HEADER OXIDOREDUCTASE 21-JUN-10 3NLK
TITLE STRUCTURE OF NEURONAL NITRIC OXIDE SYNTHASE R349A MUTANT HEME DOMAIN
TITLE 2 IN COMPLEX WITH 6-{{(3'S,4'S)-3'-[2"-(3'''-FLUOROPHENETHYLAMINO)
TITLE 3 ETHOXY]PYRROLIDIN-4'-YL}METHYL}-4-METHYLPYRIDIN-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 297-718;
COMPND 5 SYNONYM: BNOS, NOS TYPE I, NEURONAL NOS, N-NOS, NNOS, CONSTITUTIVE
COMPND 6 NOS, NC-NOS;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: NOS1, BNOS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC OXIDE SYNTHASE, INHIBITOR, HEME ENZYME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,S.L.DELKER,T.L.POULOS
REVDAT 5 06-SEP-23 3NLK 1 REMARK SEQADV LINK
REVDAT 4 17-JUL-19 3NLK 1 REMARK
REVDAT 3 08-NOV-17 3NLK 1 REMARK
REVDAT 2 24-NOV-10 3NLK 1 JRNL
REVDAT 1 03-NOV-10 3NLK 0
JRNL AUTH H.JI,S.L.DELKER,H.LI,P.MARTASEK,L.J.ROMAN,T.L.POULOS,
JRNL AUTH 2 R.B.SILVERMAN
JRNL TITL EXPLORATION OF THE ACTIVE SITE OF NEURONAL NITRIC OXIDE
JRNL TITL 2 SYNTHASE BY THE DESIGN AND SYNTHESIS OF PYRROLIDINOMETHYL
JRNL TITL 3 2-AMINOPYRIDINE DERIVATIVES.
JRNL REF J.MED.CHEM. V. 53 7804 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 20958055
JRNL DOI 10.1021/JM100947X
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 59732
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3190
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) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4111
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 195
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 183
REMARK 3 SOLVENT ATOMS : 375
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.49000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : -2.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.884
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7039 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9577 ; 1.388 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 814 ; 5.722 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 330 ;33.955 ;23.879
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1163 ;14.653 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;18.988 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 992 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5394 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4081 ; 0.683 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6615 ; 1.228 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2958 ; 2.029 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2962 ; 3.116 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 299 A 860
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5180 4.6590 22.5650
REMARK 3 T TENSOR
REMARK 3 T11: 0.1336 T22: 0.2186
REMARK 3 T33: 0.0388 T12: 0.0089
REMARK 3 T13: 0.0201 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.5260 L22: 0.8402
REMARK 3 L33: 6.3488 L12: -0.1235
REMARK 3 L13: -0.4997 L23: 0.1703
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: 0.1509 S13: 0.0084
REMARK 3 S21: -0.0562 S22: -0.0914 S23: 0.0753
REMARK 3 S31: -0.0681 S32: -0.5398 S33: 0.0997
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 299 B 860
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5820 4.8560 59.9590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.1782
REMARK 3 T33: 0.0479 T12: -0.0057
REMARK 3 T13: 0.0451 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.6680 L22: 0.8149
REMARK 3 L33: 2.9701 L12: -0.1983
REMARK 3 L13: -0.2729 L23: 0.3681
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.0700 S13: 0.0877
REMARK 3 S21: -0.0780 S22: -0.0632 S23: -0.0184
REMARK 3 S31: 0.1189 S32: -0.0233 S33: 0.0667
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3NLK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059980.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62972
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.62800
REMARK 200 R SYM FOR SHELL (I) : 0.62800
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1OM4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350, 100MM MES, 100-140MM
REMARK 280 AMMONIUM ACETATE 5MM GSH, 35UM SDS, PH 5.8, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
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 26.03000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.35500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.35500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.03000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.07000
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: 9800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 CYS A 297
REMARK 465 PRO A 298
REMARK 465 SER A 339
REMARK 465 GLN A 340
REMARK 465 HIS A 341
REMARK 465 THR A 342
REMARK 465 ARG A 343
REMARK 465 LYS A 344
REMARK 465 PRO A 345
REMARK 465 GLU A 346
REMARK 465 ASP A 347
REMARK 465 VAL A 348
REMARK 465 ALA A 349
REMARK 465 LYS A 717
REMARK 465 GLY A 718
REMARK 465 CYS B 297
REMARK 465 PRO B 298
REMARK 465 SER B 339
REMARK 465 GLN B 340
REMARK 465 HIS B 341
REMARK 465 THR B 342
REMARK 465 ARG B 343
REMARK 465 LYS B 344
REMARK 465 PRO B 345
REMARK 465 GLU B 346
REMARK 465 ASP B 347
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 OH TYR B 706 O1D HEM B 750 1.96
REMARK 500 OH TYR A 706 O1D HEM A 750 2.05
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 SER A 392 -7.31 75.58
REMARK 500 THR A 466 -89.01 -111.76
REMARK 500 CYS A 582 61.57 -152.48
REMARK 500 ARG A 603 -134.43 -113.88
REMARK 500 THR A 713 -50.48 -143.15
REMARK 500 THR B 466 -90.53 -115.47
REMARK 500 CYS B 582 58.63 -150.26
REMARK 500 ARG B 603 -137.51 -112.96
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 326 SG
REMARK 620 2 CYS A 331 SG 113.0
REMARK 620 3 CYS B 326 SG 119.1 106.2
REMARK 620 4 CYS B 331 SG 105.0 101.0 111.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 415 SG
REMARK 620 2 HEM A 750 NA 97.0
REMARK 620 3 HEM A 750 NB 90.0 88.9
REMARK 620 4 HEM A 750 NC 90.0 173.0 90.9
REMARK 620 5 HEM A 750 ND 96.9 91.0 173.1 88.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 415 SG
REMARK 620 2 HEM B 750 NA 96.3
REMARK 620 3 HEM B 750 NB 93.4 88.0
REMARK 620 4 HEM B 750 NC 90.9 172.8 91.7
REMARK 620 5 HEM B 750 ND 92.8 91.8 173.7 87.7
REMARK 620 N 1 2 3 4
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 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JSS A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860
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 B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JSS B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NLD RELATED DB: PDB
REMARK 900 RELATED ID: 3NLE RELATED DB: PDB
REMARK 900 RELATED ID: 3NLF RELATED DB: PDB
REMARK 900 RELATED ID: 3NLG RELATED DB: PDB
REMARK 900 RELATED ID: 3NLH RELATED DB: PDB
REMARK 900 RELATED ID: 3NLI RELATED DB: PDB
REMARK 900 RELATED ID: 3NLJ RELATED DB: PDB
REMARK 900 RELATED ID: 3NLM RELATED DB: PDB
REMARK 900 RELATED ID: 3NLN RELATED DB: PDB
REMARK 900 RELATED ID: 3NLO RELATED DB: PDB
REMARK 900 RELATED ID: 3NLP RELATED DB: PDB
REMARK 900 RELATED ID: 3NLQ RELATED DB: PDB
REMARK 900 RELATED ID: 3NLR RELATED DB: PDB
REMARK 900 RELATED ID: 3NLT RELATED DB: PDB
REMARK 900 RELATED ID: 3NLU RELATED DB: PDB
REMARK 900 RELATED ID: 3NLV RELATED DB: PDB
REMARK 900 RELATED ID: 3NLW RELATED DB: PDB
REMARK 900 RELATED ID: 3NLX RELATED DB: PDB
REMARK 900 RELATED ID: 3NLY RELATED DB: PDB
REMARK 900 RELATED ID: 3NLZ RELATED DB: PDB
REMARK 900 RELATED ID: 3NM0 RELATED DB: PDB
DBREF 3NLK A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 3NLK B 297 718 UNP P29476 NOS1_RAT 297 718
SEQADV 3NLK ALA A 349 UNP P29476 ARG 349 ENGINEERED MUTATION
SEQADV 3NLK ALA B 349 UNP P29476 ARG 349 ENGINEERED MUTATION
SEQRES 1 A 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 A 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 A 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 A 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 A 422 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 A 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 A 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 A 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 A 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 A 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 A 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 A 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 A 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 A 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 A 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 A 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 A 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 A 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 A 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 A 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 A 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 A 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 A 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 A 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 A 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 A 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 A 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 A 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 A 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 A 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 A 422 THR HIS VAL TRP LYS GLY
SEQRES 1 B 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 B 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 B 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 B 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 B 422 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 B 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 B 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 B 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 B 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 B 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 B 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 B 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 B 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 B 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 B 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 B 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 B 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 B 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 B 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 B 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 B 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 B 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 B 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 B 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 B 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 B 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 B 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 B 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 B 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 B 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 B 422 THR HIS VAL TRP LYS GLY
HET HEM A 750 43
HET H4B A 760 17
HET JSS A 800 27
HET ACT A 860 4
HET ZN A 900 1
HET HEM B 750 43
HET H4B B 760 17
HET JSS B 800 27
HET ACT B 860 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM JSS 6-{[(3S,4S)-4-(2-{[2-(3-FLUOROPHENYL)
HETNAM 2 JSS ETHYL]AMINO}ETHOXY)PYRROLIDIN-3-YL]METHYL}-4-
HETNAM 3 JSS METHYLPYRIDIN-2-AMINE
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 JSS 2(C21 H29 F N4 O)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 7 ZN ZN 2+
FORMUL 12 HOH *375(H2 O)
HELIX 1 1 THR A 315 SER A 320 5 6
HELIX 2 2 THR A 350 ILE A 369 1 20
HELIX 3 3 SER A 374 SER A 392 1 19
HELIX 4 4 LYS A 397 ASN A 411 1 15
HELIX 5 5 GLY A 417 TRP A 421 5 5
HELIX 6 6 THR A 434 ASN A 451 1 18
HELIX 7 7 LYS A 452 ASN A 454 5 3
HELIX 8 8 ASN A 498 GLN A 508 1 11
HELIX 9 9 PRO A 537 VAL A 541 5 5
HELIX 10 10 PHE A 551 GLY A 558 5 8
HELIX 11 11 MET A 589 VAL A 595 1 7
HELIX 12 12 VAL A 595 ASP A 600 1 6
HELIX 13 13 ILE A 606 MET A 614 1 9
HELIX 14 14 LYS A 620 SER A 623 5 4
HELIX 15 15 LEU A 624 ASP A 644 1 21
HELIX 16 16 ASP A 650 GLY A 670 1 21
HELIX 17 17 ASP A 675 VAL A 680 1 6
HELIX 18 18 SER A 684 GLN A 693 5 10
HELIX 19 19 ASP A 709 THR A 713 5 5
HELIX 20 20 THR B 315 SER B 320 5 6
HELIX 21 21 THR B 350 ILE B 369 1 20
HELIX 22 22 SER B 374 SER B 392 1 19
HELIX 23 23 LYS B 397 ASN B 411 1 15
HELIX 24 24 GLY B 417 TRP B 421 5 5
HELIX 25 25 THR B 434 ASN B 451 1 18
HELIX 26 26 LYS B 452 ASN B 454 5 3
HELIX 27 27 ASN B 498 GLN B 508 1 11
HELIX 28 28 PRO B 537 VAL B 541 5 5
HELIX 29 29 PHE B 551 GLY B 558 5 8
HELIX 30 30 GLY B 590 VAL B 595 1 6
HELIX 31 31 VAL B 595 ASP B 600 1 6
HELIX 32 32 ILE B 606 MET B 614 1 9
HELIX 33 33 LYS B 620 SER B 623 5 4
HELIX 34 34 LEU B 624 ASP B 644 1 21
HELIX 35 35 ASP B 650 GLY B 670 1 21
HELIX 36 36 ASP B 675 VAL B 680 1 6
HELIX 37 37 SER B 684 GLN B 693 5 10
HELIX 38 38 ASP B 709 HIS B 714 1 6
SHEET 1 A 2 LEU A 301 LYS A 304 0
SHEET 2 A 2 VAL A 311 ASP A 314 -1 O ASP A 314 N LEU A 301
SHEET 1 B 4 GLN A 425 ASP A 428 0
SHEET 2 B 4 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 B 4 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 4 B 4 ALA A 566 VAL A 567 -1 N VAL A 567 O PHE A 584
SHEET 1 C 3 ARG A 473 VAL A 474 0
SHEET 2 C 3 LEU A 522 GLN A 525 -1 O GLN A 525 N ARG A 473
SHEET 3 C 3 GLU A 532 PHE A 534 -1 O PHE A 534 N LEU A 522
SHEET 1 D 2 GLY A 484 LYS A 486 0
SHEET 2 D 2 THR A 492 GLY A 494 -1 O LEU A 493 N TYR A 485
SHEET 1 E 2 GLU A 543 PRO A 545 0
SHEET 2 E 2 LYS A 560 TYR A 562 -1 O TRP A 561 N VAL A 544
SHEET 1 F 3 LEU A 577 PHE A 579 0
SHEET 2 F 3 LEU A 571 ILE A 574 -1 N LEU A 572 O PHE A 579
SHEET 3 F 3 SER A 703 GLU A 705 -1 O GLU A 705 N LEU A 571
SHEET 1 G 2 LEU B 301 LYS B 304 0
SHEET 2 G 2 VAL B 311 ASP B 314 -1 O ASP B 314 N LEU B 301
SHEET 1 H 4 GLN B 425 ASP B 428 0
SHEET 2 H 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 H 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 H 4 ALA B 566 VAL B 567 -1 N VAL B 567 O PHE B 584
SHEET 1 I 3 ARG B 473 VAL B 474 0
SHEET 2 I 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 I 3 GLU B 532 PHE B 534 -1 O PHE B 534 N LEU B 522
SHEET 1 J 2 GLY B 484 LYS B 486 0
SHEET 2 J 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 K 2 GLU B 543 PRO B 545 0
SHEET 2 K 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 L 3 LEU B 577 PHE B 579 0
SHEET 2 L 3 LEU B 571 ILE B 574 -1 N LEU B 572 O PHE B 579
SHEET 3 L 3 SER B 703 GLU B 705 -1 O GLU B 705 N LEU B 571
SHEET 1 M 2 TYR B 588 MET B 589 0
SHEET 2 M 2 ILE B 648 VAL B 649 1 O VAL B 649 N TYR B 588
LINK SG CYS A 326 ZN ZN A 900 1555 1555 2.33
LINK SG CYS A 331 ZN ZN A 900 1555 1555 2.33
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.41
LINK ZN ZN A 900 SG CYS B 326 1555 1555 2.44
LINK ZN ZN A 900 SG CYS B 331 1555 1555 2.46
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.48
CISPEP 1 THR A 701 PRO A 702 0 -0.63
CISPEP 2 THR B 701 PRO B 702 0 -0.43
SITE 1 AC1 15 TRP A 409 CYS A 415 SER A 457 PHE A 584
SITE 2 AC1 15 SER A 585 GLY A 586 TRP A 587 GLU A 592
SITE 3 AC1 15 TRP A 678 TYR A 706 H4B A 760 JSS A 800
SITE 4 AC1 15 HOH A1041 HOH A1049 HOH A1107
SITE 1 AC2 15 SER A 334 MET A 336 ARG A 596 VAL A 677
SITE 2 AC2 15 TRP A 678 HEM A 750 HOH A1005 HOH A1032
SITE 3 AC2 15 HOH A1041 HOH A1046 TRP B 676 PHE B 691
SITE 4 AC2 15 HIS B 692 GLN B 693 GLU B 694
SITE 1 AC3 10 MET A 336 LEU A 337 GLN A 478 VAL A 567
SITE 2 AC3 10 GLY A 586 TRP A 587 GLU A 592 HEM A 750
SITE 3 AC3 10 HOH A1002 TRP B 306
SITE 1 AC4 2 TRP A 587 HOH A1114
SITE 1 AC5 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC6 14 TRP B 409 CYS B 415 PHE B 584 SER B 585
SITE 2 AC6 14 TRP B 587 GLU B 592 TRP B 678 PHE B 704
SITE 3 AC6 14 TYR B 706 H4B B 760 JSS B 800 HOH B1027
SITE 4 AC6 14 HOH B1033 HOH B1073
SITE 1 AC7 15 TRP A 676 PHE A 691 HIS A 692 GLN A 693
SITE 2 AC7 15 GLU A 694 SER B 334 MET B 336 ARG B 596
SITE 3 AC7 15 VAL B 677 TRP B 678 HEM B 750 HOH B1023
SITE 4 AC7 15 HOH B1033 HOH B1039 HOH B1201
SITE 1 AC8 11 MET B 336 LEU B 337 GLN B 478 VAL B 567
SITE 2 AC8 11 PHE B 584 GLY B 586 TRP B 587 TYR B 588
SITE 3 AC8 11 GLU B 592 HEM B 750 HOH B1001
SITE 1 AC9 4 GLN B 420 TRP B 587 HOH B1194 HOH B1195
CRYST1 52.060 112.140 164.710 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 0.019209 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008917 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006071 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
