ARG ASN CYS SER THR ALA GLN GLU MET PHE GLN HIS
SEQRES 13 B 440 ILE CYS ARG HIS ILE LEU TYR ALA THR ASN ASN GLY ASN
SEQRES 14 B 440 ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG SER ASP
SEQRES 15 B 440 GLY LYS HIS ASP PHE ARG LEU TRP ASN SER GLN LEU ILE
SEQRES 16 B 440 ARG TYR ALA GLY TYR GLN MET PRO ASP GLY THR ILE ARG
SEQRES 17 B 440 GLY ASP ALA ALA THR LEU GLU PHE THR GLN LEU CYS ILE
SEQRES 18 B 440 ASP LEU GLY TRP LYS PRO ARG TYR GLY ARG PHE ASP VAL
SEQRES 19 B 440 LEU PRO LEU VAL LEU GLN ALA ASP GLY GLN ASP PRO GLU
SEQRES 20 B 440 VAL PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU VAL THR
SEQRES 21 B 440 MET GLU HIS PRO LYS TYR GLU TRP PHE GLN GLU LEU GLY
SEQRES 22 B 440 LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN MET LEU
SEQRES 23 B 440 LEU GLU VAL GLY GLY LEU GLU PHE PRO ALA CYS PRO PHE
SEQRES 24 B 440 ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG ASP
SEQRES 25 B 440 PHE CYS ASP THR GLN ARG TYR ASN ILE LEU GLU GLU VAL
SEQRES 26 B 440 GLY ARG ARG MET GLY LEU GLU THR HIS THR LEU ALA SER
SEQRES 27 B 440 LEU TRP LYS ASP ARG ALA VAL THR GLU ILE ASN VAL ALA
SEQRES 28 B 440 VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR ILE MET
SEQRES 29 B 440 ASP HIS HIS THR ALA SER GLU SER PHE MET LYS HIS MET
SEQRES 30 B 440 GLN ASN GLU TYR ARG ALA ARG GLY GLY CYS PRO ALA ASP
SEQRES 31 B 440 TRP ILE TRP LEU VAL PRO PRO VAL SER GLY SER ILE THR
SEQRES 32 B 440 PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL LEU SER
SEQRES 33 B 440 PRO PHE TYR TYR TYR GLN ILE GLU PRO TRP LYS THR HIS
SEQRES 34 B 440 ILE TRP GLN ASN GLU HIS HIS HIS HIS HIS HIS
HET HEM A 901 43
HET H4B A 902 17
HET HEM B 901 43
HET H4B B 902 17
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 7 HOH *394(H2 O)
HELIX 1 1 THR A 93 ALA A 98 5 6
HELIX 2 2 PRO A 116 LEU A 119 5 4
HELIX 3 3 PRO A 129 PHE A 148 1 20
HELIX 4 4 LYS A 152 GLY A 171 1 20
HELIX 5 5 THR A 176 ASN A 190 1 15
HELIX 6 6 GLY A 196 TRP A 200 5 5
HELIX 7 7 THR A 213 ASN A 230 1 18
HELIX 8 8 ASN A 231 ASN A 233 5 3
HELIX 9 9 THR A 277 LEU A 287 1 11
HELIX 10 10 TYR A 330 GLY A 337 5 8
HELIX 11 11 GLY A 369 VAL A 374 1 6
HELIX 12 12 VAL A 374 ASP A 379 1 6
HELIX 13 13 ILE A 385 ARG A 392 1 8
HELIX 14 14 THR A 399 SER A 402 5 4
HELIX 15 15 LEU A 403 GLN A 423 1 21
HELIX 16 16 ASP A 429 GLY A 449 1 21
HELIX 17 17 ASP A 454 VAL A 459 1 6
HELIX 18 18 SER A 463 THR A 467 5 5
HELIX 19 19 THR A 467 GLN A 472 5 6
HELIX 20 20 GLU A 488 HIS A 493 1 6
HELIX 21 21 THR B 93 ALA B 98 5 6
HELIX 22 22 PRO B 116 LEU B 119 5 4
HELIX 23 23 PRO B 129 PHE B 148 1 20
HELIX 24 24 LYS B 152 GLY B 171 1 20
HELIX 25 25 THR B 176 ASN B 190 1 15
HELIX 26 26 GLY B 196 TRP B 200 5 5
HELIX 27 27 THR B 213 ASN B 230 1 18
HELIX 28 28 ASN B 231 ASN B 233 5 3
HELIX 29 29 THR B 277 LEU B 287 1 11
HELIX 30 30 PHE B 333 GLY B 337 5 5
HELIX 31 31 GLY B 369 VAL B 374 1 6
HELIX 32 32 VAL B 374 ASP B 379 1 6
HELIX 33 33 ILE B 385 ARG B 392 1 8
HELIX 34 34 THR B 399 SER B 402 5 4
HELIX 35 35 LEU B 403 GLN B 423 1 21
HELIX 36 36 ASP B 429 GLY B 449 1 21
HELIX 37 37 ASP B 454 VAL B 459 1 6
HELIX 38 38 THR B 467 GLN B 472 5 6
HELIX 39 39 GLU B 488 THR B 492 5 5
SHEET 1 A 2 VAL A 79 LYS A 82 0
SHEET 2 A 2 ILE A 89 ASP A 92 -1 N ASP A 92 O VAL A 79
SHEET 1 B 2 GLN A 204 ALA A 208 0
SHEET 2 B 2 ALA A 237 PHE A 241 1 N ILE A 238 O GLN A 204
SHEET 1 C 2 GLY A 263 GLN A 265 0
SHEET 2 C 2 ILE A 271 GLY A 273 -1 N ARG A 272 O TYR A 264
SHEET 1 D 2 LEU A 301 LEU A 303 0
SHEET 2 D 2 GLU A 311 PHE A 313 -1 N PHE A 313 O LEU A 301
SHEET 1 E 2 GLU A 322 THR A 324 0
SHEET 2 E 2 LYS A 339 TYR A 341 -1 N TRP A 340 O VAL A 323
SHEET 1 F 3 PHE A 482 TYR A 484 0
SHEET 2 F 3 LEU A 350 VAL A 353 -1 N GLU A 352 O PHE A 482
SHEET 3 F 3 LEU A 356 PHE A 358 -1 N PHE A 358 O LEU A 351
SHEET 1 G 2 VAL B 79 LYS B 82 0
SHEET 2 G 2 ILE B 89 ASP B 92 -1 N ASP B 92 O VAL B 79
SHEET 1 H 2 GLN B 204 ALA B 208 0
SHEET 2 H 2 ALA B 237 PHE B 241 1 N ILE B 238 O GLN B 204
SHEET 1 I 2 GLY B 263 GLN B 265 0
SHEET 2 I 2 ILE B 271 GLY B 273 -1 N ARG B 272 O TYR B 264
SHEET 1 J 2 LEU B 301 LEU B 303 0
SHEET 2 J 2 GLU B 311 PHE B 313 -1 N PHE B 313 O LEU B 301
SHEET 1 K 2 GLU B 322 THR B 324 0
SHEET 2 K 2 LYS B 339 TYR B 341 -1 N TRP B 340 O VAL B 323
SHEET 1 L 3 PHE B 482 TYR B 484 0
SHEET 2 L 3 LEU B 350 VAL B 353 -1 N GLU B 352 O PHE B 482
SHEET 3 L 3 LEU B 356 PHE B 358 -1 N PHE B 358 O LEU B 351
SSBOND 1 CYS A 109 CYS A 109 1555 11655 2.08
SSBOND 2 CYS B 109 CYS B 109 1555 9766 2.09
LINK FE HEM A 901 SG CYS A 194 1555 1555 2.31
LINK FE HEM B 901 SG CYS B 194 1555 1555 2.36
CISPEP 1 SER A 480 PRO A 481 0 -0.06
CISPEP 2 SER B 480 PRO B 481 0 -0.73
SITE 1 AC1 15 TRP A 188 CYS A 194 GLY A 196 SER A 236
SITE 2 AC1 15 PHE A 363 ASN A 364 GLY A 365 TRP A 366
SITE 3 AC1 15 TRP A 457 TYR A 485 H4B A 902 HOH A2185
SITE 4 AC1 15 HOH A2186 HOH A2187 HOH A2190
SITE 1 AC2 14 SER A 112 ARG A 375 TRP A 455 ILE A 456
SITE 2 AC2 14 TRP A 457 PHE A 470 HIS A 471 GLN A 472
SITE 3 AC2 14 GLU A 473 HEM A 901 HOH A2168 HOH A2189
SITE 4 AC2 14 HOH A2190 HOH A2191
SITE 1 AC3 16 TRP B 188 ARG B 193 CYS B 194 GLY B 196
SITE 2 AC3 16 SER B 236 PHE B 363 ASN B 364 GLY B 365
SITE 3 AC3 16 TRP B 366 GLU B 371 TRP B 457 TYR B 483
SITE 4 AC3 16 TYR B 485 H4B B 902 HOH B2202 HOH B2203
SITE 1 AC4 14 SER B 112 ARG B 375 TRP B 455 ILE B 456
SITE 2 AC4 14 TRP B 457 PHE B 470 HIS B 471 GLN B 472
SITE 3 AC4 14 GLU B 473 HEM B 901 HOH B2146 HOH B2183
SITE 4 AC4 14 HOH B2189 HOH B2202
CRYST1 212.980 212.980 114.200 90.00 90.00 120.00 P 61 2 2 24
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 0.004695 0.002711 0.000000 0.00000
SCALE2 0.000000 0.005422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008756 0.00000
MTRIX1 1 -0.863870 -0.503700 -0.003907 291.42731 1
MTRIX2 1 -0.503715 0.863838 0.007455 78.08660 1
MTRIX3 1 0.000380 0.008408 -0.999965 122.68790 1
MTRIX1 2 -0.866206 -0.499593 -0.009731 291.86951 1
MTRIX2 2 -0.499653 0.866210 0.005100 77.41970 1
MTRIX3 2 0.005881 0.009280 -0.999940 122.75170 1
MTRIX1 3 -0.862943 -0.505143 -0.012623 292.31000 1
MTRIX2 3 -0.505258 0.862926 0.008542 78.31740 1
MTRIX3 3 0.006578 0.013749 -0.999884 121.16290 1
(ATOM LINES ARE NOT SHOWN.)
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