HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 28-JAN-11 3QJ5
TITLE S-NITROSOGLUTATHIONE REDUCTASE (GSNOR) IN COMPLEX WITH N6022
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE CLASS-3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALCOHOL DEHYDROGENASE 5, ALCOHOL DEHYDROGENASE CLASS CHI
COMPND 5 CHAIN, ALCOHOL DEHYDROGENASE CLASS-III, GLUTATHIONE-DEPENDENT
COMPND 6 FORMALDEHYDE DEHYDROGENASE, FALDH, FDH, GSH-FDH, S-(HYDROXYMETHYL)
COMPND 7 GLUTATHIONE DEHYDROGENASE;
COMPND 8 EC: 1.1.1.1, 1.1.1.-, 1.1.1.284;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADH5, ADHX, FDH;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: VCID 1792
KEYWDS S-NITROSOGLUTATHIONE REDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CHUN,H.KIM,X.SUN
REVDAT 5 03-APR-24 3QJ5 1 REMARK
REVDAT 4 21-FEB-24 3QJ5 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3QJ5 1 REMARK
REVDAT 2 09-DEC-15 3QJ5 1 JRNL VERSN
REVDAT 1 06-APR-11 3QJ5 0
JRNL AUTH X.SUN,J.W.WASLEY,J.QIU,J.P.BLONDER,A.M.STOUT,L.S.GREEN,
JRNL AUTH 2 S.A.STRONG,D.B.COLAGIOVANNI,J.P.RICHARDS,S.C.MUTKA,L.CHUN,
JRNL AUTH 3 G.J.ROSENTHAL
JRNL TITL DISCOVERY OF S-NITROSOGLUTATHIONE REDUCTASE INHIBITORS:
JRNL TITL 2 POTENTIAL AGENTS FOR THE TREATMENT OF ASTHMA AND OTHER
JRNL TITL 3 INFLAMMATORY DISEASES.
JRNL REF ACS MED CHEM LETT V. 2 402 2011
JRNL REFN ISSN 1948-5875
JRNL PMID 24900320
JRNL DOI 10.1021/ML200045S
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 77982
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3927
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5159
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 272
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5539
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 233
REMARK 3 SOLVENT ATOMS : 740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.24000
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): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.765
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5904 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7985 ; 1.259 ; 2.009
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 753 ; 5.617 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 193 ;33.857 ;24.819
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 997 ;11.993 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;12.259 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 911 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4254 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2949 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4029 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 671 ; 0.111 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.028 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.163 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.095 ; 0.200
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): 3696 ; 0.399 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5963 ; 0.777 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2226 ; 1.290 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2017 ; 2.263 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3QJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063710.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9774
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78296
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: DIRECT REFINEMENT
REMARK 200 STARTING MODEL: NATIVE GSNOR STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 8000, 100MM K-PHOSPHATE PH
REMARK 280 7.0, 100MM ZNSO4, 1MM DTT, 3% (W/V) BUTANEDIOL, TEMPERATURE 290K,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, PH 7.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 155.03900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.42900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.42900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 232.55850
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.42900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.42900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.51950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.42900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.42900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 232.55850
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.42900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.42900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.51950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 155.03900
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: 8060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 0
REMARK 465 ALA A 1
REMARK 465 SER B 0
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 LEU A 64 -167.57 -79.62
REMARK 500 THR A 142 -50.20 -123.77
REMARK 500 PHE A 145 48.88 -82.39
REMARK 500 CYS A 173 -83.48 -152.70
REMARK 500 TRP A 285 -2.09 -140.87
REMARK 500 VAL A 341 -49.30 -132.88
REMARK 500 ILE A 367 -67.60 -100.93
REMARK 500 ASN B 2 -104.45 -170.93
REMARK 500 CYS B 173 -78.41 -152.54
REMARK 500 ILE B 268 -51.66 -130.69
REMARK 500 VAL B 341 -48.66 -131.29
REMARK 500 ILE B 367 -67.28 -98.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 1PE IS THE ORDERED PART OF PEG 8000
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 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 44 SG
REMARK 620 2 HIS A 66 NE2 102.2
REMARK 620 3 CYS A 173 SG 140.1 111.3
REMARK 620 4 022 A 374 N5 95.5 104.3 96.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 99 SG 107.6
REMARK 620 3 CYS A 102 SG 116.3 105.8
REMARK 620 4 CYS A 110 SG 106.1 119.0 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 602 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 186 O
REMARK 620 2 LYS A 187 O 65.0
REMARK 620 3 GLU A 189 OE2 140.1 85.5
REMARK 620 4 TYR A 263 OH 87.5 91.6 66.0
REMARK 620 5 HOH A 581 O 88.8 151.8 111.4 76.2
REMARK 620 6 HOH A 691 O 79.3 104.5 136.6 152.2 79.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 456 O
REMARK 620 2 HOH A 626 O 71.6
REMARK 620 3 ALA B 186 O 76.2 87.3
REMARK 620 4 LYS B 187 O 106.6 151.1 64.8
REMARK 620 5 GLU B 189 OE2 141.1 114.3 140.0 85.6
REMARK 620 6 TYR B 263 OH 147.1 79.6 87.0 90.9 66.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 44 SG
REMARK 620 2 HIS B 66 NE2 102.2
REMARK 620 3 CYS B 173 SG 135.6 112.2
REMARK 620 4 022 B 377 N5 97.1 106.9 98.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 96 SG
REMARK 620 2 CYS B 99 SG 109.3
REMARK 620 3 CYS B 102 SG 115.0 106.3
REMARK 620 4 CYS B 110 SG 105.1 117.8 103.6
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 ZN A 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 374
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 022 A 374
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 022 B 377
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 377
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N2P B 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N2P B 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N2P A 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 380
DBREF 3QJ5 A 1 373 UNP P11766 ADHX_HUMAN 2 374
DBREF 3QJ5 B 1 373 UNP P11766 ADHX_HUMAN 2 374
SEQADV 3QJ5 SER A 0 UNP P11766 EXPRESSION TAG
SEQADV 3QJ5 SER B 0 UNP P11766 EXPRESSION TAG
SEQRES 1 A 374 SER ALA ASN GLU VAL ILE LYS CYS LYS ALA ALA VAL ALA
SEQRES 2 A 374 TRP GLU ALA GLY LYS PRO LEU SER ILE GLU GLU ILE GLU
SEQRES 3 A 374 VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS ILE
SEQRES 4 A 374 ILE ALA THR ALA VAL CYS HIS THR ASP ALA TYR THR LEU
SEQRES 5 A 374 SER GLY ALA ASP PRO GLU GLY CYS PHE PRO VAL ILE LEU
SEQRES 6 A 374 GLY HIS GLU GLY ALA GLY ILE VAL GLU SER VAL GLY GLU
SEQRES 7 A 374 GLY VAL THR LYS LEU LYS ALA GLY ASP THR VAL ILE PRO
SEQRES 8 A 374 LEU TYR ILE PRO GLN CYS GLY GLU CYS LYS PHE CYS LEU
SEQRES 9 A 374 ASN PRO LYS THR ASN LEU CYS GLN LYS ILE ARG VAL THR
SEQRES 10 A 374 GLN GLY LYS GLY LEU MET PRO ASP GLY THR SER ARG PHE
SEQRES 11 A 374 THR CYS LYS GLY LYS THR ILE LEU HIS TYR MET GLY THR
SEQRES 12 A 374 SER THR PHE SER GLU TYR THR VAL VAL ALA ASP ILE SER
SEQRES 13 A 374 VAL ALA LYS ILE ASP PRO LEU ALA PRO LEU ASP LYS VAL
SEQRES 14 A 374 CYS LEU LEU GLY CYS GLY ILE SER THR GLY TYR GLY ALA
SEQRES 15 A 374 ALA VAL ASN THR ALA LYS LEU GLU PRO GLY SER VAL CYS
SEQRES 16 A 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU ALA VAL ILE
SEQRES 17 A 374 MET GLY CYS LYS VAL ALA GLY ALA SER ARG ILE ILE GLY
SEQRES 18 A 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA ARG ALA LYS GLU
SEQRES 19 A 374 PHE GLY ALA THR GLU CYS ILE ASN PRO GLN ASP PHE SER
SEQRES 20 A 374 LYS PRO ILE GLN GLU VAL LEU ILE GLU MET THR ASP GLY
SEQRES 21 A 374 GLY VAL ASP TYR SER PHE GLU CYS ILE GLY ASN VAL LYS
SEQRES 22 A 374 VAL MET ARG ALA ALA LEU GLU ALA CYS HIS LYS GLY TRP
SEQRES 23 A 374 GLY VAL SER VAL VAL VAL GLY VAL ALA ALA SER GLY GLU
SEQRES 24 A 374 GLU ILE ALA THR ARG PRO PHE GLN LEU VAL THR GLY ARG
SEQRES 25 A 374 THR TRP LYS GLY THR ALA PHE GLY GLY TRP LYS SER VAL
SEQRES 26 A 374 GLU SER VAL PRO LYS LEU VAL SER GLU TYR MET SER LYS
SEQRES 27 A 374 LYS ILE LYS VAL ASP GLU PHE VAL THR HIS ASN LEU SER
SEQRES 28 A 374 PHE ASP GLU ILE ASN LYS ALA PHE GLU LEU MET HIS SER
SEQRES 29 A 374 GLY LYS SER ILE ARG THR VAL VAL LYS ILE
SEQRES 1 B 374 SER ALA ASN GLU VAL ILE LYS CYS LYS ALA ALA VAL ALA
SEQRES 2 B 374 TRP GLU ALA GLY LYS PRO LEU SER ILE GLU GLU ILE GLU
SEQRES 3 B 374 VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS ILE
SEQRES 4 B 374 ILE ALA THR ALA VAL CYS HIS THR ASP ALA TYR THR LEU
SEQRES 5 B 374 SER GLY ALA ASP PRO GLU GLY CYS PHE PRO VAL ILE LEU
SEQRES 6 B 374 GLY HIS GLU GLY ALA GLY ILE VAL GLU SER VAL GLY GLU
SEQRES 7 B 374 GLY VAL THR LYS LEU LYS ALA GLY ASP THR VAL ILE PRO
SEQRES 8 B 374 LEU TYR ILE PRO GLN CYS GLY GLU CYS LYS PHE CYS LEU
SEQRES 9 B 374 ASN PRO LYS THR ASN LEU CYS GLN LYS ILE ARG VAL THR
SEQRES 10 B 374 GLN GLY LYS GLY LEU MET PRO ASP GLY THR SER ARG PHE
SEQRES 11 B 374 THR CYS LYS GLY LYS THR ILE LEU HIS TYR MET GLY THR
SEQRES 12 B 374 SER THR PHE SER GLU TYR THR VAL VAL ALA ASP ILE SER
SEQRES 13 B 374 VAL ALA LYS ILE ASP PRO LEU ALA PRO LEU ASP LYS VAL
SEQRES 14 B 374 CYS LEU LEU GLY CYS GLY ILE SER THR GLY TYR GLY ALA
SEQRES 15 B 374 ALA VAL ASN THR ALA LYS LEU GLU PRO GLY SER VAL CYS
SEQRES 16 B 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU ALA VAL ILE
SEQRES 17 B 374 MET GLY CYS LYS VAL ALA GLY ALA SER ARG ILE ILE GLY
SEQRES 18 B 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA ARG ALA LYS GLU
SEQRES 19 B 374 PHE GLY ALA THR GLU CYS ILE ASN PRO GLN ASP PHE SER
SEQRES 20 B 374 LYS PRO ILE GLN GLU VAL LEU ILE GLU MET THR ASP GLY
SEQRES 21 B 374 GLY VAL ASP TYR SER PHE GLU CYS ILE GLY ASN VAL LYS
SEQRES 22 B 374 VAL MET ARG ALA ALA LEU GLU ALA CYS HIS LYS GLY TRP
SEQRES 23 B 374 GLY VAL SER VAL VAL VAL GLY VAL ALA ALA SER GLY GLU
SEQRES 24 B 374 GLU ILE ALA THR ARG PRO PHE GLN LEU VAL THR GLY ARG
SEQRES 25 B 374 THR TRP LYS GLY THR ALA PHE GLY GLY TRP LYS SER VAL
SEQRES 26 B 374 GLU SER VAL PRO LYS LEU VAL SER GLU TYR MET SER LYS
SEQRES 27 B 374 LYS ILE LYS VAL ASP GLU PHE VAL THR HIS ASN LEU SER
SEQRES 28 B 374 PHE ASP GLU ILE ASN LYS ALA PHE GLU LEU MET HIS SER
SEQRES 29 B 374 GLY LYS SER ILE ARG THR VAL VAL LYS ILE
HET ZN A 375 1
HET ZN A 376 1
HET K A 602 1
HET NAD A 500 44
HET 022 A 374 31
HET 1PE A 377 16
HET 1PE A 378 16
HET N2P A 379 7
HET TRS A 380 8
HET ZN B 375 1
HET ZN B 376 1
HET K B 501 1
HET NAD B 374 44
HET 022 B 377 31
HET 1PE B 378 16
HET N2P B 379 7
HET N2P B 380 7
HETNAM ZN ZINC ION
HETNAM K POTASSIUM ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 022 3-{1-(4-CARBAMOYL-2-METHYLPHENYL)-5-[4-(1H-IMIDAZOL-1-
HETNAM 2 022 YL)PHENYL]-1H-PYRROL-2-YL}PROPANOIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM N2P PENTANE-1,5-DIAMINE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN 022 N6022
HETSYN 1PE PEG400
HETSYN TRS TRIS BUFFER
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 K 2(K 1+)
FORMUL 6 NAD 2(C21 H27 N7 O14 P2)
FORMUL 7 022 2(C24 H22 N4 O3)
FORMUL 8 1PE 3(C10 H22 O6)
FORMUL 10 N2P 3(C5 H14 N2)
FORMUL 11 TRS C4 H12 N O3 1+
FORMUL 20 HOH *740(H2 O)
HELIX 1 1 CYS A 44 GLY A 53 1 10
HELIX 2 2 ILE A 113 LYS A 119 1 7
HELIX 3 3 PRO A 164 CYS A 169 1 6
HELIX 4 4 LEU A 170 GLY A 172 5 3
HELIX 5 5 CYS A 173 ASN A 184 1 12
HELIX 6 6 GLY A 200 ALA A 213 1 14
HELIX 7 7 ASN A 224 ASP A 226 5 3
HELIX 8 8 LYS A 227 GLY A 235 1 9
HELIX 9 9 ASN A 241 PHE A 245 5 5
HELIX 10 10 PRO A 248 THR A 257 1 10
HELIX 11 11 ASN A 270 ALA A 280 1 11
HELIX 12 12 PRO A 304 THR A 309 1 6
HELIX 13 13 ALA A 317 TRP A 321 5 5
HELIX 14 14 LYS A 322 SER A 336 1 15
HELIX 15 15 VAL A 341 GLU A 343 5 3
HELIX 16 16 GLU A 353 SER A 363 1 11
HELIX 17 17 CYS B 44 SER B 52 1 9
HELIX 18 18 CYS B 99 ASN B 104 1 6
HELIX 19 19 ILE B 113 LYS B 119 1 7
HELIX 20 20 PRO B 164 CYS B 169 1 6
HELIX 21 21 LEU B 170 GLY B 172 5 3
HELIX 22 22 CYS B 173 ASN B 184 1 12
HELIX 23 23 GLY B 200 ALA B 213 1 14
HELIX 24 24 ASN B 224 ASP B 226 5 3
HELIX 25 25 LYS B 227 GLY B 235 1 9
HELIX 26 26 ASN B 241 PHE B 245 5 5
HELIX 27 27 PRO B 248 THR B 257 1 10
HELIX 28 28 ASN B 270 ALA B 280 1 11
HELIX 29 29 PRO B 304 THR B 309 1 6
HELIX 30 30 ALA B 317 TRP B 321 5 5
HELIX 31 31 LYS B 322 SER B 336 1 15
HELIX 32 32 VAL B 341 GLU B 343 5 3
HELIX 33 33 GLU B 353 SER B 363 1 11
SHEET 1 A 4 ILE A 5 VAL A 11 0
SHEET 2 A 4 SER A 20 VAL A 26 -1 O SER A 20 N VAL A 11
SHEET 3 A 4 PHE A 129 CYS A 131 -1 O THR A 130 N GLU A 25
SHEET 4 A 4 LYS A 134 ILE A 136 -1 O ILE A 136 N PHE A 129
SHEET 1 B 5 TYR A 148 ALA A 152 0
SHEET 2 B 5 GLU A 33 ALA A 42 -1 N VAL A 34 O VAL A 151
SHEET 3 B 5 GLU A 67 VAL A 75 -1 O ILE A 71 N LYS A 37
SHEET 4 B 5 THR A 87 PRO A 90 -1 O VAL A 88 N GLY A 70
SHEET 5 B 5 VAL A 156 LYS A 158 -1 O ALA A 157 N ILE A 89
SHEET 1 C 4 TYR A 148 ALA A 152 0
SHEET 2 C 4 GLU A 33 ALA A 42 -1 N VAL A 34 O VAL A 151
SHEET 3 C 4 ARG A 368 LYS A 372 -1 O VAL A 371 N THR A 41
SHEET 4 C 4 VAL A 345 SER A 350 1 N LEU A 349 O LYS A 372
SHEET 1 D 6 GLU A 238 ILE A 240 0
SHEET 2 D 6 ARG A 217 VAL A 221 1 N GLY A 220 O ILE A 240
SHEET 3 D 6 VAL A 193 PHE A 197 1 N CYS A 194 O ARG A 217
SHEET 4 D 6 TYR A 263 GLU A 266 1 O PHE A 265 N PHE A 197
SHEET 5 D 6 VAL A 287 VAL A 290 1 O VAL A 289 N SER A 264
SHEET 6 D 6 THR A 312 GLY A 315 1 O LYS A 314 N VAL A 290
SHEET 1 E 2 ILE A 300 THR A 302 0
SHEET 2 E 2 ILE B 300 THR B 302 -1 O ILE B 300 N THR A 302
SHEET 1 F 5 VAL B 62 ILE B 63 0
SHEET 2 F 5 ILE B 5 ALA B 12 -1 N ALA B 12 O VAL B 62
SHEET 3 F 5 SER B 20 VAL B 26 -1 O VAL B 26 N ILE B 5
SHEET 4 F 5 PHE B 129 CYS B 131 -1 O THR B 130 N GLU B 25
SHEET 5 F 5 LYS B 134 ILE B 136 -1 O LYS B 134 N CYS B 131
SHEET 1 G 5 TYR B 148 ALA B 152 0
SHEET 2 G 5 GLU B 33 ALA B 42 -1 N VAL B 34 O VAL B 151
SHEET 3 G 5 GLU B 67 VAL B 75 -1 O ILE B 71 N LYS B 37
SHEET 4 G 5 THR B 87 PRO B 90 -1 O VAL B 88 N GLY B 70
SHEET 5 G 5 VAL B 156 LYS B 158 -1 O ALA B 157 N ILE B 89
SHEET 1 H 4 TYR B 148 ALA B 152 0
SHEET 2 H 4 GLU B 33 ALA B 42 -1 N VAL B 34 O VAL B 151
SHEET 3 H 4 ARG B 368 LYS B 372 -1 O VAL B 371 N THR B 41
SHEET 4 H 4 VAL B 345 SER B 350 1 N LEU B 349 O LYS B 372
SHEET 1 I 6 GLU B 238 ILE B 240 0
SHEET 2 I 6 ARG B 217 VAL B 221 1 N GLY B 220 O ILE B 240
SHEET 3 I 6 VAL B 193 PHE B 197 1 N CYS B 194 O ILE B 219
SHEET 4 I 6 TYR B 263 GLU B 266 1 O PHE B 265 N PHE B 197
SHEET 5 I 6 VAL B 287 VAL B 290 1 O VAL B 289 N SER B 264
SHEET 6 I 6 THR B 312 GLY B 315 1 O LYS B 314 N VAL B 290
LINK SG CYS A 44 ZN ZN A 376 1555 1555 2.37
LINK NE2 HIS A 66 ZN ZN A 376 1555 1555 2.10
LINK SG CYS A 96 ZN ZN A 375 1555 1555 2.32
LINK SG CYS A 99 ZN ZN A 375 1555 1555 2.39
LINK SG CYS A 102 ZN ZN A 375 1555 1555 2.30
LINK SG CYS A 110 ZN ZN A 375 1555 1555 2.31
LINK SG CYS A 173 ZN ZN A 376 1555 1555 2.32
LINK O ALA A 186 K K A 602 1555 1555 3.01
LINK O LYS A 187 K K A 602 1555 1555 2.98
LINK OE2 GLU A 189 K K A 602 1555 1555 3.02
LINK OH TYR A 263 K K A 602 1555 1555 2.90
LINK N5 022 A 374 ZN ZN A 376 1555 1555 2.05
LINK O HOH A 456 K K B 501 1555 1555 3.08
LINK O HOH A 581 K K A 602 1555 1555 2.75
LINK K K A 602 O HOH A 691 1555 1555 2.76
LINK O HOH A 626 K K B 501 1555 1555 2.86
LINK SG CYS B 44 ZN ZN B 376 1555 1555 2.39
LINK NE2 HIS B 66 ZN ZN B 376 1555 1555 2.12
LINK SG CYS B 96 ZN ZN B 375 1555 1555 2.40
LINK SG CYS B 99 ZN ZN B 375 1555 1555 2.31
LINK SG CYS B 102 ZN ZN B 375 1555 1555 2.33
LINK SG CYS B 110 ZN ZN B 375 1555 1555 2.39
LINK SG CYS B 173 ZN ZN B 376 1555 1555 2.27
LINK O ALA B 186 K K B 501 1555 1555 2.98
LINK O LYS B 187 K K B 501 1555 1555 2.89
LINK OE2 GLU B 189 K K B 501 1555 1555 3.09
LINK OH TYR B 263 K K B 501 1555 1555 2.89
LINK ZN ZN B 376 N5 022 B 377 1555 1555 2.10
CISPEP 1 PHE A 60 PRO A 61 0 -6.09
CISPEP 2 PHE B 60 PRO B 61 0 -5.75
SITE 1 AC1 4 CYS A 96 CYS A 99 CYS A 102 CYS A 110
SITE 1 AC2 4 CYS A 44 HIS A 66 CYS A 173 022 A 374
SITE 1 AC3 4 CYS B 96 CYS B 99 CYS B 102 CYS B 110
SITE 1 AC4 4 CYS B 44 HIS B 66 CYS B 173 022 B 377
SITE 1 AC5 6 HOH A 456 HOH A 626 ALA B 186 LYS B 187
SITE 2 AC5 6 GLU B 189 TYR B 263
SITE 1 AC6 6 ALA A 186 LYS A 187 GLU A 189 TYR A 263
SITE 2 AC6 6 HOH A 581 HOH A 691
SITE 1 AC7 33 HIS A 45 CYS A 173 THR A 177 GLY A 198
SITE 2 AC7 33 GLY A 200 GLY A 201 VAL A 202 ASP A 222
SITE 3 AC7 33 ILE A 223 CYS A 267 ILE A 268 VAL A 273
SITE 4 AC7 33 VAL A 291 VAL A 293 THR A 316 ALA A 317
SITE 5 AC7 33 PHE A 318 ARG A 368 022 A 374 N2P A 379
SITE 6 AC7 33 HOH A 384 HOH A 391 HOH A 394 HOH A 420
SITE 7 AC7 33 HOH A 467 HOH A 468 HOH A 481 HOH A 525
SITE 8 AC7 33 HOH A 577 HOH A 609 HOH A 635 HOH A 637
SITE 9 AC7 33 HOH A 679
SITE 1 AC8 33 HIS B 45 CYS B 173 THR B 177 GLY B 198
SITE 2 AC8 33 GLY B 200 GLY B 201 VAL B 202 ASP B 222
SITE 3 AC8 33 ILE B 223 CYS B 267 ILE B 268 VAL B 273
SITE 4 AC8 33 VAL B 291 GLY B 292 VAL B 293 THR B 316
SITE 5 AC8 33 ALA B 317 PHE B 318 ARG B 368 022 B 377
SITE 6 AC8 33 N2P B 379 HOH B 431 HOH B 437 HOH B 465
SITE 7 AC8 33 HOH B 483 HOH B 495 HOH B 498 HOH B 518
SITE 8 AC8 33 HOH B 536 HOH B 553 HOH B 559 HOH B 631
SITE 9 AC8 33 HOH B 753
SITE 1 AC9 18 CYS A 44 THR A 46 HIS A 66 TYR A 92
SITE 2 AC9 18 ILE A 93 GLN A 111 ARG A 114 GLN A 117
SITE 3 AC9 18 MET A 140 CYS A 173 ZN A 376 HOH A 427
SITE 4 AC9 18 NAD A 500 HOH A 565 HOH A 601 LYS B 283
SITE 5 AC9 18 VAL B 308 THR B 309
SITE 1 BC1 17 LYS A 283 THR A 309 CYS B 44 THR B 46
SITE 2 BC1 17 HIS B 66 TYR B 92 ILE B 93 GLN B 111
SITE 3 BC1 17 ARG B 114 GLN B 117 MET B 140 CYS B 173
SITE 4 BC1 17 NAD B 374 ZN B 376 HOH B 411 HOH B 503
SITE 5 BC1 17 HOH B 647
SITE 1 BC2 5 LYS B 81 GLN B 95 CYS B 96 VAL B 324
SITE 2 BC2 5 GLU B 325
SITE 1 BC3 9 LYS A 6 CYS A 7 GLU A 147 TYR A 148
SITE 2 BC3 9 HOH A 469 TYR B 334 MET B 335 LYS B 337
SITE 3 BC3 9 ASP B 342
SITE 1 BC4 5 LYS A 81 GLN A 95 CYS A 96 GLY A 97
SITE 2 BC4 5 HOH A 413
SITE 1 BC5 7 HIS B 45 THR B 46 TYR B 49 VAL B 293
SITE 2 BC5 7 ALA B 295 NAD B 374 HOH B 715
SITE 1 BC6 4 THR A 135 GLN B 243 ASP B 244 SER B 246
SITE 1 BC7 5 HIS A 45 TYR A 49 VAL A 293 ALA A 295
SITE 2 BC7 5 NAD A 500
SITE 1 BC8 4 LYS A 314 HOH A 626 HOH A 691 LYS B 314
CRYST1 78.858 78.858 310.078 90.00 90.00 90.00 P 43 21 2 16
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 0.012681 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012681 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003225 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
