HEADER OXIDOREDUCTASE 17-JUL-02 1M6W
TITLE BINARY COMPLEX OF HUMAN GLUTATHIONE-DEPENDENT FORMALDEHYDE
TITLE 2 DEHYDROGENASE AND 12-HYDROXYDODECANOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALCOHOL DEHYDROGENASE CLASS III CHI CHAIN; ALCOHOL
COMPND 5 DEHYDROGENASE (CLASS III), CHI POLYPEPTIDE; FDH; E.C.1.2.1.1;
COMPND 6 EC: 1.1.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: APOENZYME
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADH5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TG-1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKK223-3
KEYWDS GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE, CLASS III ALCOHOL
KEYWDS 2 DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.SANGHANI,H.ROBINSON,W.F.BOSRON,T.D.HURLEY
REVDAT 6 14-FEB-24 1M6W 1 REMARK LINK
REVDAT 5 24-FEB-09 1M6W 1 VERSN
REVDAT 4 01-APR-03 1M6W 1 JRNL
REVDAT 3 27-SEP-02 1M6W 1 JRNL
REVDAT 2 05-AUG-02 1M6W 1 HETNAM FORMUL CONECT HETATM
REVDAT 2 2 1 REMARK
REVDAT 1 26-JUL-02 1M6W 0
JRNL AUTH P.C.SANGHANI,H.ROBINSON,W.F.BOSRON,T.D.HURLEY
JRNL TITL HUMAN GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE.
JRNL TITL 2 STRUCTURES OF APO, BINARY, AND INHIBITORY TERNARY COMPLEXES.
JRNL REF BIOCHEMISTRY V. 41 10778 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12196016
JRNL DOI 10.1021/BI0257639
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 43801
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 SET) : 0.191
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2278
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6391
REMARK 3 BIN R VALUE (WORKING SET) : 0.2031
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 235
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5544
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 667
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.40
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.280 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.050 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 35.54
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M6W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016670.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2667, 1.2827, 1.2837
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43971
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 23.60
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 37.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.28800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASSIUM PHOSPHATE, ZINC
REMARK 280 SULPHATE, DITHIOTHREITOL, PH 7.1, VAPOR DIFFUSION, SITTING DROP
REMARK 280 AT 277K
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 154.70850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.31600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.31600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 232.06275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.31600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.31600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.35425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.31600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.31600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 232.06275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.31600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.31600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.35425
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 154.70850
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: 5980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 114 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
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 LEU A 64 -168.73 -72.38
REMARK 500 GLN A 95 86.35 -157.15
REMARK 500 CYS A 131 116.76 -163.50
REMARK 500 LYS A 167 -63.11 -122.16
REMARK 500 CYS A 173 -89.00 -158.18
REMARK 500 LEU A 199 44.54 -103.81
REMARK 500 VAL A 293 -24.58 -142.98
REMARK 500 ALA A 294 -162.79 -127.97
REMARK 500 ALA A 295 48.64 -153.08
REMARK 500 SER A 296 -38.84 -19.41
REMARK 500 VAL A 341 -49.73 -139.39
REMARK 500 LYS A 365 74.42 -115.65
REMARK 500 SER A 366 152.57 152.54
REMARK 500 GLN B 95 85.18 -154.15
REMARK 500 LYS B 167 -60.96 -122.73
REMARK 500 CYS B 173 -74.47 -161.57
REMARK 500 VAL B 341 -51.78 -137.50
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 A1376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 44 SG
REMARK 620 2 HIS A 66 NE2 104.1
REMARK 620 3 CYS A 173 SG 128.8 112.2
REMARK 620 4 12H A4378 O13 109.7 71.4 115.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 99 SG 103.0
REMARK 620 3 CYS A 102 SG 115.8 110.7
REMARK 620 4 CYS A 110 SG 108.4 117.4 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A2001 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 186 O
REMARK 620 2 LYS A 187 O 67.4
REMARK 620 3 GLU A 189 OE2 142.9 86.0
REMARK 620 4 TYR A 263 OH 88.9 95.6 67.7
REMARK 620 5 HOH A4422 O 82.5 113.1 133.3 143.6
REMARK 620 6 HOH A4479 O 89.9 156.6 111.2 77.7 67.1
REMARK 620 7 HOH B5708 O 146.8 144.7 66.5 93.8 75.9 58.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 44 SG
REMARK 620 2 HIS B 66 NE2 103.6
REMARK 620 3 CYS B 173 SG 120.8 114.8
REMARK 620 4 12H B5378 O13 88.6 119.6 107.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 96 SG
REMARK 620 2 CYS B 99 SG 107.9
REMARK 620 3 CYS B 102 SG 111.7 105.3
REMARK 620 4 CYS B 110 SG 108.5 119.2 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B2002 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 186 O
REMARK 620 2 LYS B 187 O 66.6
REMARK 620 3 GLU B 189 OE2 143.8 86.4
REMARK 620 4 TYR B 263 OH 88.8 94.1 68.6
REMARK 620 5 HOH B5520 O 85.0 151.5 117.6 82.0
REMARK 620 6 HOH B5580 O 146.3 141.3 69.0 103.4 66.3
REMARK 620 7 HOH B5660 O 78.0 109.3 136.0 145.2 65.1 74.3
REMARK 620 N 1 2 3 4 5 6
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 1375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12H A 4378
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12H B 5378
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M6H RELATED DB: PDB
REMARK 900 RELATED ID: 1MA0 RELATED DB: PDB
DBREF 1M6W A 1 373 UNP P11766 ADHX_HUMAN 1 373
DBREF 1M6W B 1 373 UNP P11766 ADHX_HUMAN 1 373
SEQRES 1 A 373 ALA ASN GLU VAL ILE LYS CYS LYS ALA ALA VAL ALA TRP
SEQRES 2 A 373 GLU ALA GLY LYS PRO LEU SER ILE GLU GLU ILE GLU VAL
SEQRES 3 A 373 ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS ILE ILE
SEQRES 4 A 373 ALA THR ALA VAL CYS HIS THR ASP ALA TYR THR LEU SER
SEQRES 5 A 373 GLY ALA ASP PRO GLU GLY CYS PHE PRO VAL ILE LEU GLY
SEQRES 6 A 373 HIS GLU GLY ALA GLY ILE VAL GLU SER VAL GLY GLU GLY
SEQRES 7 A 373 VAL THR LYS LEU LYS ALA GLY ASP THR VAL ILE PRO LEU
SEQRES 8 A 373 TYR ILE PRO GLN CYS GLY GLU CYS LYS PHE CYS LEU ASN
SEQRES 9 A 373 PRO LYS THR ASN LEU CYS GLN LYS ILE ARG VAL THR GLN
SEQRES 10 A 373 GLY LYS GLY LEU MET PRO ASP GLY THR SER ARG PHE THR
SEQRES 11 A 373 CYS LYS GLY LYS THR ILE LEU HIS TYR MET GLY THR SER
SEQRES 12 A 373 THR PHE SER GLU TYR THR VAL VAL ALA ASP ILE SER VAL
SEQRES 13 A 373 ALA LYS ILE ASP PRO LEU ALA PRO LEU ASP LYS VAL CYS
SEQRES 14 A 373 LEU LEU GLY CYS GLY ILE SER THR GLY TYR GLY ALA ALA
SEQRES 15 A 373 VAL ASN THR ALA LYS LEU GLU PRO GLY SER VAL CYS ALA
SEQRES 16 A 373 VAL PHE GLY LEU GLY GLY VAL GLY LEU ALA VAL ILE MET
SEQRES 17 A 373 GLY CYS LYS VAL ALA GLY ALA SER ARG ILE ILE GLY VAL
SEQRES 18 A 373 ASP ILE ASN LYS ASP LYS PHE ALA ARG ALA LYS GLU PHE
SEQRES 19 A 373 GLY ALA THR GLU CYS ILE ASN PRO GLN ASP PHE SER LYS
SEQRES 20 A 373 PRO ILE GLN GLU VAL LEU ILE GLU MET THR ASP GLY GLY
SEQRES 21 A 373 VAL ASP TYR SER PHE GLU CYS ILE GLY ASN VAL LYS VAL
SEQRES 22 A 373 MET ARG ALA ALA LEU GLU ALA CYS HIS LYS GLY TRP GLY
SEQRES 23 A 373 VAL SER VAL VAL VAL GLY VAL ALA ALA SER GLY GLU GLU
SEQRES 24 A 373 ILE ALA THR ARG PRO PHE GLN LEU VAL THR GLY ARG THR
SEQRES 25 A 373 TRP LYS GLY THR ALA PHE GLY GLY TRP LYS SER VAL GLU
SEQRES 26 A 373 SER VAL PRO LYS LEU VAL SER GLU TYR MET SER LYS LYS
SEQRES 27 A 373 ILE LYS VAL ASP GLU PHE VAL THR HIS ASN LEU SER PHE
SEQRES 28 A 373 ASP GLU ILE ASN LYS ALA PHE GLU LEU MET HIS SER GLY
SEQRES 29 A 373 LYS SER ILE ARG THR VAL VAL LYS ILE
SEQRES 1 B 373 ALA ASN GLU VAL ILE LYS CYS LYS ALA ALA VAL ALA TRP
SEQRES 2 B 373 GLU ALA GLY LYS PRO LEU SER ILE GLU GLU ILE GLU VAL
SEQRES 3 B 373 ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS ILE ILE
SEQRES 4 B 373 ALA THR ALA VAL CYS HIS THR ASP ALA TYR THR LEU SER
SEQRES 5 B 373 GLY ALA ASP PRO GLU GLY CYS PHE PRO VAL ILE LEU GLY
SEQRES 6 B 373 HIS GLU GLY ALA GLY ILE VAL GLU SER VAL GLY GLU GLY
SEQRES 7 B 373 VAL THR LYS LEU LYS ALA GLY ASP THR VAL ILE PRO LEU
SEQRES 8 B 373 TYR ILE PRO GLN CYS GLY GLU CYS LYS PHE CYS LEU ASN
SEQRES 9 B 373 PRO LYS THR ASN LEU CYS GLN LYS ILE ARG VAL THR GLN
SEQRES 10 B 373 GLY LYS GLY LEU MET PRO ASP GLY THR SER ARG PHE THR
SEQRES 11 B 373 CYS LYS GLY LYS THR ILE LEU HIS TYR MET GLY THR SER
SEQRES 12 B 373 THR PHE SER GLU TYR THR VAL VAL ALA ASP ILE SER VAL
SEQRES 13 B 373 ALA LYS ILE ASP PRO LEU ALA PRO LEU ASP LYS VAL CYS
SEQRES 14 B 373 LEU LEU GLY CYS GLY ILE SER THR GLY TYR GLY ALA ALA
SEQRES 15 B 373 VAL ASN THR ALA LYS LEU GLU PRO GLY SER VAL CYS ALA
SEQRES 16 B 373 VAL PHE GLY LEU GLY GLY VAL GLY LEU ALA VAL ILE MET
SEQRES 17 B 373 GLY CYS LYS VAL ALA GLY ALA SER ARG ILE ILE GLY VAL
SEQRES 18 B 373 ASP ILE ASN LYS ASP LYS PHE ALA ARG ALA LYS GLU PHE
SEQRES 19 B 373 GLY ALA THR GLU CYS ILE ASN PRO GLN ASP PHE SER LYS
SEQRES 20 B 373 PRO ILE GLN GLU VAL LEU ILE GLU MET THR ASP GLY GLY
SEQRES 21 B 373 VAL ASP TYR SER PHE GLU CYS ILE GLY ASN VAL LYS VAL
SEQRES 22 B 373 MET ARG ALA ALA LEU GLU ALA CYS HIS LYS GLY TRP GLY
SEQRES 23 B 373 VAL SER VAL VAL VAL GLY VAL ALA ALA SER GLY GLU GLU
SEQRES 24 B 373 ILE ALA THR ARG PRO PHE GLN LEU VAL THR GLY ARG THR
SEQRES 25 B 373 TRP LYS GLY THR ALA PHE GLY GLY TRP LYS SER VAL GLU
SEQRES 26 B 373 SER VAL PRO LYS LEU VAL SER GLU TYR MET SER LYS LYS
SEQRES 27 B 373 ILE LYS VAL ASP GLU PHE VAL THR HIS ASN LEU SER PHE
SEQRES 28 B 373 ASP GLU ILE ASN LYS ALA PHE GLU LEU MET HIS SER GLY
SEQRES 29 B 373 LYS SER ILE ARG THR VAL VAL LYS ILE
HET ZN A1375 1
HET ZN A1376 1
HET K A2001 1
HET PO4 A3001 5
HET PO4 A3002 5
HET PO4 A3003 5
HET 12H A4378 15
HET ZN B1375 1
HET ZN B1376 1
HET K B2002 1
HET 12H B5378 15
HETNAM ZN ZINC ION
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM 12H 12-HYDROXYDODECANOIC ACID
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 K 2(K 1+)
FORMUL 6 PO4 3(O4 P 3-)
FORMUL 9 12H 2(C12 H24 O3)
FORMUL 14 HOH *667(H2 O)
HELIX 1 1 CYS A 44 GLY A 53 1 10
HELIX 2 2 CYS A 99 ASN A 104 1 6
HELIX 3 3 ILE A 113 LYS A 119 1 7
HELIX 4 4 PRO A 164 CYS A 169 1 6
HELIX 5 5 LEU A 170 GLY A 172 5 3
HELIX 6 6 CYS A 173 ASN A 184 1 12
HELIX 7 7 GLY A 200 ALA A 213 1 14
HELIX 8 8 ASN A 224 ASP A 226 5 3
HELIX 9 9 LYS A 227 GLY A 235 1 9
HELIX 10 10 ASN A 241 PHE A 245 5 5
HELIX 11 11 PRO A 248 THR A 257 1 10
HELIX 12 12 ASN A 270 ALA A 280 1 11
HELIX 13 13 ARG A 303 THR A 309 1 7
HELIX 14 14 ALA A 317 TRP A 321 5 5
HELIX 15 15 LYS A 322 SER A 336 1 15
HELIX 16 16 VAL A 341 GLU A 343 5 3
HELIX 17 17 GLU A 353 SER A 363 1 11
HELIX 18 18 CYS B 44 GLY B 53 1 10
HELIX 19 19 CYS B 99 ASN B 104 1 6
HELIX 20 20 ILE B 113 LYS B 119 1 7
HELIX 21 21 PRO B 164 CYS B 169 1 6
HELIX 22 22 LEU B 170 GLY B 172 5 3
HELIX 23 23 CYS B 173 ASN B 184 1 12
HELIX 24 24 GLY B 200 ALA B 213 1 14
HELIX 25 25 ASN B 224 ASP B 226 5 3
HELIX 26 26 LYS B 227 GLY B 235 1 9
HELIX 27 27 ASN B 241 PHE B 245 5 5
HELIX 28 28 PRO B 248 THR B 257 1 10
HELIX 29 29 ASN B 270 ALA B 280 1 11
HELIX 30 30 PRO B 304 THR B 309 1 6
HELIX 31 31 ALA B 317 TRP B 321 5 5
HELIX 32 32 LYS B 322 SER B 336 1 15
HELIX 33 33 VAL B 341 GLU B 343 5 3
HELIX 34 34 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 ILE A 24 N CYS A 7
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 LYS A 134 N CYS A 131
SHEET 1 B 5 VAL A 156 LYS A 158 0
SHEET 2 B 5 THR A 87 PRO A 90 -1 N ILE A 89 O ALA A 157
SHEET 3 B 5 GLU A 67 VAL A 75 -1 N GLY A 70 O VAL A 88
SHEET 4 B 5 GLU A 33 ALA A 42 -1 N LYS A 37 O ILE A 71
SHEET 5 B 5 TYR A 148 ALA A 152 -1 O VAL A 151 N VAL A 34
SHEET 1 C 6 VAL A 156 LYS A 158 0
SHEET 2 C 6 THR A 87 PRO A 90 -1 N ILE A 89 O ALA A 157
SHEET 3 C 6 GLU A 67 VAL A 75 -1 N GLY A 70 O VAL A 88
SHEET 4 C 6 GLU A 33 ALA A 42 -1 N LYS A 37 O ILE A 71
SHEET 5 C 6 ARG A 368 LYS A 372 -1 O VAL A 371 N THR A 41
SHEET 6 C 6 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 GLU A 238
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 291 1 O VAL A 289 N SER A 264
SHEET 6 D 6 THR A 312 THR A 316 1 O LYS A 314 N SER A 288
SHEET 1 E 2 ILE A 300 THR A 302 0
SHEET 2 E 2 ILE B 300 THR B 302 -1 O THR B 302 N ILE A 300
SHEET 1 F 4 ILE B 5 VAL B 11 0
SHEET 2 F 4 SER B 20 VAL B 26 -1 O ILE B 24 N CYS B 7
SHEET 3 F 4 PHE B 129 CYS B 131 -1 O THR B 130 N GLU B 25
SHEET 4 F 4 LYS B 134 ILE B 136 -1 O LYS B 134 N CYS B 131
SHEET 1 G 5 VAL B 156 LYS B 158 0
SHEET 2 G 5 THR B 87 PRO B 90 -1 N ILE B 89 O ALA B 157
SHEET 3 G 5 GLU B 67 VAL B 75 -1 N GLY B 70 O VAL B 88
SHEET 4 G 5 GLU B 33 ALA B 42 -1 N LYS B 37 O ILE B 71
SHEET 5 G 5 TYR B 148 ALA B 152 -1 O THR B 149 N ILE B 36
SHEET 1 H 6 VAL B 156 LYS B 158 0
SHEET 2 H 6 THR B 87 PRO B 90 -1 N ILE B 89 O ALA B 157
SHEET 3 H 6 GLU B 67 VAL B 75 -1 N GLY B 70 O VAL B 88
SHEET 4 H 6 GLU B 33 ALA B 42 -1 N LYS B 37 O ILE B 71
SHEET 5 H 6 ARG B 368 LYS B 372 -1 O VAL B 371 N THR B 41
SHEET 6 H 6 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 SER B 288
LINK SG CYS A 44 ZN ZN A1376 1555 1555 2.39
LINK NE2 HIS A 66 ZN ZN A1376 1555 1555 2.14
LINK SG CYS A 96 ZN ZN A1375 1555 1555 2.36
LINK SG CYS A 99 ZN ZN A1375 1555 1555 2.48
LINK SG CYS A 102 ZN ZN A1375 1555 1555 2.27
LINK SG CYS A 110 ZN ZN A1375 1555 1555 2.24
LINK SG CYS A 173 ZN ZN A1376 1555 1555 2.24
LINK O ALA A 186 K K A2001 1555 1555 2.91
LINK O LYS A 187 K K A2001 1555 1555 2.85
LINK OE2 GLU A 189 K K A2001 1555 1555 2.88
LINK OH TYR A 263 K K A2001 1555 1555 2.79
LINK ZN ZN A1376 O13 12H A4378 1555 1555 2.04
LINK K K A2001 O HOH A4422 1555 1555 3.07
LINK K K A2001 O HOH A4479 1555 1555 2.93
LINK K K A2001 O HOH B5708 1555 1555 3.11
LINK SG CYS B 44 ZN ZN B1376 1555 1555 2.37
LINK NE2 HIS B 66 ZN ZN B1376 1555 1555 2.06
LINK SG CYS B 96 ZN ZN B1375 1555 1555 2.36
LINK SG CYS B 99 ZN ZN B1375 1555 1555 2.35
LINK SG CYS B 102 ZN ZN B1375 1555 1555 2.30
LINK SG CYS B 110 ZN ZN B1375 1555 1555 2.30
LINK SG CYS B 173 ZN ZN B1376 1555 1555 2.31
LINK O ALA B 186 K K B2002 1555 1555 2.87
LINK O LYS B 187 K K B2002 1555 1555 2.79
LINK OE2 GLU B 189 K K B2002 1555 1555 2.93
LINK OH TYR B 263 K K B2002 1555 1555 2.71
LINK ZN ZN B1376 O13 12H B5378 1555 1555 1.96
LINK K K B2002 O HOH B5520 1555 1555 3.05
LINK K K B2002 O HOH B5580 1555 1555 2.88
LINK K K B2002 O HOH B5660 1555 1555 3.01
CISPEP 1 PHE A 60 PRO A 61 0 -0.33
CISPEP 2 PHE B 60 PRO B 61 0 0.00
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 12H A4378
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 12H B5378
SITE 1 AC5 6 ALA A 186 LYS A 187 GLU A 189 TYR A 263
SITE 2 AC5 6 HOH A4422 HOH A4479
SITE 1 AC6 7 ALA B 186 LYS B 187 GLU B 189 TYR B 263
SITE 2 AC6 7 HOH B5520 HOH B5580 HOH B5660
SITE 1 AC7 4 LYS A 314 HOH A4422 HOH A4560 LYS B 314
SITE 1 AC8 7 LYS A 83 LYS A 158 HOH A4470 HOH A4577
SITE 2 AC8 7 HOH A4592 HOH A4632 LYS B 83
SITE 1 AC9 8 HIS A 45 GLY A 201 VAL A 202 ARG A 368
SITE 2 AC9 8 HOH A4411 HOH A4570 HOH A4603 HOH A4628
SITE 1 BC1 14 CYS A 44 THR A 46 HIS A 66 TYR A 92
SITE 2 BC1 14 LEU A 109 GLN A 111 ARG A 114 MET A 140
SITE 3 BC1 14 CYS A 173 GLY A 292 ALA A 317 ZN A1376
SITE 4 BC1 14 HOH A4395 LYS B 283
SITE 1 BC2 12 LYS A 283 CYS B 44 THR B 46 HIS B 66
SITE 2 BC2 12 TYR B 92 GLN B 111 ARG B 114 CYS B 173
SITE 3 BC2 12 VAL B 293 ALA B 317 ZN B1376 HOH B5451
CRYST1 78.632 78.632 309.417 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 0.012717 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012717 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003232 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
