HEADER OXIDOREDUCTASE 01-JUL-09 3I4C
TITLE CRYSTAL STRUCTURE OF SULFOLOBUS SOLFATARICUS ADH(SSADH) DOUBLE MUTANT
TITLE 2 (W95L,N249Y)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAD-DEPENDENT ALCOHOL DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D, E, H;
COMPND 4 EC: 1.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 GENE: ADH, SSO2536;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: RB791;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS ARCHAEON, ZINC, NAD(H)-DEPENDENT, MUTANT, OXIDOREDUCTASE, METAL-
KEYWDS 2 BINDING, METHYLATION, NAD
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ESPOSITO,A.PENNACCHIO,A.ZAGARI,M.ROSSI,C.A.RAIA
REVDAT 4 01-NOV-23 3I4C 1 REMARK
REVDAT 3 10-NOV-21 3I4C 1 REMARK SEQADV
REVDAT 2 15-SEP-09 3I4C 1 JRNL
REVDAT 1 21-JUL-09 3I4C 0
JRNL AUTH A.PENNACCHIO,L.ESPOSITO,A.ZAGARI,M.ROSSI,C.A.RAIA
JRNL TITL ROLE OF TRYPTOPHAN 95 IN SUBSTRATE SPECIFICITY AND
JRNL TITL 2 STRUCTURAL STABILITY OF SULFOLOBUS SOLFATARICUS ALCOHOL
JRNL TITL 3 DEHYDROGENASE
JRNL REF EXTREMOPHILES V. 13 751 2009
JRNL REFN ISSN 1431-0651
JRNL PMID 19588068
JRNL DOI 10.1007/S00792-009-0256-0
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 366826.860
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 140498
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) : 0.228
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7092
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 19263
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1040
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14704
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 429
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.09000
REMARK 3 B22 (A**2) : 5.19000
REMARK 3 B33 (A**2) : -3.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.58000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 1.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.160 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.310 ; 3.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 44.94
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3I4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000053947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 149954
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.5000
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 (%) : 90.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.43300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1NTO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7%(W/V) PEG 4000, 7%(V/V) ISOPROPANOL,
REMARK 280 50MM SODIUM CITRATE PH 5.6, 50MM TRIS PH 7.8, 25MM COCL2 , VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 107.86450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.77250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.86450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.77250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 196.80418
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 116.84535
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 ILE A 9
REMARK 465 GLY A 10
REMARK 465 LYS A 11
REMARK 465 GLY A 50
REMARK 465 ASN A 51
REMARK 465 LEU A 52
REMARK 465 ARG A 53
REMARK 465 VAL B 7
REMARK 465 GLU B 8
REMARK 465 ILE B 9
REMARK 465 GLY B 10
REMARK 465 LYS B 11
REMARK 465 PRO B 12
REMARK 465 LEU B 13
REMARK 465 SER B 14
REMARK 465 LEU B 15
REMARK 465 GLN B 46
REMARK 465 GLY B 47
REMARK 465 ARG B 48
REMARK 465 PHE B 49
REMARK 465 GLY B 50
REMARK 465 ASN B 51
REMARK 465 LEU B 52
REMARK 465 ARG B 53
REMARK 465 ILE B 54
REMARK 465 VAL B 55
REMARK 465 GLU B 56
REMARK 465 ASP B 57
REMARK 465 LEU B 58
REMARK 465 GLY B 59
REMARK 465 VAL B 60
REMARK 465 LYS B 61
REMARK 465 ASN B 333
REMARK 465 LEU B 334
REMARK 465 GLU B 335
REMARK 465 ASN B 336
REMARK 465 PHE B 337
REMARK 465 LYS B 338
REMARK 465 ALA B 339
REMARK 465 ILE B 340
REMARK 465 GLY B 341
REMARK 465 ARG B 342
REMARK 465 VAL C 42
REMARK 465 HIS C 43
REMARK 465 MET C 44
REMARK 465 ARG C 45
REMARK 465 GLN C 46
REMARK 465 GLY C 47
REMARK 465 ARG C 48
REMARK 465 PHE C 49
REMARK 465 GLY C 50
REMARK 465 ASN C 51
REMARK 465 LEU C 52
REMARK 465 ARG C 53
REMARK 465 ILE C 54
REMARK 465 VAL C 55
REMARK 465 GLU C 56
REMARK 465 ASP C 57
REMARK 465 LEU C 58
REMARK 465 GLY C 59
REMARK 465 VAL C 60
REMARK 465 LYS C 61
REMARK 465 LEU C 62
REMARK 465 PRO C 63
REMARK 465 VAL C 64
REMARK 465 LEU C 334
REMARK 465 GLU C 335
REMARK 465 ASN C 336
REMARK 465 PHE C 337
REMARK 465 LYS C 338
REMARK 465 ALA C 339
REMARK 465 ILE C 340
REMARK 465 GLY C 341
REMARK 465 VAL D 7
REMARK 465 GLU D 8
REMARK 465 ILE D 9
REMARK 465 GLY D 10
REMARK 465 LYS D 11
REMARK 465 PRO D 12
REMARK 465 GLN D 46
REMARK 465 GLY D 47
REMARK 465 ARG D 48
REMARK 465 PHE D 49
REMARK 465 GLY D 50
REMARK 465 ASN D 51
REMARK 465 LEU D 52
REMARK 465 ARG D 53
REMARK 465 ASP D 79
REMARK 465 PHE D 337
REMARK 465 LYS D 338
REMARK 465 ALA D 339
REMARK 465 ILE D 340
REMARK 465 GLY D 341
REMARK 465 VAL E 7
REMARK 465 GLU E 8
REMARK 465 ILE E 9
REMARK 465 GLY E 10
REMARK 465 LYS E 11
REMARK 465 PRO E 12
REMARK 465 GLY E 47
REMARK 465 ARG E 48
REMARK 465 PHE E 49
REMARK 465 GLY E 50
REMARK 465 ASN E 51
REMARK 465 LEU E 52
REMARK 465 ARG E 53
REMARK 465 ILE E 54
REMARK 465 VAL E 55
REMARK 465 GLU E 56
REMARK 465 ASP E 57
REMARK 465 LEU E 58
REMARK 465 GLY E 59
REMARK 465 VAL E 60
REMARK 465 LYS E 61
REMARK 465 LEU E 334
REMARK 465 GLU E 335
REMARK 465 ASN E 336
REMARK 465 PHE E 337
REMARK 465 LYS E 338
REMARK 465 ALA E 339
REMARK 465 ILE E 340
REMARK 465 LEU H 52
REMARK 465 ARG H 53
REMARK 465 ILE H 54
REMARK 465 VAL H 55
REMARK 465 GLU H 56
REMARK 465 ASP H 57
REMARK 465 LEU H 58
REMARK 465 GLY H 59
REMARK 465 ASN H 336
REMARK 465 PHE H 337
REMARK 465 LYS H 338
REMARK 465 ALA H 339
REMARK 465 ILE H 340
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 338 CB CG CD CE NZ
REMARK 470 ILE A 340 CB CG1 CG2 CD1
REMARK 470 LYS B 22 CD CE NZ
REMARK 470 LYS B 24 CD CE NZ
REMARK 470 LYS B 86 CD CE NZ
REMARK 470 LYS C 11 CB CG CD CE NZ
REMARK 470 ARG C 307 CB CG CD NE CZ NH1 NH2
REMARK 470 HIS E 43 CG ND1 CD2 CE1 NE2
REMARK 470 LYS H 22 CE NZ
REMARK 470 ARG H 48 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 61 CD CE NZ
REMARK 470 ARG H 142 CD NE CZ NH1 NH2
REMARK 470 GLU H 206 CB CG CD OE1 OE2
REMARK 470 LYS H 315 CG CD CE NZ
REMARK 470 LYS H 320 CD CE NZ
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 108 54.71 -116.90
REMARK 500 ILE A 120 -61.25 -120.09
REMARK 500 CYS A 154 -74.68 -124.75
REMARK 500 SER A 238 -4.72 75.95
REMARK 500 VAL A 256 -61.03 -100.48
REMARK 500 LEU A 295 -43.90 -147.07
REMARK 500 VAL A 296 -139.21 -128.11
REMARK 500 PHE A 337 45.09 36.39
REMARK 500 ALA B 3 116.90 -172.00
REMARK 500 GLU B 108 56.87 -119.32
REMARK 500 ILE B 120 -58.72 -122.91
REMARK 500 CYS B 154 -73.77 -126.25
REMARK 500 VAL B 256 -61.79 -103.61
REMARK 500 LEU B 295 -44.30 -145.86
REMARK 500 VAL B 296 -138.46 -125.66
REMARK 500 ASN B 298 -168.61 -107.02
REMARK 500 ALA C 3 111.15 -167.41
REMARK 500 GLU C 108 55.52 -117.79
REMARK 500 ILE C 120 -55.78 -124.07
REMARK 500 CYS C 154 -74.43 -126.13
REMARK 500 VAL C 256 -61.12 -102.14
REMARK 500 LEU C 295 -48.87 -145.71
REMARK 500 VAL C 296 -134.22 -125.82
REMARK 500 ASN C 298 -169.04 -103.76
REMARK 500 ASP D 57 -88.96 -92.43
REMARK 500 LEU D 58 3.52 -61.38
REMARK 500 GLU D 108 53.50 -119.52
REMARK 500 CYS D 154 -74.88 -121.77
REMARK 500 SER D 238 -0.42 71.95
REMARK 500 VAL D 256 -60.74 -104.67
REMARK 500 LEU D 295 -46.68 -146.68
REMARK 500 VAL D 296 -138.72 -124.86
REMARK 500 ASN D 298 -168.61 -103.73
REMARK 500 GLU E 108 53.09 -119.06
REMARK 500 CYS E 154 -72.40 -124.57
REMARK 500 VAL E 256 -63.13 -103.96
REMARK 500 LEU E 295 -44.08 -144.28
REMARK 500 VAL E 296 -135.98 -129.08
REMARK 500 ASN E 298 -169.69 -106.65
REMARK 500 PHE H 49 82.21 -176.14
REMARK 500 ILE H 120 -62.22 -120.38
REMARK 500 TYR H 126 49.91 -75.08
REMARK 500 CYS H 154 -74.94 -122.36
REMARK 500 SER H 238 -5.69 75.36
REMARK 500 VAL H 256 -61.94 -102.71
REMARK 500 LEU H 295 -46.18 -146.75
REMARK 500 VAL H 296 -138.57 -124.87
REMARK 500 ASN H 298 -168.64 -105.60
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 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 HIS A 68 NE2 103.0
REMARK 620 3 GLU A 69 OE2 104.0 111.9
REMARK 620 4 CYS A 154 SG 117.3 111.4 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 98 OE2
REMARK 620 2 CYS A 101 SG 102.5
REMARK 620 3 CYS A 104 SG 107.1 114.6
REMARK 620 4 CYS A 112 SG 109.9 118.6 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 38 SG
REMARK 620 2 HIS B 68 NE2 102.7
REMARK 620 3 GLU B 69 OE2 103.0 114.4
REMARK 620 4 CYS B 154 SG 118.4 107.6 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 98 OE2
REMARK 620 2 CYS B 101 SG 100.8
REMARK 620 3 CYS B 104 SG 111.0 115.7
REMARK 620 4 CYS B 112 SG 110.0 117.5 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 38 SG
REMARK 620 2 HIS C 68 NE2 102.2
REMARK 620 3 GLU C 69 OE2 105.7 114.3
REMARK 620 4 CYS C 154 SG 116.7 108.6 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 98 OE2
REMARK 620 2 CYS C 101 SG 98.3
REMARK 620 3 CYS C 104 SG 112.8 115.4
REMARK 620 4 CYS C 112 SG 106.6 119.3 104.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 38 SG
REMARK 620 2 HIS D 68 NE2 104.7
REMARK 620 3 GLU D 69 OE2 105.1 116.3
REMARK 620 4 CYS D 154 SG 119.4 106.5 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 98 OE2
REMARK 620 2 CYS D 101 SG 102.9
REMARK 620 3 CYS D 104 SG 106.5 116.8
REMARK 620 4 CYS D 112 SG 110.2 115.1 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 38 SG
REMARK 620 2 HIS E 68 NE2 104.3
REMARK 620 3 GLU E 69 OE2 102.4 115.9
REMARK 620 4 CYS E 154 SG 119.7 107.1 107.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 98 OE2
REMARK 620 2 CYS E 101 SG 102.0
REMARK 620 3 CYS E 104 SG 106.6 115.1
REMARK 620 4 CYS E 112 SG 111.6 116.8 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 38 SG
REMARK 620 2 HIS H 68 NE2 99.5
REMARK 620 3 GLU H 69 OE2 101.4 113.3
REMARK 620 4 CYS H 154 SG 123.0 107.9 111.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU H 98 OE2
REMARK 620 2 CYS H 101 SG 100.7
REMARK 620 3 CYS H 104 SG 108.7 113.7
REMARK 620 4 CYS H 112 SG 110.8 118.4 104.5
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 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JVB RELATED DB: PDB
REMARK 900 NATIVE STRUCTURE
REMARK 900 RELATED ID: 1NTO RELATED DB: PDB
REMARK 900 N249Y-SSADH MONOCLINIC FORM
REMARK 900 RELATED ID: 1NVG RELATED DB: PDB
REMARK 900 N249Y-SSADH TETRAGONAL FORM
REMARK 900 RELATED ID: 1R37 RELATED DB: PDB
REMARK 900 SSADH COMPLEX WITH NAD AND 2-ETHOXYETHANOL
DBREF 3I4C A 1 347 UNP P39462 ADH_SULSO 1 347
DBREF 3I4C B 1 347 UNP P39462 ADH_SULSO 1 347
DBREF 3I4C C 1 347 UNP P39462 ADH_SULSO 1 347
DBREF 3I4C D 1 347 UNP P39462 ADH_SULSO 1 347
DBREF 3I4C E 1 347 UNP P39462 ADH_SULSO 1 347
DBREF 3I4C H 1 347 UNP P39462 ADH_SULSO 1 347
SEQADV 3I4C LEU A 95 UNP P39462 TRP 95 ENGINEERED MUTATION
SEQADV 3I4C TYR A 249 UNP P39462 ASN 249 ENGINEERED MUTATION
SEQADV 3I4C LEU B 95 UNP P39462 TRP 95 ENGINEERED MUTATION
SEQADV 3I4C TYR B 249 UNP P39462 ASN 249 ENGINEERED MUTATION
SEQADV 3I4C LEU C 95 UNP P39462 TRP 95 ENGINEERED MUTATION
SEQADV 3I4C TYR C 249 UNP P39462 ASN 249 ENGINEERED MUTATION
SEQADV 3I4C LEU D 95 UNP P39462 TRP 95 ENGINEERED MUTATION
SEQADV 3I4C TYR D 249 UNP P39462 ASN 249 ENGINEERED MUTATION
SEQADV 3I4C LEU E 95 UNP P39462 TRP 95 ENGINEERED MUTATION
SEQADV 3I4C TYR E 249 UNP P39462 ASN 249 ENGINEERED MUTATION
SEQADV 3I4C LEU H 95 UNP P39462 TRP 95 ENGINEERED MUTATION
SEQADV 3I4C TYR H 249 UNP P39462 ASN 249 ENGINEERED MUTATION
SEQRES 1 A 347 MET ARG ALA VAL ARG LEU VAL GLU ILE GLY LYS PRO LEU
SEQRES 2 A 347 SER LEU GLN GLU ILE GLY VAL PRO LYS PRO LYS GLY PRO
SEQRES 3 A 347 GLN VAL LEU ILE LYS VAL GLU ALA ALA GLY VAL CYS HIS
SEQRES 4 A 347 SER ASP VAL HIS MET ARG GLN GLY ARG PHE GLY ASN LEU
SEQRES 5 A 347 ARG ILE VAL GLU ASP LEU GLY VAL LYS LEU PRO VAL THR
SEQRES 6 A 347 LEU GLY HIS GLU ILE ALA GLY LYS ILE GLU GLU VAL GLY
SEQRES 7 A 347 ASP GLU VAL VAL GLY TYR SER LYS GLY ASP LEU VAL ALA
SEQRES 8 A 347 VAL ASN PRO LEU GLN GLY GLU GLY ASN CYS TYR TYR CYS
SEQRES 9 A 347 ARG ILE GLY GLU GLU HIS LEU CYS ASP SER PRO ARG TRP
SEQRES 10 A 347 LEU GLY ILE ASN PHE ASP GLY ALA TYR ALA GLU TYR VAL
SEQRES 11 A 347 ILE VAL PRO HIS TYR LYS TYR MET TYR LYS LEU ARG ARG
SEQRES 12 A 347 LEU ASN ALA VAL GLU ALA ALA PRO LEU THR CYS SER GLY
SEQRES 13 A 347 ILE THR THR TYR ARG ALA VAL ARG LYS ALA SER LEU ASP
SEQRES 14 A 347 PRO THR LYS THR LEU LEU VAL VAL GLY ALA GLY GLY GLY
SEQRES 15 A 347 LEU GLY THR MET ALA VAL GLN ILE ALA LYS ALA VAL SER
SEQRES 16 A 347 GLY ALA THR ILE ILE GLY VAL ASP VAL ARG GLU GLU ALA
SEQRES 17 A 347 VAL GLU ALA ALA LYS ARG ALA GLY ALA ASP TYR VAL ILE
SEQRES 18 A 347 ASN ALA SER MET GLN ASP PRO LEU ALA GLU ILE ARG ARG
SEQRES 19 A 347 ILE THR GLU SER LYS GLY VAL ASP ALA VAL ILE ASP LEU
SEQRES 20 A 347 ASN TYR SER GLU LYS THR LEU SER VAL TYR PRO LYS ALA
SEQRES 21 A 347 LEU ALA LYS GLN GLY LYS TYR VAL MET VAL GLY LEU PHE
SEQRES 22 A 347 GLY ALA ASP LEU HIS TYR HIS ALA PRO LEU ILE THR LEU
SEQRES 23 A 347 SER GLU ILE GLN PHE VAL GLY SER LEU VAL GLY ASN GLN
SEQRES 24 A 347 SER ASP PHE LEU GLY ILE MET ARG LEU ALA GLU ALA GLY
SEQRES 25 A 347 LYS VAL LYS PRO MET ILE THR LYS THR MET LYS LEU GLU
SEQRES 26 A 347 GLU ALA ASN GLU ALA ILE ASP ASN LEU GLU ASN PHE LYS
SEQRES 27 A 347 ALA ILE GLY ARG GLN VAL LEU ILE PRO
SEQRES 1 B 347 MET ARG ALA VAL ARG LEU VAL GLU ILE GLY LYS PRO LEU
SEQRES 2 B 347 SER LEU GLN GLU ILE GLY VAL PRO LYS PRO LYS GLY PRO
SEQRES 3 B 347 GLN VAL LEU ILE LYS VAL GLU ALA ALA GLY VAL CYS HIS
SEQRES 4 B 347 SER ASP VAL HIS MET ARG GLN GLY ARG PHE GLY ASN LEU
SEQRES 5 B 347 ARG ILE VAL GLU ASP LEU GLY VAL LYS LEU PRO VAL THR
SEQRES 6 B 347 LEU GLY HIS GLU ILE ALA GLY LYS ILE GLU GLU VAL GLY
SEQRES 7 B 347 ASP GLU VAL VAL GLY TYR SER LYS GLY ASP LEU VAL ALA
SEQRES 8 B 347 VAL ASN PRO LEU GLN GLY GLU GLY ASN CYS TYR TYR CYS
SEQRES 9 B 347 ARG ILE GLY GLU GLU HIS LEU CYS ASP SER PRO ARG TRP
SEQRES 10 B 347 LEU GLY ILE ASN PHE ASP GLY ALA TYR ALA GLU TYR VAL
SEQRES 11 B 347 ILE VAL PRO HIS TYR LYS TYR MET TYR LYS LEU ARG ARG
SEQRES 12 B 347 LEU ASN ALA VAL GLU ALA ALA PRO LEU THR CYS SER GLY
SEQRES 13 B 347 ILE THR THR TYR ARG ALA VAL ARG LYS ALA SER LEU ASP
SEQRES 14 B 347 PRO THR LYS THR LEU LEU VAL VAL GLY ALA GLY GLY GLY
SEQRES 15 B 347 LEU GLY THR MET ALA VAL GLN ILE ALA LYS ALA VAL SER
SEQRES 16 B 347 GLY ALA THR ILE ILE GLY VAL ASP VAL ARG GLU GLU ALA
SEQRES 17 B 347 VAL GLU ALA ALA LYS ARG ALA GLY ALA ASP TYR VAL ILE
SEQRES 18 B 347 ASN ALA SER MET GLN ASP PRO LEU ALA GLU ILE ARG ARG
SEQRES 19 B 347 ILE THR GLU SER LYS GLY VAL ASP ALA VAL ILE ASP LEU
SEQRES 20 B 347 ASN TYR SER GLU LYS THR LEU SER VAL TYR PRO LYS ALA
SEQRES 21 B 347 LEU ALA LYS GLN GLY LYS TYR VAL MET VAL GLY LEU PHE
SEQRES 22 B 347 GLY ALA ASP LEU HIS TYR HIS ALA PRO LEU ILE THR LEU
SEQRES 23 B 347 SER GLU ILE GLN PHE VAL GLY SER LEU VAL GLY ASN GLN
SEQRES 24 B 347 SER ASP PHE LEU GLY ILE MET ARG LEU ALA GLU ALA GLY
SEQRES 25 B 347 LYS VAL LYS PRO MET ILE THR LYS THR MET LYS LEU GLU
SEQRES 26 B 347 GLU ALA ASN GLU ALA ILE ASP ASN LEU GLU ASN PHE LYS
SEQRES 27 B 347 ALA ILE GLY ARG GLN VAL LEU ILE PRO
SEQRES 1 C 347 MET ARG ALA VAL ARG LEU VAL GLU ILE GLY LYS PRO LEU
SEQRES 2 C 347 SER LEU GLN GLU ILE GLY VAL PRO LYS PRO LYS GLY PRO
SEQRES 3 C 347 GLN VAL LEU ILE LYS VAL GLU ALA ALA GLY VAL CYS HIS
SEQRES 4 C 347 SER ASP VAL HIS MET ARG GLN GLY ARG PHE GLY ASN LEU
SEQRES 5 C 347 ARG ILE VAL GLU ASP LEU GLY VAL LYS LEU PRO VAL THR
SEQRES 6 C 347 LEU GLY HIS GLU ILE ALA GLY LYS ILE GLU GLU VAL GLY
SEQRES 7 C 347 ASP GLU VAL VAL GLY TYR SER LYS GLY ASP LEU VAL ALA
SEQRES 8 C 347 VAL ASN PRO LEU GLN GLY GLU GLY ASN CYS TYR TYR CYS
SEQRES 9 C 347 ARG ILE GLY GLU GLU HIS LEU CYS ASP SER PRO ARG TRP
SEQRES 10 C 347 LEU GLY ILE ASN PHE ASP GLY ALA TYR ALA GLU TYR VAL
SEQRES 11 C 347 ILE VAL PRO HIS TYR LYS TYR MET TYR LYS LEU ARG ARG
SEQRES 12 C 347 LEU ASN ALA VAL GLU ALA ALA PRO LEU THR CYS SER GLY
SEQRES 13 C 347 ILE THR THR TYR ARG ALA VAL ARG LYS ALA SER LEU ASP
SEQRES 14 C 347 PRO THR LYS THR LEU LEU VAL VAL GLY ALA GLY GLY GLY
SEQRES 15 C 347 LEU GLY THR MET ALA VAL GLN ILE ALA LYS ALA VAL SER
SEQRES 16 C 347 GLY ALA THR ILE ILE GLY VAL ASP VAL ARG GLU GLU ALA
SEQRES 17 C 347 VAL GLU ALA ALA LYS ARG ALA GLY ALA ASP TYR VAL ILE
SEQRES 18 C 347 ASN ALA SER MET GLN ASP PRO LEU ALA GLU ILE ARG ARG
SEQRES 19 C 347 ILE THR GLU SER LYS GLY VAL ASP ALA VAL ILE ASP LEU
SEQRES 20 C 347 ASN TYR SER GLU LYS THR LEU SER VAL TYR PRO LYS ALA
SEQRES 21 C 347 LEU ALA LYS GLN GLY LYS TYR VAL MET VAL GLY LEU PHE
SEQRES 22 C 347 GLY ALA ASP LEU HIS TYR HIS ALA PRO LEU ILE THR LEU
SEQRES 23 C 347 SER GLU ILE GLN PHE VAL GLY SER LEU VAL GLY ASN GLN
SEQRES 24 C 347 SER ASP PHE LEU GLY ILE MET ARG LEU ALA GLU ALA GLY
SEQRES 25 C 347 LYS VAL LYS PRO MET ILE THR LYS THR MET LYS LEU GLU
SEQRES 26 C 347 GLU ALA ASN GLU ALA ILE ASP ASN LEU GLU ASN PHE LYS
SEQRES 27 C 347 ALA ILE GLY ARG GLN VAL LEU ILE PRO
SEQRES 1 D 347 MET ARG ALA VAL ARG LEU VAL GLU ILE GLY LYS PRO LEU
SEQRES 2 D 347 SER LEU GLN GLU ILE GLY VAL PRO LYS PRO LYS GLY PRO
SEQRES 3 D 347 GLN VAL LEU ILE LYS VAL GLU ALA ALA GLY VAL CYS HIS
SEQRES 4 D 347 SER ASP VAL HIS MET ARG GLN GLY ARG PHE GLY ASN LEU
SEQRES 5 D 347 ARG ILE VAL GLU ASP LEU GLY VAL LYS LEU PRO VAL THR
SEQRES 6 D 347 LEU GLY HIS GLU ILE ALA GLY LYS ILE GLU GLU VAL GLY
SEQRES 7 D 347 ASP GLU VAL VAL GLY TYR SER LYS GLY ASP LEU VAL ALA
SEQRES 8 D 347 VAL ASN PRO LEU GLN GLY GLU GLY ASN CYS TYR TYR CYS
SEQRES 9 D 347 ARG ILE GLY GLU GLU HIS LEU CYS ASP SER PRO ARG TRP
SEQRES 10 D 347 LEU GLY ILE ASN PHE ASP GLY ALA TYR ALA GLU TYR VAL
SEQRES 11 D 347 ILE VAL PRO HIS TYR LYS TYR MET TYR LYS LEU ARG ARG
SEQRES 12 D 347 LEU ASN ALA VAL GLU ALA ALA PRO LEU THR CYS SER GLY
SEQRES 13 D 347 ILE THR THR TYR ARG ALA VAL ARG LYS ALA SER LEU ASP
SEQRES 14 D 347 PRO THR LYS THR LEU LEU VAL VAL GLY ALA GLY GLY GLY
SEQRES 15 D 347 LEU GLY THR MET ALA VAL GLN ILE ALA LYS ALA VAL SER
SEQRES 16 D 347 GLY ALA THR ILE ILE GLY VAL ASP VAL ARG GLU GLU ALA
SEQRES 17 D 347 VAL GLU ALA ALA LYS ARG ALA GLY ALA ASP TYR VAL ILE
SEQRES 18 D 347 ASN ALA SER MET GLN ASP PRO LEU ALA GLU ILE ARG ARG
SEQRES 19 D 347 ILE THR GLU SER LYS GLY VAL ASP ALA VAL ILE ASP LEU
SEQRES 20 D 347 ASN TYR SER GLU LYS THR LEU SER VAL TYR PRO LYS ALA
SEQRES 21 D 347 LEU ALA LYS GLN GLY LYS TYR VAL MET VAL GLY LEU PHE
SEQRES 22 D 347 GLY ALA ASP LEU HIS TYR HIS ALA PRO LEU ILE THR LEU
SEQRES 23 D 347 SER GLU ILE GLN PHE VAL GLY SER LEU VAL GLY ASN GLN
SEQRES 24 D 347 SER ASP PHE LEU GLY ILE MET ARG LEU ALA GLU ALA GLY
SEQRES 25 D 347 LYS VAL LYS PRO MET ILE THR LYS THR MET LYS LEU GLU
SEQRES 26 D 347 GLU ALA ASN GLU ALA ILE ASP ASN LEU GLU ASN PHE LYS
SEQRES 27 D 347 ALA ILE GLY ARG GLN VAL LEU ILE PRO
SEQRES 1 E 347 MET ARG ALA VAL ARG LEU VAL GLU ILE GLY LYS PRO LEU
SEQRES 2 E 347 SER LEU GLN GLU ILE GLY VAL PRO LYS PRO LYS GLY PRO
SEQRES 3 E 347 GLN VAL LEU ILE LYS VAL GLU ALA ALA GLY VAL CYS HIS
SEQRES 4 E 347 SER ASP VAL HIS MET ARG GLN GLY ARG PHE GLY ASN LEU
SEQRES 5 E 347 ARG ILE VAL GLU ASP LEU GLY VAL LYS LEU PRO VAL THR
SEQRES 6 E 347 LEU GLY HIS GLU ILE ALA GLY LYS ILE GLU GLU VAL GLY
SEQRES 7 E 347 ASP GLU VAL VAL GLY TYR SER LYS GLY ASP LEU VAL ALA
SEQRES 8 E 347 VAL ASN PRO LEU GLN GLY GLU GLY ASN CYS TYR TYR CYS
SEQRES 9 E 347 ARG ILE GLY GLU GLU HIS LEU CYS ASP SER PRO ARG TRP
SEQRES 10 E 347 LEU GLY ILE ASN PHE ASP GLY ALA TYR ALA GLU TYR VAL
SEQRES 11 E 347 ILE VAL PRO HIS TYR LYS TYR MET TYR LYS LEU ARG ARG
SEQRES 12 E 347 LEU ASN ALA VAL GLU ALA ALA PRO LEU THR CYS SER GLY
SEQRES 13 E 347 ILE THR THR TYR ARG ALA VAL ARG LYS ALA SER LEU ASP
SEQRES 14 E 347 PRO THR LYS THR LEU LEU VAL VAL GLY ALA GLY GLY GLY
SEQRES 15 E 347 LEU GLY THR MET ALA VAL GLN ILE ALA LYS ALA VAL SER
SEQRES 16 E 347 GLY ALA THR ILE ILE GLY VAL ASP VAL ARG GLU GLU ALA
SEQRES 17 E 347 VAL GLU ALA ALA LYS ARG ALA GLY ALA ASP TYR VAL ILE
SEQRES 18 E 347 ASN ALA SER MET GLN ASP PRO LEU ALA GLU ILE ARG ARG
SEQRES 19 E 347 ILE THR GLU SER LYS GLY VAL ASP ALA VAL ILE ASP LEU
SEQRES 20 E 347 ASN TYR SER GLU LYS THR LEU SER VAL TYR PRO LYS ALA
SEQRES 21 E 347 LEU ALA LYS GLN GLY LYS TYR VAL MET VAL GLY LEU PHE
SEQRES 22 E 347 GLY ALA ASP LEU HIS TYR HIS ALA PRO LEU ILE THR LEU
SEQRES 23 E 347 SER GLU ILE GLN PHE VAL GLY SER LEU VAL GLY ASN GLN
SEQRES 24 E 347 SER ASP PHE LEU GLY ILE MET ARG LEU ALA GLU ALA GLY
SEQRES 25 E 347 LYS VAL LYS PRO MET ILE THR LYS THR MET LYS LEU GLU
SEQRES 26 E 347 GLU ALA ASN GLU ALA ILE ASP ASN LEU GLU ASN PHE LYS
SEQRES 27 E 347 ALA ILE GLY ARG GLN VAL LEU ILE PRO
SEQRES 1 H 347 MET ARG ALA VAL ARG LEU VAL GLU ILE GLY LYS PRO LEU
SEQRES 2 H 347 SER LEU GLN GLU ILE GLY VAL PRO LYS PRO LYS GLY PRO
SEQRES 3 H 347 GLN VAL LEU ILE LYS VAL GLU ALA ALA GLY VAL CYS HIS
SEQRES 4 H 347 SER ASP VAL HIS MET ARG GLN GLY ARG PHE GLY ASN LEU
SEQRES 5 H 347 ARG ILE VAL GLU ASP LEU GLY VAL LYS LEU PRO VAL THR
SEQRES 6 H 347 LEU GLY HIS GLU ILE ALA GLY LYS ILE GLU GLU VAL GLY
SEQRES 7 H 347 ASP GLU VAL VAL GLY TYR SER LYS GLY ASP LEU VAL ALA
SEQRES 8 H 347 VAL ASN PRO LEU GLN GLY GLU GLY ASN CYS TYR TYR CYS
SEQRES 9 H 347 ARG ILE GLY GLU GLU HIS LEU CYS ASP SER PRO ARG TRP
SEQRES 10 H 347 LEU GLY ILE ASN PHE ASP GLY ALA TYR ALA GLU TYR VAL
SEQRES 11 H 347 ILE VAL PRO HIS TYR LYS TYR MET TYR LYS LEU ARG ARG
SEQRES 12 H 347 LEU ASN ALA VAL GLU ALA ALA PRO LEU THR CYS SER GLY
SEQRES 13 H 347 ILE THR THR TYR ARG ALA VAL ARG LYS ALA SER LEU ASP
SEQRES 14 H 347 PRO THR LYS THR LEU LEU VAL VAL GLY ALA GLY GLY GLY
SEQRES 15 H 347 LEU GLY THR MET ALA VAL GLN ILE ALA LYS ALA VAL SER
SEQRES 16 H 347 GLY ALA THR ILE ILE GLY VAL ASP VAL ARG GLU GLU ALA
SEQRES 17 H 347 VAL GLU ALA ALA LYS ARG ALA GLY ALA ASP TYR VAL ILE
SEQRES 18 H 347 ASN ALA SER MET GLN ASP PRO LEU ALA GLU ILE ARG ARG
SEQRES 19 H 347 ILE THR GLU SER LYS GLY VAL ASP ALA VAL ILE ASP LEU
SEQRES 20 H 347 ASN TYR SER GLU LYS THR LEU SER VAL TYR PRO LYS ALA
SEQRES 21 H 347 LEU ALA LYS GLN GLY LYS TYR VAL MET VAL GLY LEU PHE
SEQRES 22 H 347 GLY ALA ASP LEU HIS TYR HIS ALA PRO LEU ILE THR LEU
SEQRES 23 H 347 SER GLU ILE GLN PHE VAL GLY SER LEU VAL GLY ASN GLN
SEQRES 24 H 347 SER ASP PHE LEU GLY ILE MET ARG LEU ALA GLU ALA GLY
SEQRES 25 H 347 LYS VAL LYS PRO MET ILE THR LYS THR MET LYS LEU GLU
SEQRES 26 H 347 GLU ALA ASN GLU ALA ILE ASP ASN LEU GLU ASN PHE LYS
SEQRES 27 H 347 ALA ILE GLY ARG GLN VAL LEU ILE PRO
HET ZN A 400 1
HET ZN A 500 1
HET ZN B 400 1
HET ZN B 500 1
HET ZN C 400 1
HET ZN C 500 1
HET ZN D 400 1
HET ZN D 500 1
HET ZN E 400 1
HET ZN E 500 1
HET ZN H 400 1
HET ZN H 500 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 12(ZN 2+)
FORMUL 19 HOH *429(H2 O)
HELIX 1 1 HIS A 39 GLY A 47 1 9
HELIX 2 2 CYS A 101 ILE A 106 1 6
HELIX 3 3 GLU A 108 CYS A 112 5 5
HELIX 4 4 HIS A 134 LYS A 136 5 3
HELIX 5 5 ASN A 145 ALA A 150 1 6
HELIX 6 6 PRO A 151 THR A 153 5 3
HELIX 7 7 CYS A 154 ALA A 166 1 13
HELIX 8 8 GLY A 181 SER A 195 1 15
HELIX 9 9 ARG A 205 ALA A 215 1 11
HELIX 10 10 ASP A 227 THR A 236 1 10
HELIX 11 11 SER A 250 TYR A 257 1 8
HELIX 12 12 ALA A 281 GLU A 288 1 8
HELIX 13 13 ASN A 298 ALA A 311 1 14
HELIX 14 14 LYS A 323 GLU A 325 5 3
HELIX 15 15 GLU A 326 ASN A 336 1 11
HELIX 16 16 HIS B 39 ARG B 45 1 7
HELIX 17 17 CYS B 101 ILE B 106 1 6
HELIX 18 18 GLU B 108 CYS B 112 5 5
HELIX 19 19 HIS B 134 LYS B 136 5 3
HELIX 20 20 ASN B 145 ALA B 150 1 6
HELIX 21 21 PRO B 151 THR B 153 5 3
HELIX 22 22 CYS B 154 ALA B 166 1 13
HELIX 23 23 GLY B 181 SER B 195 1 15
HELIX 24 24 ARG B 205 GLY B 216 1 12
HELIX 25 25 ASP B 227 THR B 236 1 10
HELIX 26 26 SER B 250 TYR B 257 1 8
HELIX 27 27 ALA B 281 GLU B 288 1 8
HELIX 28 28 ASN B 298 ALA B 311 1 14
HELIX 29 29 GLU B 326 ASP B 332 1 7
HELIX 30 30 CYS C 101 ILE C 106 1 6
HELIX 31 31 GLU C 108 CYS C 112 5 5
HELIX 32 32 HIS C 134 LYS C 136 5 3
HELIX 33 33 ASN C 145 ALA C 150 1 6
HELIX 34 34 PRO C 151 THR C 153 5 3
HELIX 35 35 CYS C 154 ALA C 166 1 13
HELIX 36 36 GLY C 181 SER C 195 1 15
HELIX 37 37 ARG C 205 GLY C 216 1 12
HELIX 38 38 ASP C 227 THR C 236 1 10
HELIX 39 39 SER C 250 TYR C 257 1 8
HELIX 40 40 ALA C 281 GLU C 288 1 8
HELIX 41 41 ASN C 298 ALA C 311 1 14
HELIX 42 42 LYS C 323 GLU C 325 5 3
HELIX 43 43 GLU C 326 ASN C 333 1 8
HELIX 44 44 HIS D 39 ARG D 45 1 7
HELIX 45 45 CYS D 101 ILE D 106 1 6
HELIX 46 46 GLU D 108 CYS D 112 5 5
HELIX 47 47 HIS D 134 LYS D 136 5 3
HELIX 48 48 ASN D 145 ALA D 150 1 6
HELIX 49 49 PRO D 151 THR D 153 5 3
HELIX 50 50 CYS D 154 ALA D 166 1 13
HELIX 51 51 GLY D 181 SER D 195 1 15
HELIX 52 52 ARG D 205 GLY D 216 1 12
HELIX 53 53 ASP D 227 THR D 236 1 10
HELIX 54 54 SER D 250 TYR D 257 1 8
HELIX 55 55 ALA D 281 GLU D 288 1 8
HELIX 56 56 ASN D 298 ALA D 311 1 14
HELIX 57 57 GLU D 326 ASN D 336 1 11
HELIX 58 58 HIS E 39 GLN E 46 1 8
HELIX 59 59 CYS E 101 ILE E 106 1 6
HELIX 60 60 GLU E 108 CYS E 112 5 5
HELIX 61 61 HIS E 134 LYS E 136 5 3
HELIX 62 62 ASN E 145 ALA E 150 1 6
HELIX 63 63 PRO E 151 THR E 153 5 3
HELIX 64 64 CYS E 154 ALA E 166 1 13
HELIX 65 65 GLY E 181 SER E 195 1 15
HELIX 66 66 ARG E 205 GLY E 216 1 12
HELIX 67 67 ASP E 227 THR E 236 1 10
HELIX 68 68 SER E 250 TYR E 257 1 8
HELIX 69 69 HIS E 280 GLU E 288 1 9
HELIX 70 70 ASN E 298 ALA E 311 1 14
HELIX 71 71 GLU E 326 ASN E 333 1 8
HELIX 72 72 HIS H 39 GLN H 46 1 8
HELIX 73 73 CYS H 101 ILE H 106 1 6
HELIX 74 74 GLU H 108 CYS H 112 5 5
HELIX 75 75 HIS H 134 LYS H 136 5 3
HELIX 76 76 ASN H 145 ALA H 150 1 6
HELIX 77 77 PRO H 151 THR H 153 5 3
HELIX 78 78 CYS H 154 ALA H 166 1 13
HELIX 79 79 GLY H 181 SER H 195 1 15
HELIX 80 80 ARG H 205 GLY H 216 1 12
HELIX 81 81 ASP H 227 THR H 236 1 10
HELIX 82 82 SER H 250 TYR H 257 1 8
HELIX 83 83 HIS H 280 GLU H 288 1 9
HELIX 84 84 ASN H 298 ALA H 311 1 14
HELIX 85 85 LYS H 323 GLU H 325 5 3
HELIX 86 86 GLU H 326 GLU H 335 1 10
SHEET 1 A 3 SER A 14 GLU A 17 0
SHEET 2 A 3 ARG A 2 LEU A 6 -1 N ARG A 5 O SER A 14
SHEET 3 A 3 VAL A 64 THR A 65 -1 O VAL A 64 N LEU A 6
SHEET 1 B 5 TYR A 129 VAL A 132 0
SHEET 2 B 5 VAL A 28 VAL A 37 -1 N ILE A 30 O VAL A 130
SHEET 3 B 5 GLU A 69 VAL A 77 -1 O GLU A 76 N LEU A 29
SHEET 4 B 5 LEU A 89 VAL A 92 -1 O VAL A 90 N GLY A 72
SHEET 5 B 5 MET A 138 LYS A 140 -1 O TYR A 139 N ALA A 91
SHEET 1 C 4 TYR A 129 VAL A 132 0
SHEET 2 C 4 VAL A 28 VAL A 37 -1 N ILE A 30 O VAL A 130
SHEET 3 C 4 ARG A 342 LEU A 345 -1 O LEU A 345 N ALA A 35
SHEET 4 C 4 THR A 319 MET A 322 1 N LYS A 320 O ARG A 342
SHEET 1 D 2 LEU A 95 GLN A 96 0
SHEET 2 D 2 ARG A 116 TRP A 117 -1 O ARG A 116 N GLN A 96
SHEET 1 E12 TYR A 219 ASN A 222 0
SHEET 2 E12 THR A 198 ASP A 203 1 N GLY A 201 O TYR A 219
SHEET 3 E12 THR A 173 VAL A 177 1 N LEU A 174 O THR A 198
SHEET 4 E12 VAL A 241 LEU A 247 1 O ILE A 245 N VAL A 177
SHEET 5 E12 LEU A 261 VAL A 270 1 O VAL A 268 N VAL A 244
SHEET 6 E12 GLN A 290 SER A 294 1 O GLN A 290 N TYR A 267
SHEET 7 E12 GLN B 290 SER B 294 -1 O PHE B 291 N PHE A 291
SHEET 8 E12 LEU B 261 VAL B 270 1 N TYR B 267 O GLN B 290
SHEET 9 E12 VAL B 241 LEU B 247 1 N VAL B 244 O VAL B 268
SHEET 10 E12 THR B 173 VAL B 177 1 N LEU B 175 O ILE B 245
SHEET 11 E12 THR B 198 ASP B 203 1 O ILE B 200 N LEU B 174
SHEET 12 E12 TYR B 219 ASN B 222 1 O TYR B 219 N GLY B 201
SHEET 1 F 2 ASP A 276 HIS A 280 0
SHEET 2 F 2 ASP B 276 HIS B 280 -1 O LEU B 277 N TYR A 279
SHEET 1 G 2 ARG B 5 LEU B 6 0
SHEET 2 G 2 VAL B 64 THR B 65 -1 O VAL B 64 N LEU B 6
SHEET 1 H 5 TYR B 129 VAL B 132 0
SHEET 2 H 5 VAL B 28 GLY B 36 -1 N ILE B 30 O VAL B 130
SHEET 3 H 5 GLU B 69 VAL B 77 -1 O LYS B 73 N LYS B 31
SHEET 4 H 5 LEU B 89 VAL B 92 -1 O VAL B 90 N GLY B 72
SHEET 5 H 5 MET B 138 LYS B 140 -1 O TYR B 139 N ALA B 91
SHEET 1 I 4 TYR B 129 VAL B 132 0
SHEET 2 I 4 VAL B 28 GLY B 36 -1 N ILE B 30 O VAL B 130
SHEET 3 I 4 VAL B 344 ILE B 346 -1 O LEU B 345 N ALA B 35
SHEET 4 I 4 THR B 321 LYS B 323 1 N MET B 322 O ILE B 346
SHEET 1 J 2 LEU B 95 GLN B 96 0
SHEET 2 J 2 ARG B 116 TRP B 117 -1 O ARG B 116 N GLN B 96
SHEET 1 K 2 ARG C 2 ARG C 5 0
SHEET 2 K 2 SER C 14 GLU C 17 -1 O SER C 14 N ARG C 5
SHEET 1 L 5 TYR C 129 VAL C 132 0
SHEET 2 L 5 VAL C 28 VAL C 37 -1 N ILE C 30 O VAL C 130
SHEET 3 L 5 GLU C 69 VAL C 77 -1 O LYS C 73 N LYS C 31
SHEET 4 L 5 LEU C 89 VAL C 92 -1 O VAL C 90 N GLY C 72
SHEET 5 L 5 MET C 138 LYS C 140 -1 O TYR C 139 N ALA C 91
SHEET 1 M 4 TYR C 129 VAL C 132 0
SHEET 2 M 4 VAL C 28 VAL C 37 -1 N ILE C 30 O VAL C 130
SHEET 3 M 4 GLN C 343 LEU C 345 -1 O LEU C 345 N ALA C 35
SHEET 4 M 4 LYS C 320 MET C 322 1 N MET C 322 O VAL C 344
SHEET 1 N 2 LEU C 95 GLN C 96 0
SHEET 2 N 2 ARG C 116 TRP C 117 -1 O ARG C 116 N GLN C 96
SHEET 1 O12 TYR C 219 ASN C 222 0
SHEET 2 O12 THR C 198 ASP C 203 1 N GLY C 201 O TYR C 219
SHEET 3 O12 THR C 173 VAL C 177 1 N LEU C 174 O ILE C 200
SHEET 4 O12 VAL C 241 LEU C 247 1 O ILE C 245 N LEU C 175
SHEET 5 O12 LEU C 261 VAL C 270 1 O ALA C 262 N VAL C 241
SHEET 6 O12 GLN C 290 SER C 294 1 O GLN C 290 N TYR C 267
SHEET 7 O12 GLN D 290 SER D 294 -1 O PHE D 291 N PHE C 291
SHEET 8 O12 LEU D 261 VAL D 270 1 N TYR D 267 O GLN D 290
SHEET 9 O12 VAL D 241 LEU D 247 1 N VAL D 244 O VAL D 268
SHEET 10 O12 THR D 173 VAL D 177 1 N LEU D 175 O ILE D 245
SHEET 11 O12 THR D 198 ASP D 203 1 O ILE D 200 N LEU D 174
SHEET 12 O12 TYR D 219 ASN D 222 1 O TYR D 219 N GLY D 201
SHEET 1 P 2 ASP C 276 HIS C 280 0
SHEET 2 P 2 ASP D 276 HIS D 280 -1 O LEU D 277 N TYR C 279
SHEET 1 Q 3 SER D 14 GLU D 17 0
SHEET 2 Q 3 ARG D 2 LEU D 6 -1 N ALA D 3 O GLN D 16
SHEET 3 Q 3 VAL D 64 THR D 65 -1 O VAL D 64 N LEU D 6
SHEET 1 R 5 TYR D 129 VAL D 132 0
SHEET 2 R 5 VAL D 28 VAL D 37 -1 N ILE D 30 O VAL D 130
SHEET 3 R 5 GLU D 69 VAL D 77 -1 O LYS D 73 N LYS D 31
SHEET 4 R 5 LEU D 89 VAL D 92 -1 O VAL D 90 N GLY D 72
SHEET 5 R 5 MET D 138 LYS D 140 -1 O TYR D 139 N ALA D 91
SHEET 1 S 4 TYR D 129 VAL D 132 0
SHEET 2 S 4 VAL D 28 VAL D 37 -1 N ILE D 30 O VAL D 130
SHEET 3 S 4 GLN D 343 ILE D 346 -1 O LEU D 345 N ALA D 35
SHEET 4 S 4 LYS D 320 LYS D 323 1 N MET D 322 O ILE D 346
SHEET 1 T 2 LEU D 95 GLN D 96 0
SHEET 2 T 2 ARG D 116 TRP D 117 -1 O ARG D 116 N GLN D 96
SHEET 1 U 3 SER E 14 GLU E 17 0
SHEET 2 U 3 ARG E 2 LEU E 6 -1 N ARG E 5 O SER E 14
SHEET 3 U 3 VAL E 64 THR E 65 -1 O VAL E 64 N LEU E 6
SHEET 1 V 5 TYR E 129 VAL E 132 0
SHEET 2 V 5 VAL E 28 VAL E 37 -1 N ILE E 30 O VAL E 130
SHEET 3 V 5 GLU E 69 VAL E 77 -1 O GLU E 76 N LEU E 29
SHEET 4 V 5 LEU E 89 VAL E 92 -1 O VAL E 90 N GLY E 72
SHEET 5 V 5 MET E 138 LYS E 140 -1 O TYR E 139 N ALA E 91
SHEET 1 W 4 TYR E 129 VAL E 132 0
SHEET 2 W 4 VAL E 28 VAL E 37 -1 N ILE E 30 O VAL E 130
SHEET 3 W 4 ARG E 342 ILE E 346 -1 O LEU E 345 N ALA E 35
SHEET 4 W 4 THR E 319 LYS E 323 1 N MET E 322 O ILE E 346
SHEET 1 X 2 LEU E 95 GLN E 96 0
SHEET 2 X 2 ARG E 116 TRP E 117 -1 O ARG E 116 N GLN E 96
SHEET 1 Y 6 TYR E 219 ASN E 222 0
SHEET 2 Y 6 THR E 198 ASP E 203 1 N GLY E 201 O TYR E 219
SHEET 3 Y 6 THR E 173 VAL E 177 1 N LEU E 174 O ILE E 200
SHEET 4 Y 6 VAL E 241 LEU E 247 1 O ILE E 245 N LEU E 175
SHEET 5 Y 6 LEU E 261 VAL E 270 1 O VAL E 268 N VAL E 244
SHEET 6 Y 6 GLN E 290 SER E 294 1 O GLN E 290 N TYR E 267
SHEET 1 Z 3 SER H 14 GLU H 17 0
SHEET 2 Z 3 ARG H 2 LEU H 6 -1 N ARG H 5 O SER H 14
SHEET 3 Z 3 VAL H 64 THR H 65 -1 O VAL H 64 N LEU H 6
SHEET 1 AA 5 TYR H 129 VAL H 132 0
SHEET 2 AA 5 VAL H 28 VAL H 37 -1 N ILE H 30 O VAL H 130
SHEET 3 AA 5 GLU H 69 VAL H 77 -1 O GLU H 76 N LEU H 29
SHEET 4 AA 5 LEU H 89 VAL H 92 -1 O VAL H 90 N GLY H 72
SHEET 5 AA 5 MET H 138 LYS H 140 -1 O TYR H 139 N ALA H 91
SHEET 1 AB 4 TYR H 129 VAL H 132 0
SHEET 2 AB 4 VAL H 28 VAL H 37 -1 N ILE H 30 O VAL H 130
SHEET 3 AB 4 ARG H 342 LEU H 345 -1 O LEU H 345 N ALA H 35
SHEET 4 AB 4 THR H 319 MET H 322 1 N MET H 322 O VAL H 344
SHEET 1 AC 2 LEU H 95 GLN H 96 0
SHEET 2 AC 2 ARG H 116 TRP H 117 -1 O ARG H 116 N GLN H 96
SHEET 1 AD 6 TYR H 219 ASN H 222 0
SHEET 2 AD 6 THR H 198 ASP H 203 1 N GLY H 201 O TYR H 219
SHEET 3 AD 6 THR H 173 VAL H 177 1 N LEU H 174 O ILE H 200
SHEET 4 AD 6 VAL H 241 LEU H 247 1 O ILE H 245 N LEU H 175
SHEET 5 AD 6 LEU H 261 VAL H 270 1 O VAL H 268 N ASP H 246
SHEET 6 AD 6 GLN H 290 SER H 294 1 O GLN H 290 N TYR H 267
LINK SG CYS A 38 ZN ZN A 500 1555 1555 2.29
LINK NE2 HIS A 68 ZN ZN A 500 1555 1555 2.06
LINK OE2 GLU A 69 ZN ZN A 500 1555 1555 2.09
LINK OE2 GLU A 98 ZN ZN A 400 1555 1555 2.08
LINK SG CYS A 101 ZN ZN A 400 1555 1555 2.27
LINK SG CYS A 104 ZN ZN A 400 1555 1555 2.31
LINK SG CYS A 112 ZN ZN A 400 1555 1555 2.33
LINK SG CYS A 154 ZN ZN A 500 1555 1555 2.31
LINK SG CYS B 38 ZN ZN B 500 1555 1555 2.28
LINK NE2 HIS B 68 ZN ZN B 500 1555 1555 2.07
LINK OE2 GLU B 69 ZN ZN B 500 1555 1555 2.11
LINK OE2 GLU B 98 ZN ZN B 400 1555 1555 2.07
LINK SG CYS B 101 ZN ZN B 400 1555 1555 2.30
LINK SG CYS B 104 ZN ZN B 400 1555 1555 2.26
LINK SG CYS B 112 ZN ZN B 400 1555 1555 2.33
LINK SG CYS B 154 ZN ZN B 500 1555 1555 2.38
LINK SG CYS C 38 ZN ZN C 500 1555 1555 2.33
LINK NE2 HIS C 68 ZN ZN C 500 1555 1555 2.10
LINK OE2 GLU C 69 ZN ZN C 500 1555 1555 2.11
LINK OE2 GLU C 98 ZN ZN C 400 1555 1555 2.09
LINK SG CYS C 101 ZN ZN C 400 1555 1555 2.29
LINK SG CYS C 104 ZN ZN C 400 1555 1555 2.29
LINK SG CYS C 112 ZN ZN C 400 1555 1555 2.32
LINK SG CYS C 154 ZN ZN C 500 1555 1555 2.34
LINK SG CYS D 38 ZN ZN D 500 1555 1555 2.31
LINK NE2 HIS D 68 ZN ZN D 500 1555 1555 2.09
LINK OE2 GLU D 69 ZN ZN D 500 1555 1555 2.09
LINK OE2 GLU D 98 ZN ZN D 400 1555 1555 2.11
LINK SG CYS D 101 ZN ZN D 400 1555 1555 2.28
LINK SG CYS D 104 ZN ZN D 400 1555 1555 2.28
LINK SG CYS D 112 ZN ZN D 400 1555 1555 2.31
LINK SG CYS D 154 ZN ZN D 500 1555 1555 2.35
LINK SG CYS E 38 ZN ZN E 500 1555 1555 2.31
LINK NE2 HIS E 68 ZN ZN E 500 1555 1555 2.11
LINK OE2 GLU E 69 ZN ZN E 500 1555 1555 2.13
LINK OE2 GLU E 98 ZN ZN E 400 1555 1555 2.10
LINK SG CYS E 101 ZN ZN E 400 1555 1555 2.30
LINK SG CYS E 104 ZN ZN E 400 1555 1555 2.29
LINK SG CYS E 112 ZN ZN E 400 1555 1555 2.29
LINK SG CYS E 154 ZN ZN E 500 1555 1555 2.32
LINK SG CYS H 38 ZN ZN H 500 1555 1555 2.30
LINK NE2 HIS H 68 ZN ZN H 500 1555 1555 2.07
LINK OE2 GLU H 69 ZN ZN H 500 1555 1555 2.12
LINK OE2 GLU H 98 ZN ZN H 400 1555 1555 2.08
LINK SG CYS H 101 ZN ZN H 400 1555 1555 2.30
LINK SG CYS H 104 ZN ZN H 400 1555 1555 2.29
LINK SG CYS H 112 ZN ZN H 400 1555 1555 2.27
LINK SG CYS H 154 ZN ZN H 500 1555 1555 2.32
CISPEP 1 LEU A 62 PRO A 63 0 0.70
CISPEP 2 LEU B 62 PRO B 63 0 0.67
CISPEP 3 LEU D 62 PRO D 63 0 -0.10
CISPEP 4 LEU E 62 PRO E 63 0 -0.10
CISPEP 5 LEU H 62 PRO H 63 0 -0.07
SITE 1 AC1 4 GLU A 98 CYS A 101 CYS A 104 CYS A 112
SITE 1 AC2 4 CYS A 38 HIS A 68 GLU A 69 CYS A 154
SITE 1 AC3 4 GLU B 98 CYS B 101 CYS B 104 CYS B 112
SITE 1 AC4 4 CYS B 38 HIS B 68 GLU B 69 CYS B 154
SITE 1 AC5 5 GLU C 98 CYS C 101 CYS C 104 CYS C 112
SITE 2 AC5 5 ASP C 113
SITE 1 AC6 4 CYS C 38 HIS C 68 GLU C 69 CYS C 154
SITE 1 AC7 4 GLU D 98 CYS D 101 CYS D 104 CYS D 112
SITE 1 AC8 4 CYS D 38 HIS D 68 GLU D 69 CYS D 154
SITE 1 AC9 4 GLU E 98 CYS E 101 CYS E 104 CYS E 112
SITE 1 BC1 4 CYS E 38 HIS E 68 GLU E 69 CYS E 154
SITE 1 BC2 4 GLU H 98 CYS H 101 CYS H 104 CYS H 112
SITE 1 BC3 4 CYS H 38 HIS H 68 GLU H 69 CYS H 154
CRYST1 215.729 91.545 118.368 90.00 99.20 90.00 C 1 2 1 24
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 0.004635 0.000000 0.000751 0.00000
SCALE2 0.000000 0.010924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008558 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
