HEADER OXIDOREDUCTASE 20-AUG-15 5ADI
TITLE STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN IN
TITLE 2 COMPLEX WITH 7-(((5-((METHYLAMINO)METHYL)PYRIDIN-3-YL)OXY)
TITLE 3 METHYL)QUINOLIN-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 302-721;
COMPND 5 SYNONYM: CONSTITUTIVE NOS, NC-NOS, NOS TYPE I, NEURONAL NOS, N-NOS,
COMPND 6 NNOS, PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1, BNOS, NEURONAL NITRIC
COMPND 7 OXIDE SYNTHASE;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PCWORI
KEYWDS OXIDOREDUCTASE, NITRIC OXIDE SYNTHASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 2 25-NOV-15 5ADI 1 JRNL
REVDAT 1 28-OCT-15 5ADI 0
JRNL AUTH M.A.CINELLI,H.LI,A.V.PENSA,S.KANG,L.J.ROMAN,P.MARTASEK,
JRNL AUTH 2 T.L.POULOS,R.B.SILVERMAN
JRNL TITL PHENYL ETHER- AND ANILINE-CONTAINING 2-AMINOQUINOLINES AS
JRNL TITL 2 POTENT AND SELECTIVE INHIBITORS OF NEURONAL NITRIC OXIDE
JRNL TITL 3 SYNTHASE.
JRNL REF J.MED.CHEM. V. 58 8694 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 26469213
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01330
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.200
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.309
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.00
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.85
REMARK 3 NUMBER OF REFLECTIONS : 54597
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1872
REMARK 3 R VALUE (WORKING SET) : 0.1846
REMARK 3 FREE R VALUE : 0.2368
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 5063
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 68.3418 - 6.8338 1.00 3305 135 0.1606 0.2004
REMARK 3 2 6.8338 - 5.4249 1.00 3299 164 0.1575 0.2057
REMARK 3 3 5.4249 - 4.7393 1.00 3241 163 0.1341 0.1888
REMARK 3 4 4.7393 - 4.3061 1.00 3302 173 0.1199 0.1563
REMARK 3 5 4.3061 - 3.9975 1.00 3300 167 0.1265 0.2005
REMARK 3 6 3.9975 - 3.7618 1.00 3276 179 0.1332 0.1854
REMARK 3 7 3.7618 - 3.5734 1.00 3300 185 0.1372 0.1934
REMARK 3 8 3.5734 - 3.4179 1.00 3236 179 0.1498 0.1938
REMARK 3 9 3.4179 - 3.2863 1.00 3281 170 0.1698 0.2283
REMARK 3 10 3.2863 - 3.1729 1.00 3310 165 0.1746 0.2341
REMARK 3 11 3.1729 - 3.0737 1.00 3268 149 0.1783 0.2398
REMARK 3 12 3.0737 - 2.9858 1.00 3309 164 0.1867 0.2198
REMARK 3 13 2.9858 - 2.9072 1.00 3255 178 0.1932 0.2574
REMARK 3 14 2.9072 - 2.8363 1.00 3326 152 0.2103 0.2826
REMARK 3 15 2.8363 - 2.7718 1.00 3285 155 0.2263 0.2935
REMARK 3 16 2.7718 - 2.7128 1.00 3354 140 0.2291 0.3071
REMARK 3 17 2.7128 - 2.6586 0.99 3240 174 0.2444 0.2854
REMARK 3 18 2.6586 - 2.6084 1.00 3201 199 0.2456 0.3057
REMARK 3 19 2.6084 - 2.5618 1.00 3340 158 0.2381 0.3128
REMARK 3 20 2.5618 - 2.5184 1.00 3300 169 0.2535 0.2676
REMARK 3 21 2.5184 - 2.4778 1.00 3221 181 0.2619 0.3238
REMARK 3 22 2.4778 - 2.4396 1.00 3309 191 0.2843 0.3566
REMARK 3 23 2.4396 - 2.4038 1.00 3253 174 0.2871 0.3229
REMARK 3 24 2.4038 - 2.3699 1.00 3223 197 0.2881 0.3590
REMARK 3 25 2.3699 - 2.3379 1.00 3302 188 0.2994 0.3215
REMARK 3 26 2.3379 - 2.3075 1.00 3286 155 0.3083 0.3433
REMARK 3 27 2.3075 - 2.2787 1.00 3253 176 0.3371 0.3644
REMARK 3 28 2.2787 - 2.2512 1.00 3328 144 0.3441 0.4035
REMARK 3 29 2.2512 - 2.2250 0.99 3269 178 0.3626 0.4194
REMARK 3 30 2.2250 - 2.2000 1.00 3303 161 0.3507 0.4121
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.31
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.98
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 7114
REMARK 3 ANGLE : 1.135 9684
REMARK 3 CHIRALITY : 0.071 996
REMARK 3 PLANARITY : 0.005 1221
REMARK 3 DIHEDRAL : 15.163 2581
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 302:721)
REMARK 3 ORIGIN FOR THE GROUP (A): 117.2316 250.4667 359.1951
REMARK 3 T TENSOR
REMARK 3 T11: 0.1502 T22: 0.2179
REMARK 3 T33: 0.2341 T12: -0.0170
REMARK 3 T13: 0.0451 T23: 0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 0.5137 L22: 0.9329
REMARK 3 L33: 1.7748 L12: -0.1669
REMARK 3 L13: 0.1256 L23: 0.2398
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: 0.0088 S13: 0.0250
REMARK 3 S21: -0.0604 S22: -0.0526 S23: -0.0531
REMARK 3 S31: 0.0656 S32: 0.1709 S33: 0.0376
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 302:721)
REMARK 3 ORIGIN FOR THE GROUP (A): 115.7749 249.3145 322.0441
REMARK 3 T TENSOR
REMARK 3 T11: 0.1992 T22: 0.2468
REMARK 3 T33: 0.2594 T12: -0.0196
REMARK 3 T13: 0.0382 T23: -0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 0.3943 L22: 0.7664
REMARK 3 L33: 2.8998 L12: -0.2758
REMARK 3 L13: -0.0172 L23: 0.0347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: 0.0498 S13: -0.0227
REMARK 3 S21: 0.0166 S22: -0.0744 S23: 0.0896
REMARK 3 S31: 0.0400 S32: -0.0692 S33: 0.0655
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESIDUES 344 TO 351 IN CHAIN A AND 344 TO 353 IN CHAIN B
REMARK 3 ARE DISORDERED
REMARK 4
REMARK 4 5ADI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-AUG-15.
REMARK 100 THE PDBE ID CODE IS EBI-64746.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
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 : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (Q315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54717
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.9
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.10
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) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.0
REMARK 200 R MERGE FOR SHELL (I) : 1.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: OVERALL RMERGE 0.132 RPIM 0.099 CC ONE HALF 0.989
REMARK 200 HIGHEST RESOLUTION SHELL RMERGE 1.695 RPIM 1.298 CC ONE
REMARK 200 HALF 0.301
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-9% PED3350 40MM CITRIC ACID
REMARK 280 60MM BISTRISPROPANE 10% GLYCEROL 5MM TCEP
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 26.10500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.10500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.40000
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: 9320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.5 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 344
REMARK 465 GLN A 345
REMARK 465 HIS A 346
REMARK 465 ALA A 347
REMARK 465 ARG A 348
REMARK 465 ARG A 349
REMARK 465 PRO A 350
REMARK 465 GLU A 351
REMARK 465 CYS B 302
REMARK 465 PRO B 303
REMARK 465 SER B 344
REMARK 465 GLN B 345
REMARK 465 HIS B 346
REMARK 465 ALA B 347
REMARK 465 ARG B 348
REMARK 465 ARG B 349
REMARK 465 PRO B 350
REMARK 465 GLU B 351
REMARK 465 ASP B 352
REMARK 465 VAL B 353
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 722 CA C O CB CG CD CE NZ
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 711 O1D HEM B 750 2.15
REMARK 500 O HOH A 2039 O HOH A 2073 2.09
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 GLU A 314 -3.27 66.50
REMARK 500 THR A 471 -86.80 -113.74
REMARK 500 CYS A 587 56.92 -152.50
REMARK 500 ARG A 608 -125.42 -120.10
REMARK 500 CYS A 677 94.36 -163.05
REMARK 500 ARG B 376 31.96 -142.31
REMARK 500 THR B 471 -79.42 -108.62
REMARK 500 ASP B 494 20.38 -71.70
REMARK 500 ARG B 608 -138.63 -123.21
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 HEM A 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 420 SG
REMARK 620 2 HEM A 750 NB 98.6
REMARK 620 3 HEM A 750 NC 96.2 86.3
REMARK 620 4 HEM A 750 NA 101.3 89.7 162.4
REMARK 620 5 HEM A 750 ND 101.1 160.2 90.4 87.5
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 HEM B 750 NB
REMARK 620 2 HEM B 750 NA 84.0
REMARK 620 3 CYS B 420 SG 98.1 100.7
REMARK 620 4 HEM B 750 ND 160.3 91.4 101.7
REMARK 620 5 HEM B 750 NC 89.6 163.2 95.6 89.5
REMARK 620 N 1 2 3 4
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 336 SG
REMARK 620 2 CYS B 336 SG 102.0
REMARK 620 3 CYS A 331 SG 114.1 102.2
REMARK 620 4 CYS B 331 SG 104.4 113.9 119.2
REMARK 620 N 1 2 3
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 TUE A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TUE B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TUE B 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AD4 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((3-(2-(DIMETHYLAMINO)ETHYL)
REMARK 900 PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5AD5 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((3-(2-(METHYLAMINO)ETHYL)
REMARK 900 PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5AD6 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((3-(DIMETHYLAMINO)METHYL)
REMARK 900 PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5AD7 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((3-(METHYLAMINO)METHYL)
REMARK 900 PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5AD8 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((3-AMINOMETHYL)PHENOXY)
REMARK 900 METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5AD9 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((4-(DIMETHYLAMINO)METHYL)
REMARK 900 PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADA RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-(((3-((DIMETHYLAMINO)METHYL)
REMARK 900 PHENYL)AMINO)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADB RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((4-CHLORO-3-((METHYLAMINO)
REMARK 900 METHYL)PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADC RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-(((5-((METHYLAMINO)METHYL)
REMARK 900 PYRIDIN-3-YL)OXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADD RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 7-((3-(METHYLAMINO)METHYL)
REMARK 900 PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADE RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE M336V
REMARK 900 D597N MUTANT HEME DOMAIN IN COMPLEX WITH 7-((4-
REMARK 900 CHLORO-3-((METHYLAMINO)METHYL)PHENOXY)METHYL)QUINOLIN-2
REMARK 900 -AMINE
REMARK 900 RELATED ID: 5ADF RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN
REMARK 900 IN COMPLEX WITH 7-(((3-((DIMETHYLAMINO)METHYL)PHENYL)
REMARK 900 AMINO)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADG RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN
REMARK 900 IN COMPLEX WITH 7-((4-CHLORO-3-((METHYLAMINO)METHYL
REMARK 900 )PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADJ RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH 7-((3-(2-(METHYLAMINO)
REMARK 900 ETHYL)PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADK RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH 7-((3-(DIMETHYLAMINO)
REMARK 900 METHYL)PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADL RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH 7-((3-(METHYLAMINO)METHYL
REMARK 900 )PHENOXY)METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADM RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH 7-((3-AMINOMETHYL)PHENOXY
REMARK 900 )METHYL)QUINOLIN-2-AMINE
REMARK 900 RELATED ID: 5ADN RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH 7-(((3-((DIMETHYLAMINO)
REMARK 900 METHYL)PHENYL)AMINO)METHYL)QUINOLIN-2-AMINE
DBREF 5ADI A 302 722 UNP P29475 NOS1_HUMAN 302 722
DBREF 5ADI B 302 722 UNP P29475 NOS1_HUMAN 302 722
SEQADV 5ADI ALA A 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5ADI ASP A 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQADV 5ADI ALA B 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5ADI ASP B 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQRES 1 A 421 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU
SEQRES 2 A 421 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 A 421 GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE
SEQRES 4 A 421 MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL
SEQRES 5 A 421 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 A 421 ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 A 421 LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 A 421 ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 A 421 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 A 421 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 A 421 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 A 421 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 A 421 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 A 421 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 A 421 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 A 421 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 A 421 CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE
SEQRES 18 A 421 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 A 421 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 421 VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP
SEQRES 21 A 421 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 A 421 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 A 421 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 421 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 A 421 GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR
SEQRES 26 A 421 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 A 421 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 A 421 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 A 421 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 A 421 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 A 421 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 A 421 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 A 421 THR HIS VAL TRP LYS
SEQRES 1 B 421 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU
SEQRES 2 B 421 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 B 421 GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE
SEQRES 4 B 421 MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL
SEQRES 5 B 421 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 B 421 ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 B 421 LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 B 421 ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 B 421 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 B 421 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 B 421 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 B 421 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 B 421 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 B 421 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 B 421 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 B 421 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 B 421 CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE
SEQRES 18 B 421 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 B 421 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 421 VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP
SEQRES 21 B 421 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 B 421 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 B 421 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 421 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 B 421 GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR
SEQRES 26 B 421 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 B 421 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 B 421 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 B 421 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 B 421 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 B 421 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 B 421 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 B 421 THR HIS VAL TRP LYS
HET HEM A 750 43
HET H4B A 760 17
HET TUE A 800 22
HET ZN A 900 1
HET HEM B 750 43
HET H4B B 760 17
HET TUE B 800 22
HET TUE B 801 22
HETNAM TUE 7-[[5-[(METHYLIDENEAMINO)METHYL]PYRIDIN-3-YL]
HETNAM 2 TUE OXYMETHYL]QUINOLIN-2-AMINE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ZN ZINC ION
HETSYN HEM HEME
FORMUL 2 TUE 3(C17 H16 N4 O)
FORMUL 3 H4B 2(C9 H15 N5 O3)
FORMUL 4 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 ZN ZN 2+
FORMUL 6 HOH *393(H2 O)
HELIX 1 1 THR A 320 SER A 325 5 6
HELIX 2 2 THR A 355 ILE A 374 1 20
HELIX 3 3 SER A 379 SER A 397 1 19
HELIX 4 4 LYS A 402 ASN A 416 1 15
HELIX 5 5 GLY A 422 TRP A 426 5 5
HELIX 6 6 THR A 439 ASN A 456 1 18
HELIX 7 7 LYS A 457 ASN A 459 5 3
HELIX 8 8 ASN A 503 GLN A 513 1 11
HELIX 9 9 PRO A 542 VAL A 546 5 5
HELIX 10 10 TRP A 558 GLY A 563 5 6
HELIX 11 11 GLY A 595 VAL A 600 1 6
HELIX 12 12 VAL A 600 ASP A 605 1 6
HELIX 13 13 ILE A 611 MET A 619 1 9
HELIX 14 14 LYS A 625 SER A 628 5 4
HELIX 15 15 LEU A 629 ASP A 649 1 21
HELIX 16 16 ASP A 655 ARG A 674 1 20
HELIX 17 17 ASP A 680 VAL A 685 1 6
HELIX 18 18 SER A 689 THR A 693 5 5
HELIX 19 19 ASP A 714 THR A 718 5 5
HELIX 20 20 THR B 320 SER B 325 5 6
HELIX 21 21 THR B 355 ILE B 374 1 20
HELIX 22 22 SER B 379 SER B 397 1 19
HELIX 23 23 LYS B 402 ASN B 416 1 15
HELIX 24 24 GLY B 422 TRP B 426 5 5
HELIX 25 25 THR B 439 ASN B 456 1 18
HELIX 26 26 LYS B 457 ASN B 459 5 3
HELIX 27 27 ASN B 503 GLN B 513 1 11
HELIX 28 28 PRO B 542 VAL B 546 5 5
HELIX 29 29 TRP B 558 GLY B 563 5 6
HELIX 30 30 GLY B 595 VAL B 600 1 6
HELIX 31 31 VAL B 600 ASP B 605 1 6
HELIX 32 32 ILE B 611 MET B 619 1 9
HELIX 33 33 LYS B 625 SER B 628 5 4
HELIX 34 34 LEU B 629 ASP B 649 1 21
HELIX 35 35 ASP B 655 GLY B 675 1 21
HELIX 36 36 ASP B 680 VAL B 685 1 6
HELIX 37 37 SER B 689 THR B 693 5 5
HELIX 38 38 THR B 693 HIS B 697 5 5
HELIX 39 39 ASP B 714 THR B 718 5 5
SHEET 1 AA 2 LEU A 306 LYS A 309 0
SHEET 2 AA 2 VAL A 316 ASP A 319 -1 O LEU A 317 N VAL A 308
SHEET 1 AB 4 GLN A 430 ASP A 433 0
SHEET 2 AB 4 ALA A 463 ILE A 466 1 O ILE A 464 N PHE A 432
SHEET 3 AB 4 PHE A 589 SER A 590 -1 O SER A 590 N ALA A 463
SHEET 4 AB 4 ALA A 571 VAL A 572 -1 O VAL A 572 N PHE A 589
SHEET 1 AC 3 ARG A 478 VAL A 479 0
SHEET 2 AC 3 LEU A 527 GLN A 530 -1 O GLN A 530 N ARG A 478
SHEET 3 AC 3 GLU A 537 PHE A 539 -1 O GLU A 537 N LEU A 529
SHEET 1 AD 2 GLY A 489 LYS A 491 0
SHEET 2 AD 2 THR A 497 GLY A 499 -1 O LEU A 498 N TYR A 490
SHEET 1 AE 2 GLU A 548 PRO A 550 0
SHEET 2 AE 2 LYS A 565 TYR A 567 -1 O TRP A 566 N VAL A 549
SHEET 1 AF 3 LEU A 582 PHE A 584 0
SHEET 2 AF 3 LEU A 576 ILE A 579 -1 O LEU A 577 N PHE A 584
SHEET 3 AF 3 SER A 708 GLU A 710 -1 O SER A 708 N GLU A 578
SHEET 1 AG 2 TYR A 593 MET A 594 0
SHEET 2 AG 2 ILE A 653 VAL A 654 1 N VAL A 654 O TYR A 593
SHEET 1 BA 2 LEU B 306 LYS B 309 0
SHEET 2 BA 2 VAL B 316 ASP B 319 -1 O LEU B 317 N VAL B 308
SHEET 1 BB 4 GLN B 430 ASP B 433 0
SHEET 2 BB 4 ALA B 463 ILE B 466 1 O ILE B 464 N PHE B 432
SHEET 3 BB 4 PHE B 589 SER B 590 -1 O SER B 590 N ALA B 463
SHEET 4 BB 4 ALA B 571 VAL B 572 -1 O VAL B 572 N PHE B 589
SHEET 1 BC 3 ARG B 478 VAL B 479 0
SHEET 2 BC 3 LEU B 527 GLN B 530 -1 O GLN B 530 N ARG B 478
SHEET 3 BC 3 GLU B 537 PHE B 539 -1 O GLU B 537 N LEU B 529
SHEET 1 BD 2 GLY B 489 LYS B 491 0
SHEET 2 BD 2 THR B 497 GLY B 499 -1 O LEU B 498 N TYR B 490
SHEET 1 BE 2 GLU B 548 PRO B 550 0
SHEET 2 BE 2 LYS B 565 TYR B 567 -1 O TRP B 566 N VAL B 549
SHEET 1 BF 3 LEU B 582 PHE B 584 0
SHEET 2 BF 3 LEU B 576 ILE B 579 -1 O LEU B 577 N PHE B 584
SHEET 3 BF 3 SER B 708 GLU B 710 -1 O SER B 708 N GLU B 578
SHEET 1 BG 2 TYR B 593 MET B 594 0
SHEET 2 BG 2 ILE B 653 VAL B 654 1 N VAL B 654 O TYR B 593
LINK SG CYS A 420 FE HEM A 750 1555 1555 2.38
LINK ZN ZN A 900 SG CYS B 331 1555 1555 2.36
LINK ZN ZN A 900 SG CYS A 336 1555 1555 2.34
LINK ZN ZN A 900 SG CYS B 336 1555 1555 2.26
LINK ZN ZN A 900 SG CYS A 331 1555 1555 2.31
LINK SG CYS B 420 FE HEM B 750 1555 1555 2.36
CISPEP 1 THR A 706 PRO A 707 0 -1.57
CISPEP 2 THR B 706 PRO B 707 0 0.85
SITE 1 AC1 14 TRP A 414 ARG A 419 CYS A 420 PHE A 589
SITE 2 AC1 14 SER A 590 TRP A 592 GLU A 597 TRP A 683
SITE 3 AC1 14 PHE A 709 TYR A 711 H4B A 760 TUE A 800
SITE 4 AC1 14 HOH A2227 HOH A2228
SITE 1 AC2 13 SER A 339 MET A 341 ARG A 601 VAL A 682
SITE 2 AC2 13 TRP A 683 HEM A 750 HOH A2214 HOH A2228
SITE 3 AC2 13 TRP B 681 PHE B 696 HIS B 697 GLN B 698
SITE 4 AC2 13 GLU B 699
SITE 1 AC3 7 VAL A 572 PHE A 589 TRP A 592 TYR A 593
SITE 2 AC3 7 GLU A 597 TYR A 711 HEM A 750
SITE 1 AC4 4 CYS A 331 CYS A 336 CYS B 331 CYS B 336
SITE 1 AC5 14 TRP B 414 ARG B 419 CYS B 420 SER B 462
SITE 2 AC5 14 PHE B 589 SER B 590 TRP B 592 GLU B 597
SITE 3 AC5 14 TRP B 683 PHE B 709 TYR B 711 H4B B 760
SITE 4 AC5 14 TUE B 800 HOH B2163
SITE 1 AC6 14 TRP A 681 PHE A 696 HIS A 697 GLN A 698
SITE 2 AC6 14 GLU A 699 SER B 339 MET B 341 ARG B 601
SITE 3 AC6 14 VAL B 682 TRP B 683 HEM B 750 TUE B 800
SITE 4 AC6 14 HOH B2156 HOH B2157
SITE 1 AC7 7 PRO B 570 VAL B 572 TRP B 592 GLU B 597
SITE 2 AC7 7 TYR B 711 HEM B 750 H4B B 760
SITE 1 AC8 7 PHE B 360 LYS B 364 MET B 383 LEU B 386
SITE 2 AC8 7 GLU B 387 ASN B 390 ASP B 394
CRYST1 52.210 122.800 164.400 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 0.019153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008143 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006083 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
