HEADER OXIDOREDUCTASE 13-SEP-99 1D0O
TITLE BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-
TITLE 2 BROMO-7-NITROINDAZOLE (H4B PRESENT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.14.13.39;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 CELL: ENDOTHELIAL CELLS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.RAMAN,H.LI,P.MARTASEK,G.J.SOUTHAN,B.S.S.MASTERS,T.L.POULOS
REVDAT 6 07-FEB-24 1D0O 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 1D0O 1 VERSN
REVDAT 4 20-OCT-10 1D0O 1 REMARK
REVDAT 3 24-FEB-09 1D0O 1 VERSN
REVDAT 2 01-APR-03 1D0O 1 JRNL
REVDAT 1 21-NOV-01 1D0O 0
JRNL AUTH C.S.RAMAN,H.LI,P.MARTASEK,G.SOUTHAN,B.S.MASTERS,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURE OF NITRIC OXIDE SYNTHASE BOUND TO NITRO
JRNL TITL 2 INDAZOLE REVEALS A NOVEL INACTIVATION MECHANISM.
JRNL REF BIOCHEMISTRY V. 40 13448 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11695891
JRNL DOI 10.1021/BI010957U
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.S.RAMAN,H.LI,P.MARTASEK,V.KRAL,B.S.MASTERS,T.L.POULOS
REMARK 1 TITL CRYSTAL STRUCTURE OF CONSTITUTIVE ENDOTHELIAL NITRIC OXIDE
REMARK 1 TITL 2 SYNTHASE: A PARADIGM FOR PTERIN FUNCTION INVOLVING A NOVEL
REMARK 1 TITL 3 METAL CENTER
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 95 939 1998
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)81718-3
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 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 DOI 10.1126/SCIENCE.278.5337.425
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 58970
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) : 0.200
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2976
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.04
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5295
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 299
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 173
REMARK 3 SOLVENT ATOMS : 426
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.425
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.36
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.275
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 108 TO 120 ARE DISORDERED,
REMARK 3 BUT THE TENTATIVE MODEL WAS INCLUDED
REMARK 3 IN THE REFINEMENT.
REMARK 3 COFACTOR H4B WAS PRESENT IN THE
REMARK 3 PROTEIN SAMPLE USED FOR THE
REMARK 3 CRYSTALLIZATION AND HAVE BEEN
REMARK 3 REPLACED BY 3-BR-7-NITRO-INDAZOLE
REMARK 3 DURING THE CRYSTAL GROWTH.
REMARK 4
REMARK 4 1D0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73044
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.61200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, CACODYLATE, MAGNESIUM
REMARK 280 ACETATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 280K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 28.79500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.89000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.89000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.79500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.03000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 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 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 39
REMARK 465 ARG A 40
REMARK 465 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 THR A 46
REMARK 465 PRO A 47
REMARK 465 HIS A 48
REMARK 465 ALA A 49
REMARK 465 PRO A 50
REMARK 465 ASP A 51
REMARK 465 HIS A 52
REMARK 465 SER A 53
REMARK 465 PRO A 54
REMARK 465 ALA A 55
REMARK 465 PRO A 56
REMARK 465 ASN A 57
REMARK 465 SER A 58
REMARK 465 PRO A 59
REMARK 465 THR A 60
REMARK 465 LEU A 61
REMARK 465 THR A 62
REMARK 465 ARG A 63
REMARK 465 PRO A 64
REMARK 465 PRO A 65
REMARK 465 GLU A 66
REMARK 465 SER B 39
REMARK 465 ARG B 40
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 THR B 46
REMARK 465 PRO B 47
REMARK 465 HIS B 48
REMARK 465 ALA B 49
REMARK 465 PRO B 50
REMARK 465 ASP B 51
REMARK 465 HIS B 52
REMARK 465 SER B 53
REMARK 465 PRO B 54
REMARK 465 ALA B 55
REMARK 465 PRO B 56
REMARK 465 ASN B 57
REMARK 465 SER B 58
REMARK 465 PRO B 59
REMARK 465 THR B 60
REMARK 465 LEU B 61
REMARK 465 THR B 62
REMARK 465 ARG B 63
REMARK 465 PRO B 64
REMARK 465 PRO B 65
REMARK 465 GLU B 66
REMARK 465 GLY B 67
REMARK 465 PRO B 68
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 LYS A 69 31.27 -75.97
REMARK 500 LYS A 110 -69.57 -124.75
REMARK 500 PRO A 115 100.03 -35.67
REMARK 500 LYS A 194 71.07 -106.34
REMARK 500 ASN A 225 72.75 -104.05
REMARK 500 ARG A 240 130.47 -173.04
REMARK 500 SER A 262 -176.88 -64.32
REMARK 500 ASN A 285 48.23 -161.76
REMARK 500 ALA A 353 70.62 -158.24
REMARK 500 THR A 366 -63.95 -97.55
REMARK 500 ARG A 374 -133.46 -118.66
REMARK 500 PRO B 108 -162.91 -114.40
REMARK 500 ARG B 109 -21.18 -159.84
REMARK 500 PRO B 115 170.57 -49.52
REMARK 500 PRO B 121 130.76 -37.99
REMARK 500 SER B 145 174.04 -59.97
REMARK 500 ARG B 189 2.13 -64.31
REMARK 500 ARG B 223 14.05 59.34
REMARK 500 ASN B 225 70.84 -100.72
REMARK 500 GLN B 259 -67.73 18.26
REMARK 500 ASP B 260 25.20 -72.40
REMARK 500 ASN B 285 21.53 -150.98
REMARK 500 ALA B 353 66.33 -157.06
REMARK 500 THR B 366 -65.50 -97.44
REMARK 500 ARG B 374 -137.76 -116.21
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 ZN A 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 101 SG 111.2
REMARK 620 3 CYS B 96 SG 115.5 108.3
REMARK 620 4 CYS B 101 SG 110.5 105.4 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 186 SG
REMARK 620 2 HEM A 500 NA 98.5
REMARK 620 3 HEM A 500 NB 91.7 85.6
REMARK 620 4 HEM A 500 NC 101.3 160.2 92.9
REMARK 620 5 HEM A 500 ND 101.4 91.4 166.8 85.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CAD A 950 AS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 384 SG
REMARK 620 2 CAD A 950 C1 95.5
REMARK 620 3 CAD A 950 C2 92.9 95.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 186 SG
REMARK 620 2 HEM B 500 NA 99.5
REMARK 620 3 HEM B 500 NB 98.4 85.8
REMARK 620 4 HEM B 500 NC 98.8 161.7 91.7
REMARK 620 5 HEM B 500 ND 92.5 91.0 169.0 88.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CAD B 951 AS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 384 SG
REMARK 620 2 CAD B 951 C1 95.8
REMARK 620 3 CAD B 951 C2 94.5 94.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 850
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 851
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INE A 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INE B 765
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAD A 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INE B 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INE A 766
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAD B 951
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 881
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NSE RELATED DB: PDB
REMARK 900 ENOS HEME DOMAIN COMPLEXED WITH SEITU
REMARK 900 RELATED ID: 1D0C RELATED DB: PDB
REMARK 900 ENOS HEME DOMAIN COMPLEXED WITH 3-BR-7-NI (H4B FREE)
REMARK 900 RELATED ID: 1D0O RELATED DB: PDB
REMARK 900 ENOS HEME DOMAIN COMPLEXED WITH 3-BR-7-NI (H4B PRESENT)
REMARK 900 RELATED ID: 1D1V RELATED DB: PDB
REMARK 900 ENOS HEME DOMAIN COMPLEXED WITH S-ETHYL-N-PHENYL-ISOTHIOUREA (H4B
REMARK 900 BOUND)
REMARK 900 RELATED ID: 1D1W RELATED DB: PDB
REMARK 900 ENOS HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)
REMARK 900 RELATED ID: 1D1X RELATED DB: PDB
REMARK 900 ENOS HEME DOMAIN COMPLEXED WITH 1,4-PBITU (H4B BOUND)
REMARK 900 RELATED ID: 1D1Y RELATED DB: PDB
REMARK 900 ENOS HEME DOMAIN COMPLEXED WITH 1,3-PBITU (H4B FREE)
DBREF 1D0O A 39 482 UNP P29473 NOS3_BOVIN 39 482
DBREF 1D0O B 39 482 UNP P29473 NOS3_BOVIN 39 482
SEQADV 1D0O ARG A 100 UNP P29473 CYS 100 CONFLICT
SEQADV 1D0O ARG B 100 UNP P29473 CYS 100 CONFLICT
SEQRES 1 A 444 SER ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP
SEQRES 2 A 444 HIS SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO
SEQRES 3 A 444 PRO GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU
SEQRES 4 A 444 LEU GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER
SEQRES 5 A 444 GLN GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY
SEQRES 6 A 444 SER LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER
SEQRES 7 A 444 PRO GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA
SEQRES 8 A 444 ARG ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG
SEQRES 9 A 444 SER GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL
SEQRES 10 A 444 GLU ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG
SEQRES 11 A 444 GLU SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG
SEQRES 12 A 444 ASN ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS
SEQRES 13 A 444 LEU GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN
SEQRES 14 A 444 GLU MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA
SEQRES 15 A 444 THR ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE
SEQRES 16 A 444 PRO GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP
SEQRES 17 A 444 ASN SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN
SEQRES 18 A 444 ASP GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE
SEQRES 19 A 444 THR GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN
SEQRES 20 A 444 GLY ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO
SEQRES 21 A 444 ASP GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU
SEQRES 22 A 444 VAL LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP
SEQRES 23 A 444 PHE ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA
SEQRES 24 A 444 VAL SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE
SEQRES 25 A 444 SER ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU
SEQRES 26 A 444 ILE GLY THR ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN
SEQRES 27 A 444 ILE LEU GLU ASP VAL ALA VAL CYS MET ASP LEU ASP THR
SEQRES 28 A 444 ARG THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL
SEQRES 29 A 444 GLU ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA
SEQRES 30 A 444 LYS VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER
SEQRES 31 A 444 PHE MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY
SEQRES 32 A 444 GLY CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE
SEQRES 33 A 444 SER GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL
SEQRES 34 A 444 ASN TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP
SEQRES 35 A 444 PRO TRP
SEQRES 1 B 444 SER ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP
SEQRES 2 B 444 HIS SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO
SEQRES 3 B 444 PRO GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU
SEQRES 4 B 444 LEU GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER
SEQRES 5 B 444 GLN GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY
SEQRES 6 B 444 SER LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER
SEQRES 7 B 444 PRO GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA
SEQRES 8 B 444 ARG ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG
SEQRES 9 B 444 SER GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL
SEQRES 10 B 444 GLU ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG
SEQRES 11 B 444 GLU SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG
SEQRES 12 B 444 ASN ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS
SEQRES 13 B 444 LEU GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN
SEQRES 14 B 444 GLU MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA
SEQRES 15 B 444 THR ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE
SEQRES 16 B 444 PRO GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP
SEQRES 17 B 444 ASN SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN
SEQRES 18 B 444 ASP GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE
SEQRES 19 B 444 THR GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN
SEQRES 20 B 444 GLY ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO
SEQRES 21 B 444 ASP GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU
SEQRES 22 B 444 VAL LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP
SEQRES 23 B 444 PHE ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA
SEQRES 24 B 444 VAL SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE
SEQRES 25 B 444 SER ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU
SEQRES 26 B 444 ILE GLY THR ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN
SEQRES 27 B 444 ILE LEU GLU ASP VAL ALA VAL CYS MET ASP LEU ASP THR
SEQRES 28 B 444 ARG THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL
SEQRES 29 B 444 GLU ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA
SEQRES 30 B 444 LYS VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER
SEQRES 31 B 444 PHE MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY
SEQRES 32 B 444 GLY CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE
SEQRES 33 B 444 SER GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL
SEQRES 34 B 444 ASN TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP
SEQRES 35 B 444 PRO TRP
HET ACT A 850 4
HET ACT A 860 4
HET ZN A 900 1
HET HEM A 500 43
HET INE A 760 13
HET CAD A 950 3
HET INE A 766 13
HET GOL A 880 6
HET ACT B 851 4
HET ACT B 861 4
HET INE B 765 13
HET HEM B 500 43
HET INE B 761 13
HET CAD B 951 3
HET GOL B 881 6
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM INE 3-BROMO-7-NITROINDAZOLE
HETNAM CAD CACODYLIC ACID
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN CAD HYDROXYDIMETHYLARSINE OXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ACT 4(C2 H3 O2 1-)
FORMUL 5 ZN ZN 2+
FORMUL 6 HEM 2(C34 H32 FE N4 O4)
FORMUL 7 INE 4(C7 H4 BR N3 O2)
FORMUL 8 CAD 2(C2 H7 AS O2)
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 18 HOH *426(H2 O)
HELIX 1 1 THR A 85 SER A 90 5 6
HELIX 2 2 PRO A 121 ILE A 140 1 20
HELIX 3 3 SER A 145 GLY A 163 1 19
HELIX 4 4 ARG A 168 ASN A 182 1 15
HELIX 5 5 GLY A 188 TRP A 192 5 5
HELIX 6 6 SER A 205 ASN A 222 1 18
HELIX 7 7 ARG A 223 ASN A 225 5 3
HELIX 8 8 ASN A 269 HIS A 279 1 11
HELIX 9 9 PRO A 308 VAL A 312 5 5
HELIX 10 10 LEU A 322 GLY A 329 5 8
HELIX 11 11 SER A 361 THR A 366 1 6
HELIX 12 12 THR A 366 ASP A 371 1 6
HELIX 13 13 ILE A 377 MET A 385 1 9
HELIX 14 14 THR A 391 SER A 394 5 4
HELIX 15 15 LEU A 395 ALA A 415 1 21
HELIX 16 16 ASP A 421 GLY A 441 1 21
HELIX 17 17 ASP A 446 VAL A 451 1 6
HELIX 18 18 SER A 455 THR A 459 5 5
HELIX 19 19 THR B 85 SER B 90 5 6
HELIX 20 20 PRO B 121 ILE B 140 1 20
HELIX 21 21 SER B 145 GLY B 163 1 19
HELIX 22 22 ARG B 168 ASN B 182 1 15
HELIX 23 23 GLY B 188 TRP B 192 5 5
HELIX 24 24 SER B 205 ASN B 222 1 18
HELIX 25 25 ARG B 223 ASN B 225 5 3
HELIX 26 26 ASN B 269 HIS B 279 1 11
HELIX 27 27 PHE B 325 GLY B 329 5 5
HELIX 28 28 MET B 360 THR B 366 1 7
HELIX 29 29 THR B 366 ASP B 371 1 6
HELIX 30 30 ILE B 377 MET B 385 1 9
HELIX 31 31 THR B 391 SER B 394 5 4
HELIX 32 32 LEU B 395 ALA B 415 1 21
HELIX 33 33 ASP B 421 GLY B 441 1 21
HELIX 34 34 ASP B 446 VAL B 451 1 6
HELIX 35 35 SER B 455 THR B 459 5 5
SHEET 1 A 2 ARG A 72 LYS A 74 0
SHEET 2 A 2 ILE A 81 TYR A 83 -1 O THR A 82 N VAL A 73
SHEET 1 B 4 GLN A 196 ASP A 199 0
SHEET 2 B 4 ALA A 229 VAL A 232 1 O ILE A 230 N PHE A 198
SHEET 3 B 4 PHE A 355 SER A 356 -1 N SER A 356 O ALA A 229
SHEET 4 B 4 ALA A 337 VAL A 338 -1 O VAL A 338 N PHE A 355
SHEET 1 C 3 ARG A 244 ILE A 245 0
SHEET 2 C 3 LEU A 293 GLN A 296 -1 N GLN A 296 O ARG A 244
SHEET 3 C 3 GLU A 303 PHE A 305 -1 N GLU A 303 O LEU A 295
SHEET 1 D 2 GLY A 255 ARG A 257 0
SHEET 2 D 2 VAL A 263 GLY A 265 -1 O ARG A 264 N TYR A 256
SHEET 1 E 2 GLU A 314 PRO A 316 0
SHEET 2 E 2 ARG A 331 TYR A 333 -1 O TRP A 332 N VAL A 315
SHEET 1 F 3 LEU A 348 PHE A 350 0
SHEET 2 F 3 LEU A 342 ILE A 345 -1 O LEU A 343 N PHE A 350
SHEET 3 F 3 ALA A 474 ARG A 476 -1 O ALA A 474 N GLU A 344
SHEET 1 G 2 TYR A 359 MET A 360 0
SHEET 2 G 2 ILE A 419 VAL A 420 1 N VAL A 420 O TYR A 359
SHEET 1 H 2 ARG B 72 LYS B 74 0
SHEET 2 H 2 ILE B 81 TYR B 83 -1 O THR B 82 N VAL B 73
SHEET 1 I 4 GLN B 196 ASP B 199 0
SHEET 2 I 4 ALA B 229 VAL B 232 1 O ILE B 230 N PHE B 198
SHEET 3 I 4 PHE B 355 SER B 356 -1 N SER B 356 O ALA B 229
SHEET 4 I 4 ALA B 337 VAL B 338 -1 O VAL B 338 N PHE B 355
SHEET 1 J 3 ARG B 244 ILE B 245 0
SHEET 2 J 3 LEU B 293 GLN B 296 -1 N GLN B 296 O ARG B 244
SHEET 3 J 3 GLU B 303 PHE B 305 -1 N GLU B 303 O LEU B 295
SHEET 1 K 2 GLY B 255 TYR B 256 0
SHEET 2 K 2 ARG B 264 GLY B 265 -1 O ARG B 264 N TYR B 256
SHEET 1 L 2 GLU B 314 PRO B 316 0
SHEET 2 L 2 ARG B 331 TYR B 333 -1 O TRP B 332 N VAL B 315
SHEET 1 M 3 LEU B 348 PHE B 350 0
SHEET 2 M 3 LEU B 342 ILE B 345 -1 O LEU B 343 N PHE B 350
SHEET 3 M 3 ALA B 474 ARG B 476 -1 O ALA B 474 N GLU B 344
LINK SG CYS A 96 ZN ZN A 900 1555 1555 2.33
LINK SG CYS A 101 ZN ZN A 900 1555 1555 2.33
LINK SG CYS A 186 FE HEM A 500 1555 1555 2.23
LINK SG CYS A 384 AS CAD A 950 1555 1555 2.36
LINK ZN ZN A 900 SG CYS B 96 1555 1555 2.32
LINK ZN ZN A 900 SG CYS B 101 1555 1555 2.29
LINK SG CYS B 186 FE HEM B 500 1555 1555 2.24
LINK SG CYS B 384 AS CAD B 951 1555 1555 2.32
CISPEP 1 SER A 472 PRO A 473 0 -1.31
CISPEP 2 SER B 472 PRO B 473 0 0.92
SITE 1 AC1 6 GLN A 249 TYR A 359 GLU A 363 ASN A 368
SITE 2 AC1 6 HOH A1008 HOH A1030
SITE 1 AC2 6 TRP A 358 VAL A 420 SER A 428 HOH A 972
SITE 2 AC2 6 HOH A1091 HOH A1147
SITE 1 AC3 7 GLN B 249 TYR B 359 GLU B 363 ASN B 368
SITE 2 AC3 7 HOH B 956 HOH B1129 HOH B1130
SITE 1 AC4 6 GLN B 191 TRP B 358 VAL B 420 SER B 428
SITE 2 AC4 6 HEM B 500 HOH B1138
SITE 1 AC5 4 CYS A 96 CYS A 101 CYS B 96 CYS B 101
SITE 1 AC6 11 TRP A 180 ARG A 185 CYS A 186 PHE A 355
SITE 2 AC6 11 SER A 356 TRP A 358 TRP A 449 PHE A 475
SITE 3 AC6 11 TYR A 477 INE A 760 HOH A1008
SITE 1 AC7 8 PRO A 336 PHE A 355 GLY A 357 TRP A 358
SITE 2 AC7 8 TYR A 359 MET A 360 GLU A 363 HEM A 500
SITE 1 AC8 11 SER A 104 ARG A 367 TRP A 449 GOL A 880
SITE 2 AC8 11 HOH A1035 TRP B 76 TRP B 447 PHE B 462
SITE 3 AC8 11 HIS B 463 GLN B 464 GLU B 465
SITE 1 AC9 4 CYS A 384 GLN A 437 ARG A 440 GLY A 441
SITE 1 BC1 12 TRP B 180 ARG B 185 CYS B 186 PHE B 355
SITE 2 BC1 12 SER B 356 TRP B 358 GLU B 363 TRP B 449
SITE 3 BC1 12 TYR B 477 INE B 761 ACT B 861 HOH B1130
SITE 1 BC2 9 PRO B 336 PHE B 355 SER B 356 GLY B 357
SITE 2 BC2 9 TRP B 358 TYR B 359 MET B 360 GLU B 363
SITE 3 BC2 9 HEM B 500
SITE 1 BC3 10 TRP A 76 TRP A 447 PHE A 462 HIS A 463
SITE 2 BC3 10 GLN A 464 GLU A 465 SER B 104 ARG B 367
SITE 3 BC3 10 TRP B 449 HOH B1016
SITE 1 BC4 2 TYR B 83 CYS B 384
SITE 1 BC5 4 ARG A 367 HIS A 373 HOH A1035 INE B 765
SITE 1 BC6 5 TRP A 76 HIS B 373 HOH B1007 HOH B1016
SITE 2 BC6 5 HOH B1091
CRYST1 57.590 106.060 155.780 90.00 90.00 90.00 P 21 21 21 8
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 0.017364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009429 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006419 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
