HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 31-JAN-17 5UO4
TITLE STRUCTURE OF HUMAN NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
TITLE 2 COMPLEX WITH 3-[(2-AMINO-4-METHYLQUINOLIN-7-YL)METHOXY]-5-(2-
TITLE 3 (METHYLAMINO)ETHYL)BENZONITRILE
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 BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC, OXIDE, SYNTHASE, INHIBITOR, COMPLEX, HEME, ENZYME,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 5 06-MAR-24 5UO4 1 REMARK LINK
REVDAT 4 25-DEC-19 5UO4 1 REMARK
REVDAT 3 13-SEP-17 5UO4 1 REMARK
REVDAT 2 24-MAY-17 5UO4 1 JRNL
REVDAT 1 03-MAY-17 5UO4 0
JRNL AUTH M.A.CINELLI,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN
JRNL TITL NITRILE IN THE HOLE: DISCOVERY OF A SMALL AUXILIARY POCKET
JRNL TITL 2 IN NEURONAL NITRIC OXIDE SYNTHASE LEADING TO THE DEVELOPMENT
JRNL TITL 3 OF POTENT AND SELECTIVE 2-AMINOQUINOLINE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 3958 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28422508
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00259
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 39.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 70879
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 3471
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 39.1430 - 6.1944 0.99 4404 196 0.1477 0.1667
REMARK 3 2 6.1944 - 4.9197 1.00 4424 213 0.1318 0.1708
REMARK 3 3 4.9197 - 4.2987 0.99 4400 226 0.1172 0.1640
REMARK 3 4 4.2987 - 3.9061 1.00 4397 240 0.1293 0.1833
REMARK 3 5 3.9061 - 3.6263 1.00 4395 245 0.1384 0.1824
REMARK 3 6 3.6263 - 3.4127 1.00 4402 232 0.1595 0.2213
REMARK 3 7 3.4127 - 3.2418 1.00 4438 217 0.1760 0.2744
REMARK 3 8 3.2418 - 3.1008 0.99 4375 216 0.1855 0.2207
REMARK 3 9 3.1008 - 2.9814 1.00 4458 230 0.1798 0.2566
REMARK 3 10 2.9814 - 2.8786 1.00 4402 222 0.1844 0.2366
REMARK 3 11 2.8786 - 2.7886 1.00 4441 202 0.1958 0.2718
REMARK 3 12 2.7886 - 2.7089 1.00 4472 191 0.2167 0.2537
REMARK 3 13 2.7089 - 2.6376 1.00 4381 254 0.1954 0.2632
REMARK 3 14 2.6376 - 2.5733 0.99 4417 234 0.1904 0.2886
REMARK 3 15 2.5733 - 2.5148 1.00 4357 220 0.2006 0.2527
REMARK 3 16 2.5148 - 2.4613 0.99 4400 264 0.2226 0.2693
REMARK 3 17 2.4613 - 2.4121 0.99 4349 229 0.2365 0.3128
REMARK 3 18 2.4121 - 2.3666 0.99 4366 254 0.2315 0.2894
REMARK 3 19 2.3666 - 2.3243 0.99 4413 245 0.2541 0.3113
REMARK 3 20 2.3243 - 2.2849 0.98 4291 201 0.2884 0.3654
REMARK 3 21 2.2849 - 2.2480 0.95 4253 196 0.4066 0.4887
REMARK 3 22 2.2480 - 2.2135 0.86 3789 188 0.4184 0.4560
REMARK 3 23 2.2135 - 2.1809 0.81 3548 170 0.3459 0.3440
REMARK 3 24 2.1809 - 2.1502 0.99 4461 195 0.3214 0.3625
REMARK 3 25 2.1502 - 2.1211 0.99 4302 235 0.3391 0.3943
REMARK 3 26 2.1211 - 2.0936 0.99 4376 221 0.3462 0.4291
REMARK 3 27 2.0936 - 2.0674 0.98 4376 255 0.3610 0.4254
REMARK 3 28 2.0674 - 2.0425 0.92 4060 209 0.3660 0.4038
REMARK 3 29 2.0425 - 2.0188 0.89 3875 199 0.3671 0.4340
REMARK 3 30 2.0188 - 1.9961 0.68 3039 167 0.4038 0.4420
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.320
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 : 0.007 7159
REMARK 3 ANGLE : 1.089 9740
REMARK 3 CHIRALITY : 0.040 1000
REMARK 3 PLANARITY : 0.005 1226
REMARK 3 DIHEDRAL : 14.816 2609
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): 117.6778 250.2090 361.2303
REMARK 3 T TENSOR
REMARK 3 T11: 0.2167 T22: 0.3749
REMARK 3 T33: 0.2627 T12: -0.0175
REMARK 3 T13: 0.0347 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 0.5611 L22: 0.8821
REMARK 3 L33: 1.4218 L12: -0.2020
REMARK 3 L13: 0.0062 L23: 0.1731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: 0.0258 S13: 0.0360
REMARK 3 S21: -0.0395 S22: -0.0770 S23: -0.0337
REMARK 3 S31: 0.0826 S32: 0.0790 S33: 0.0514
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 304:721)
REMARK 3 ORIGIN FOR THE GROUP (A): 116.1149 248.7699 323.8094
REMARK 3 T TENSOR
REMARK 3 T11: 0.2779 T22: 0.4214
REMARK 3 T33: 0.2723 T12: 0.0078
REMARK 3 T13: 0.0295 T23: -0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 0.5310 L22: 0.6457
REMARK 3 L33: 2.1833 L12: -0.1359
REMARK 3 L13: 0.0341 L23: 0.1757
REMARK 3 S TENSOR
REMARK 3 S11: 0.0609 S12: 0.0679 S13: -0.0001
REMARK 3 S21: -0.0448 S22: -0.0828 S23: 0.0868
REMARK 3 S31: 0.0012 S32: -0.2030 S33: 0.0271
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 5UO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000223050.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-16
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 : 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) : 0.979
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS OCT15, 2015
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72937
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : 0.13200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
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) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 3.55900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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: NULL
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, 35 MM CITRIC ACID, 65 MM
REMARK 280 BIS-TRIS PROPANE, 10% GLYCEROL, 5 MM TCEP, PH 7.2, VAPOR
REMARK 280 DIFFUSION, 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 26.19600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.59850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.25750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.59850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.19600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.25750
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: 10350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 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: 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 O HOH A 1137 O HOH A 1164 2.06
REMARK 500 OE1 GLU A 578 O HOH A 901 2.19
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 -4.96 68.15
REMARK 500 GLU A 351 -1.73 87.27
REMARK 500 SER A 397 14.72 59.81
REMARK 500 THR A 471 -85.08 -114.62
REMARK 500 CYS A 587 54.88 -157.03
REMARK 500 ARG A 608 -133.10 -118.98
REMARK 500 CYS A 677 105.07 -160.27
REMARK 500 THR B 396 -0.81 -145.80
REMARK 500 THR B 471 -80.65 -111.98
REMARK 500 CYS B 587 57.22 -157.84
REMARK 500 ARG B 608 -135.22 -116.29
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 807 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 331 SG
REMARK 620 2 CYS A 336 SG 111.0
REMARK 620 3 CYS B 331 SG 120.1 104.6
REMARK 620 4 CYS B 336 SG 104.3 100.8 114.5
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 101.0
REMARK 620 3 HEM A 801 NB 96.2 85.6
REMARK 620 4 HEM A 801 NC 96.3 162.6 90.6
REMARK 620 5 HEM A 801 ND 103.2 90.7 160.5 87.2
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 99.4
REMARK 620 3 HEM B 801 NB 97.1 85.2
REMARK 620 4 HEM B 801 NC 97.1 163.3 90.4
REMARK 620 5 HEM B 801 ND 103.6 91.5 159.3 86.9
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 8F1 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8F1 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 805
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UNR RELATED DB: PDB
REMARK 900 RELATED ID: 5UNU RELATED DB: PDB
REMARK 900 RELATED ID: 5UNX RELATED DB: PDB
REMARK 900 RELATED ID: 5UNW RELATED DB: PDB
REMARK 900 RELATED ID: 5UO1 RELATED DB: PDB
REMARK 900 RELATED ID: 5UNY RELATED DB: PDB
REMARK 900 RELATED ID: 5UO3 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO5 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO6 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO7 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO8 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO2 RELATED DB: PDB
REMARK 900 RELATED ID: 5UNS RELATED DB: PDB
REMARK 900 RELATED ID: 5UNZ RELATED DB: PDB
REMARK 900 RELATED ID: 5UO0 RELATED DB: PDB
REMARK 900 RELATED ID: 5UNT RELATED DB: PDB
REMARK 900 RELATED ID: 5UNV RELATED DB: PDB
REMARK 900 RELATED ID: 5UOD RELATED DB: PDB
REMARK 900 RELATED ID: 5UO9 RELATED DB: PDB
REMARK 900 RELATED ID: 5UOA RELATED DB: PDB
REMARK 900 RELATED ID: 5UOB RELATED DB: PDB
REMARK 900 RELATED ID: 5UOC RELATED DB: PDB
DBREF 5UO4 A 302 722 UNP P29475 NOS1_HUMAN 302 722
DBREF 5UO4 B 302 722 UNP P29475 NOS1_HUMAN 302 722
SEQADV 5UO4 ALA A 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5UO4 ASP A 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQADV 5UO4 ALA B 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5UO4 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 8F1 A 803 26
HET GOL A 804 6
HET GOL A 805 6
HET GOL A 806 6
HET ZN A 807 1
HET HEM B 801 43
HET H4B B 802 17
HET 8F1 B 803 26
HET GOL B 804 6
HET GOL B 805 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM 8F1 3-[(2-AMINO-4-METHYLQUINOLIN-7-YL)METHOXY]-5-[2-
HETNAM 2 8F1 (METHYLAMINO)ETHYL]BENZONITRILE
HETNAM GOL GLYCEROL
HETNAM ZN ZINC ION
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 8F1 2(C21 H22 N4 O)
FORMUL 6 GOL 5(C3 H8 O3)
FORMUL 9 ZN ZN 2+
FORMUL 15 HOH *503(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 THR A 693 5 5
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 GLY B 514 1 12
HELIX 28 AD1 PRO B 542 VAL B 546 5 5
HELIX 29 AD2 PHE B 556 GLY B 563 5 8
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 HIS B 719 1 6
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 807 1555 1555 2.34
LINK SG CYS A 336 ZN ZN A 807 1555 1555 2.34
LINK SG CYS A 420 FE HEM A 801 1555 1555 2.37
LINK ZN ZN A 807 SG CYS B 331 1555 1555 2.31
LINK ZN ZN A 807 SG CYS B 336 1555 1555 2.36
LINK SG CYS B 420 FE HEM B 801 1555 1555 2.34
CISPEP 1 THR A 706 PRO A 707 0 -0.70
CISPEP 2 THR B 706 PRO B 707 0 3.89
SITE 1 AC1 15 TRP A 414 ARG A 419 CYS A 420 VAL A 421
SITE 2 AC1 15 PHE A 589 SER A 590 TRP A 592 MET A 594
SITE 3 AC1 15 GLU A 597 TRP A 683 PHE A 709 TYR A 711
SITE 4 AC1 15 8F1 A 803 HOH A 915 HOH A 943
SITE 1 AC2 14 SER A 339 ARG A 601 VAL A 682 TRP A 683
SITE 2 AC2 14 HEM A 801 HOH A 943 HOH A 987 HOH A1024
SITE 3 AC2 14 HOH A1034 TRP B 681 PHE B 696 HIS B 697
SITE 4 AC2 14 GLN B 698 GLU B 699
SITE 1 AC3 10 PRO A 570 VAL A 572 ASN A 574 PHE A 589
SITE 2 AC3 10 TRP A 592 TYR A 593 GLU A 597 TYR A 711
SITE 3 AC3 10 HEM A 801 HOH A 940
SITE 1 AC4 1 ARG A 304
SITE 1 AC5 4 GLN A 369 ARG A 674 HOH A 966 HOH A1077
SITE 1 AC6 5 PHE A 377 ASN A 717 HIS A 719 HOH A 948
SITE 2 AC6 5 HOH A 961
SITE 1 AC7 4 CYS A 331 CYS A 336 CYS B 331 CYS B 336
SITE 1 AC8 15 TRP B 414 ARG B 419 CYS B 420 SER B 462
SITE 2 AC8 15 MET B 575 PHE B 589 SER B 590 TRP B 592
SITE 3 AC8 15 GLU B 597 TRP B 683 TYR B 711 8F1 B 803
SITE 4 AC8 15 HOH B 920 HOH B 937 HOH B1005
SITE 1 AC9 14 TRP A 681 PHE A 696 HIS A 697 GLN A 698
SITE 2 AC9 14 GLU A 699 SER B 339 ARG B 601 VAL B 682
SITE 3 AC9 14 TRP B 683 HEM B 801 HOH B 920 HOH B 988
SITE 4 AC9 14 HOH B 989 HOH B1037
SITE 1 AD1 10 PRO B 570 VAL B 572 ASN B 574 PHE B 589
SITE 2 AD1 10 TRP B 592 TYR B 593 GLU B 597 TYR B 711
SITE 3 AD1 10 HEM B 801 HOH B 920
SITE 1 AD2 3 GLN B 369 ARG B 674 HOH B1008
SITE 1 AD3 7 GLN A 647 SER A 658 LYS B 625 THR B 626
SITE 2 AD3 7 SER B 627 HOH B 969 HOH B1065
CRYST1 52.392 122.515 165.197 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 0.019087 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008162 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006053 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
