HEADER OXIDOREDUCTASE/INHIBITOR 19-MAY-17 5VV2
TITLE STRUCTURE OF HUMAN NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
TITLE 2 COMPLEX WITH 7-(((3-(5-FLUOROPYRIDIN-3-YL)PROPYL)AMINO)METHYL)
TITLE 3 QUINOLIN-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 302-722;
COMPND 5 SYNONYM: CONSTITUTIVE NOS,NC-NOS,NOS TYPE I,NEURONAL NOS,NNOS,
COMPND 6 PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1,BNOS;
COMPND 7 EC: 1.14.13.39;
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 ORGAN: BRAIN;
SOURCE 6 GENE: NOS1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC OXIDE SYNTHASE, INHIBITOR COMPLEX, HEME ENZYME,
KEYWDS 2 OXIDOREDUCTASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.HUIYING,L.P.THOMAS
REVDAT 4 04-OCT-23 5VV2 1 LINK
REVDAT 3 25-DEC-19 5VV2 1 REMARK
REVDAT 2 06-SEP-17 5VV2 1 JRNL
REVDAT 1 23-AUG-17 5VV2 0
JRNL AUTH A.V.PENSA,M.A.CINELLI,H.LI,G.CHREIFI,P.MUKHERJEE,L.J.ROMAN,
JRNL AUTH 2 P.MARTASEK,T.L.POULOS,R.B.SILVERMAN
JRNL TITL HYDROPHILIC, POTENT, AND SELECTIVE 7-SUBSTITUTED
JRNL TITL 2 2-AMINOQUINOLINES AS IMPROVED HUMAN NEURONAL NITRIC OXIDE
JRNL TITL 3 SYNTHASE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 7146 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28776992
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00835
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 72281
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 3533
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 68.4035 - 6.2130 1.00 4398 193 0.1523 0.1771
REMARK 3 2 6.2130 - 4.9319 1.00 4394 213 0.1413 0.1658
REMARK 3 3 4.9319 - 4.3085 1.00 4346 224 0.1174 0.1714
REMARK 3 4 4.3085 - 3.9147 1.00 4384 225 0.1248 0.1665
REMARK 3 5 3.9147 - 3.6341 1.00 4363 254 0.1391 0.1935
REMARK 3 6 3.6341 - 3.4198 1.00 4347 229 0.1473 0.1940
REMARK 3 7 3.4198 - 3.2486 1.00 4376 223 0.1526 0.2204
REMARK 3 8 3.2486 - 3.1072 1.00 4374 209 0.1779 0.2201
REMARK 3 9 3.1072 - 2.9875 1.00 4397 220 0.1779 0.2170
REMARK 3 10 2.9875 - 2.8845 1.00 4358 222 0.1741 0.2217
REMARK 3 11 2.8845 - 2.7943 1.00 4417 202 0.1781 0.1990
REMARK 3 12 2.7943 - 2.7144 1.00 4365 200 0.1870 0.2239
REMARK 3 13 2.7144 - 2.6429 1.00 4348 242 0.2138 0.2778
REMARK 3 14 2.6429 - 2.5784 1.00 4406 230 0.2192 0.3071
REMARK 3 15 2.5784 - 2.5198 1.00 4369 224 0.2229 0.2567
REMARK 3 16 2.5198 - 2.4662 1.00 4343 252 0.2477 0.2830
REMARK 3 17 2.4662 - 2.4169 1.00 4334 253 0.2581 0.3097
REMARK 3 18 2.4169 - 2.3713 1.00 4310 226 0.2504 0.3188
REMARK 3 19 2.3713 - 2.3289 1.00 4368 258 0.2681 0.3139
REMARK 3 20 2.3289 - 2.2894 1.00 4375 206 0.2667 0.3035
REMARK 3 21 2.2894 - 2.2525 0.99 4366 211 0.2972 0.3228
REMARK 3 22 2.2525 - 2.2178 0.99 4376 228 0.3213 0.3324
REMARK 3 23 2.2178 - 2.1852 0.99 4314 201 0.3087 0.3122
REMARK 3 24 2.1852 - 2.1544 0.99 4431 200 0.3193 0.3890
REMARK 3 25 2.1544 - 2.1253 1.00 4390 243 0.3405 0.3569
REMARK 3 26 2.1253 - 2.0977 1.00 4273 227 0.3426 0.4007
REMARK 3 27 2.0977 - 2.0715 1.00 4388 246 0.3586 0.4057
REMARK 3 28 2.0715 - 2.0465 0.99 4363 211 0.3919 0.4028
REMARK 3 29 2.0465 - 2.0227 1.00 4300 232 0.3702 0.4188
REMARK 3 30 2.0227 - 2.0000 0.99 4364 202 0.3907 0.4162
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.820
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 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 : 0.008 7117
REMARK 3 ANGLE : 1.134 9695
REMARK 3 CHIRALITY : 0.071 1001
REMARK 3 PLANARITY : 0.004 1226
REMARK 3 DIHEDRAL : 14.872 2595
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): 117.5089 249.1258 360.7703
REMARK 3 T TENSOR
REMARK 3 T11: 0.1507 T22: 0.2240
REMARK 3 T33: 0.2119 T12: -0.0223
REMARK 3 T13: 0.0337 T23: 0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.8692 L22: 1.0491
REMARK 3 L33: 2.4800 L12: -0.1688
REMARK 3 L13: -0.0625 L23: 0.1957
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: -0.0251 S13: 0.0259
REMARK 3 S21: -0.0563 S22: -0.0764 S23: -0.0307
REMARK 3 S31: 0.1182 S32: 0.1424 S33: 0.0621
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 304:721)
REMARK 3 ORIGIN FOR THE GROUP (A): 116.2031 247.9853 323.5343
REMARK 3 T TENSOR
REMARK 3 T11: 0.1952 T22: 0.2803
REMARK 3 T33: 0.2362 T12: 0.0024
REMARK 3 T13: 0.0300 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 0.7396 L22: 0.9439
REMARK 3 L33: 3.9881 L12: -0.2558
REMARK 3 L13: -0.2059 L23: 0.2022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: 0.1306 S13: -0.0158
REMARK 3 S21: -0.0893 S22: -0.1104 S23: 0.1149
REMARK 3 S31: 0.0018 S32: -0.2962 S33: 0.0479
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000223554.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 0.7.1
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72495
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 69.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : 0.14000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 1.99100
REMARK 200 R SYM FOR SHELL (I) : 1.99100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.8.0049
REMARK 200 STARTING MODEL: 4UH5
REMARK 200
REMARK 200 REMARK: PLATE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG3350 35MM CITRIC ACID 65MM BIS
REMARK 280 -TRIS-PROPANE 10% GLYCEROL 5MM TCEP, PH 7.2, 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 26.18000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.04000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.18000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.04000
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: 9350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 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 465 LYS B 722
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 -2.88 69.04
REMARK 500 THR A 471 -86.49 -112.79
REMARK 500 CYS A 587 58.02 -151.90
REMARK 500 ARG A 608 -133.65 -117.61
REMARK 500 THR B 396 -3.10 -142.33
REMARK 500 THR B 471 -73.07 -116.11
REMARK 500 CYS B 587 58.81 -149.93
REMARK 500 ARG B 608 -132.15 -112.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1211 DISTANCE = 5.97 ANGSTROMS
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 804 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 331 SG
REMARK 620 2 CYS A 336 SG 108.3
REMARK 620 3 CYS B 331 SG 122.3 105.6
REMARK 620 4 CYS B 336 SG 104.1 96.7 116.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 420 SG
REMARK 620 2 HEM A 801 NA 98.6
REMARK 620 3 HEM A 801 NB 97.9 84.6
REMARK 620 4 HEM A 801 NC 101.1 160.3 90.6
REMARK 620 5 HEM A 801 ND 103.8 89.6 158.1 87.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 420 SG
REMARK 620 2 HEM B 801 NA 98.1
REMARK 620 3 HEM B 801 NB 101.7 85.5
REMARK 620 4 HEM B 801 NC 98.5 163.4 89.9
REMARK 620 5 HEM B 801 ND 98.3 91.8 160.0 87.0
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9P4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9P4 B 803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VUP RELATED DB: PDB
REMARK 900 RELATED ID: 5VUR RELATED DB: PDB
REMARK 900 RELATED ID: 5VUT RELATED DB: PDB
REMARK 900 RELATED ID: 5VUU RELATED DB: PDB
REMARK 900 RELATED ID: 5VUS RELATED DB: PDB
REMARK 900 RELATED ID: 5VV4 RELATED DB: PDB
REMARK 900 RELATED ID: 5VUI RELATED DB: PDB
REMARK 900 RELATED ID: 5VUM RELATED DB: PDB
REMARK 900 RELATED ID: 5VUO RELATED DB: PDB
REMARK 900 RELATED ID: 5VUV RELATED DB: PDB
REMARK 900 RELATED ID: 5VUZ RELATED DB: PDB
REMARK 900 RELATED ID: 5VV1 RELATED DB: PDB
REMARK 900 RELATED ID: 5VUW RELATED DB: PDB
REMARK 900 RELATED ID: 5VUX RELATED DB: PDB
REMARK 900 RELATED ID: 5VUY RELATED DB: PDB
REMARK 900 RELATED ID: 5VV3 RELATED DB: PDB
REMARK 900 RELATED ID: 5VUL RELATED DB: PDB
REMARK 900 RELATED ID: 5VUQ RELATED DB: PDB
REMARK 900 RELATED ID: 5VV5 RELATED DB: PDB
REMARK 900 RELATED ID: 5VV6 RELATED DB: PDB
REMARK 900 RELATED ID: 5VVN RELATED DB: PDB
REMARK 900 RELATED ID: 5VV8 RELATED DB: PDB
REMARK 900 RELATED ID: 5VV9 RELATED DB: PDB
REMARK 900 RELATED ID: 5VVA RELATED DB: PDB
REMARK 900 RELATED ID: 5VVB RELATED DB: PDB
REMARK 900 RELATED ID: 5VVD RELATED DB: PDB
REMARK 900 RELATED ID: 5VUJ RELATED DB: PDB
REMARK 900 RELATED ID: 5VUK RELATED DB: PDB
REMARK 900 RELATED ID: 5VUN RELATED DB: PDB
REMARK 900 RELATED ID: 5VV0 RELATED DB: PDB
REMARK 900 RELATED ID: 5VV7 RELATED DB: PDB
REMARK 900 RELATED ID: 5VVC RELATED DB: PDB
REMARK 900 RELATED ID: 5VVG RELATED DB: PDB
DBREF 5VV2 A 302 722 UNP P29475 NOS1_HUMAN 302 722
DBREF 5VV2 B 302 722 UNP P29475 NOS1_HUMAN 302 722
SEQADV 5VV2 ALA A 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5VV2 ASP A 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQADV 5VV2 ALA B 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5VV2 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 801 43
HET H4B A 802 17
HET 9P4 A 803 23
HET ZN A 804 1
HET HEM B 801 43
HET H4B B 802 17
HET 9P4 B 803 23
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM 9P4 7-({[3-(5-FLUOROPYRIDIN-3-YL)PROPYL]AMINO}METHYL)
HETNAM 2 9P4 QUINOLIN-2-AMINE
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 9P4 2(C18 H19 F N4)
FORMUL 6 ZN ZN 2+
FORMUL 10 HOH *528(H2 O)
HELIX 1 AA1 THR A 320 SER A 325 5 6
HELIX 2 AA2 THR A 355 ILE A 374 1 20
HELIX 3 AA3 SER A 379 SER A 397 1 19
HELIX 4 AA4 LYS A 402 ASN A 416 1 15
HELIX 5 AA5 GLY A 422 TRP A 426 5 5
HELIX 6 AA6 THR A 439 ASN A 456 1 18
HELIX 7 AA7 LYS A 457 ASN A 459 5 3
HELIX 8 AA8 ASN A 503 GLN A 513 1 11
HELIX 9 AA9 PRO A 542 VAL A 546 5 5
HELIX 10 AB1 PHE A 556 GLY A 563 5 8
HELIX 11 AB2 GLY A 595 VAL A 600 1 6
HELIX 12 AB3 VAL A 600 ASP A 605 1 6
HELIX 13 AB4 ILE A 611 MET A 619 1 9
HELIX 14 AB5 LYS A 625 SER A 628 5 4
HELIX 15 AB6 LEU A 629 ASP A 649 1 21
HELIX 16 AB7 ASP A 655 GLY A 675 1 21
HELIX 17 AB8 ASP A 680 VAL A 685 1 6
HELIX 18 AB9 SER A 689 GLN A 698 5 10
HELIX 19 AC1 ASP A 714 THR A 718 5 5
HELIX 20 AC2 THR B 320 SER B 325 5 6
HELIX 21 AC3 THR B 355 ILE B 374 1 20
HELIX 22 AC4 SER B 379 SER B 397 1 19
HELIX 23 AC5 LYS B 402 ASN B 416 1 15
HELIX 24 AC6 GLY B 422 TRP B 426 5 5
HELIX 25 AC7 THR B 439 ASN B 456 1 18
HELIX 26 AC8 LYS B 457 ASN B 459 5 3
HELIX 27 AC9 ASN B 503 GLN B 513 1 11
HELIX 28 AD1 PRO B 542 VAL B 546 5 5
HELIX 29 AD2 TRP B 558 GLY B 563 5 6
HELIX 30 AD3 GLY B 595 VAL B 600 1 6
HELIX 31 AD4 VAL B 600 ASP B 605 1 6
HELIX 32 AD5 ILE B 611 MET B 619 1 9
HELIX 33 AD6 LYS B 625 SER B 628 5 4
HELIX 34 AD7 LEU B 629 ASP B 649 1 21
HELIX 35 AD8 ASP B 655 GLY B 675 1 21
HELIX 36 AD9 ASP B 680 VAL B 685 1 6
HELIX 37 AE1 SER B 689 GLN B 698 5 10
HELIX 38 AE2 ASP B 714 THR B 718 5 5
SHEET 1 AA1 2 LEU A 306 LYS A 309 0
SHEET 2 AA1 2 VAL A 316 ASP A 319 -1 O ASP A 319 N LEU A 306
SHEET 1 AA2 4 GLN A 430 ASP A 433 0
SHEET 2 AA2 4 ALA A 463 ILE A 466 1 O ILE A 464 N PHE A 432
SHEET 3 AA2 4 PHE A 589 SER A 590 -1 O SER A 590 N ALA A 463
SHEET 4 AA2 4 ALA A 571 VAL A 572 -1 N VAL A 572 O PHE A 589
SHEET 1 AA3 3 ARG A 478 VAL A 479 0
SHEET 2 AA3 3 LEU A 527 GLN A 530 -1 O GLN A 530 N ARG A 478
SHEET 3 AA3 3 GLU A 537 PHE A 539 -1 O PHE A 539 N LEU A 527
SHEET 1 AA4 2 GLY A 489 LYS A 491 0
SHEET 2 AA4 2 THR A 497 GLY A 499 -1 O LEU A 498 N TYR A 490
SHEET 1 AA5 2 GLU A 548 PRO A 550 0
SHEET 2 AA5 2 LYS A 565 TYR A 567 -1 O TRP A 566 N VAL A 549
SHEET 1 AA6 3 LEU A 582 PHE A 584 0
SHEET 2 AA6 3 LEU A 576 ILE A 579 -1 N LEU A 577 O PHE A 584
SHEET 3 AA6 3 SER A 708 GLU A 710 -1 O GLU A 710 N LEU A 576
SHEET 1 AA7 2 TYR A 593 MET A 594 0
SHEET 2 AA7 2 ILE A 653 VAL A 654 1 O VAL A 654 N TYR A 593
SHEET 1 AA8 2 LEU B 306 LYS B 309 0
SHEET 2 AA8 2 VAL B 316 ASP B 319 -1 O ASP B 319 N LEU B 306
SHEET 1 AA9 4 GLN B 430 ASP B 433 0
SHEET 2 AA9 4 ALA B 463 ILE B 466 1 O ILE B 464 N PHE B 432
SHEET 3 AA9 4 PHE B 589 SER B 590 -1 O SER B 590 N ALA B 463
SHEET 4 AA9 4 ALA B 571 VAL B 572 -1 N VAL B 572 O PHE B 589
SHEET 1 AB1 3 ARG B 478 VAL B 479 0
SHEET 2 AB1 3 LEU B 527 GLN B 530 -1 O GLN B 530 N ARG B 478
SHEET 3 AB1 3 GLU B 537 PHE B 539 -1 O PHE B 539 N LEU B 527
SHEET 1 AB2 2 GLY B 489 LYS B 491 0
SHEET 2 AB2 2 THR B 497 GLY B 499 -1 O LEU B 498 N TYR B 490
SHEET 1 AB3 2 GLU B 548 PRO B 550 0
SHEET 2 AB3 2 LYS B 565 TYR B 567 -1 O TRP B 566 N VAL B 549
SHEET 1 AB4 3 LEU B 582 PHE B 584 0
SHEET 2 AB4 3 LEU B 576 ILE B 579 -1 N LEU B 577 O PHE B 584
SHEET 3 AB4 3 SER B 708 GLU B 710 -1 O GLU B 710 N LEU B 576
SHEET 1 AB5 2 TYR B 593 MET B 594 0
SHEET 2 AB5 2 ILE B 653 VAL B 654 1 O VAL B 654 N TYR B 593
LINK SG CYS A 331 ZN ZN A 804 1555 1555 2.33
LINK SG CYS A 336 ZN ZN A 804 1555 1555 2.37
LINK SG CYS A 420 FE HEM A 801 1555 1555 2.34
LINK ZN ZN A 804 SG CYS B 331 1555 1555 2.32
LINK ZN ZN A 804 SG CYS B 336 1555 1555 2.35
LINK SG CYS B 420 FE HEM B 801 1555 1555 2.35
CISPEP 1 THR A 706 PRO A 707 0 -2.59
CISPEP 2 THR B 706 PRO B 707 0 -2.51
CISPEP 3 THR B 706 PRO B 707 0 -0.82
SITE 1 AC1 17 TRP A 414 ALA A 417 ARG A 419 CYS A 420
SITE 2 AC1 17 PHE A 589 SER A 590 TRP A 592 GLU A 597
SITE 3 AC1 17 TRP A 683 PHE A 709 TYR A 711 H4B A 802
SITE 4 AC1 17 9P4 A 803 HOH A 909 HOH A 937 HOH A 975
SITE 5 AC1 17 HOH A1068
SITE 1 AC2 15 SER A 339 ARG A 601 VAL A 682 TRP A 683
SITE 2 AC2 15 HEM A 801 HOH A 931 HOH A 938 HOH A 975
SITE 3 AC2 15 HOH A1040 HOH A1069 TRP B 681 PHE B 696
SITE 4 AC2 15 HIS B 697 GLN B 698 GLU B 699
SITE 1 AC3 8 MET A 341 HIS A 342 VAL A 572 TRP A 592
SITE 2 AC3 8 GLU A 597 HEM A 801 HOH A 909 HOH A1145
SITE 1 AC4 4 CYS A 331 CYS A 336 CYS B 331 CYS B 336
SITE 1 AC5 17 TRP B 414 ARG B 419 CYS B 420 SER B 462
SITE 2 AC5 17 PHE B 589 SER B 590 TRP B 592 GLU B 597
SITE 3 AC5 17 TRP B 683 PHE B 709 TYR B 711 H4B B 802
SITE 4 AC5 17 9P4 B 803 HOH B 910 HOH B 917 HOH B 944
SITE 5 AC5 17 HOH B 967
SITE 1 AC6 16 TRP A 681 PHE A 696 HIS A 697 GLN A 698
SITE 2 AC6 16 GLU A 699 SER B 339 MET B 341 ARG B 601
SITE 3 AC6 16 VAL B 682 TRP B 683 HEM B 801 HOH B 942
SITE 4 AC6 16 HOH B 944 HOH B 955 HOH B 992 HOH B1009
SITE 1 AC7 8 TRP A 311 MET B 341 HIS B 342 VAL B 572
SITE 2 AC7 8 TRP B 592 GLU B 597 HEM B 801 HOH B 967
CRYST1 52.360 122.080 165.030 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 0.019099 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008191 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
