HEADER TRANSCRIPTION 29-JUN-10 2XIG
TITLE THE STRUCTURE OF THE HELICOBACTER PYLORI FERRIC UPTAKE
TITLE 2 REGULATOR FUR REVEALS THREE FUNCTIONAL METAL BINDING SITES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERRIC UPTAKE REGULATION PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: FERRIC UPTAKE REGULATOR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_TAXID: 85962;
SOURCE 4 STRAIN: 26695;
SOURCE 5 ATCC: 43504;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET11A
KEYWDS HPFUR, TRANSCRIPTION, HOMEOSTASIS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DIAN,S.VITALE,G.A.LEONARD,F.FAUQUANT,C.MULLER,C.BAHLAWANE,
AUTHOR 2 H.DE REUSE,I.MICHAUD-SORET,L.TERRADOT
REVDAT 2 06-APR-11 2XIG 1 JRNL
REVDAT 1 19-JAN-11 2XIG 0
JRNL AUTH C.DIAN,S.VITALE,G.A.LEONARD,C.BAHLAWANE,C.FAUQUANT,D.LEDUC,
JRNL AUTH 2 C.MULLER,H.DE REUSE,I.MICHAUD-SORET,L.TERRADOT
JRNL TITL THE STRUCTURE OF THE HELICOBACTER PYLORI FERRIC UPTAKE
JRNL TITL 2 REGULATOR FUR REVEALS THREE FUNCTIONAL METAL BINDING SITES.
JRNL REF MOL.MICROBIOL. V. 79 1260 2011
JRNL REFN ISSN 0950-382X
JRNL PMID 21208302
JRNL DOI 10.1111/J.1365-2958.2010.07517.X
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.850
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.097
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.96
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.40
REMARK 3 NUMBER OF REFLECTIONS : 99642
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1999
REMARK 3 R VALUE (WORKING SET) : 0.1981
REMARK 3 FREE R VALUE : 0.2339
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 5032
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 35.1029 - 3.9840 0.89 9129 445 0.1724 0.1864
REMARK 3 2 3.9840 - 3.1628 0.92 9350 533 0.1698 0.2028
REMARK 3 3 3.1628 - 2.7632 0.93 9503 578 0.1951 0.2292
REMARK 3 4 2.7632 - 2.5107 0.93 9519 495 0.2054 0.2689
REMARK 3 5 2.5107 - 2.3307 0.93 9569 486 0.2102 0.2292
REMARK 3 6 2.3307 - 2.1934 0.93 9482 487 0.2094 0.2717
REMARK 3 7 2.1934 - 2.0835 0.93 9586 502 0.2169 0.2714
REMARK 3 8 2.0835 - 1.9928 0.93 9534 435 0.2210 0.2610
REMARK 3 9 1.9928 - 1.9161 0.93 9541 517 0.2474 0.3075
REMARK 3 10 1.9161 - 1.8500 0.93 9397 554 0.2821 0.3119
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.386
REMARK 3 B_SOL : 59.921
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.21
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.3609
REMARK 3 B22 (A**2) : 4.5069
REMARK 3 B33 (A**2) : -9.8678
REMARK 3 B12 (A**2) : 3.9897
REMARK 3 B13 (A**2) : -2.2187
REMARK 3 B23 (A**2) : -2.4059
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 4888
REMARK 3 ANGLE : 0.870 6564
REMARK 3 CHIRALITY : 0.061 733
REMARK 3 PLANARITY : 0.003 843
REMARK 3 DIHEDRAL : 17.233 1870
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9312 1.9482 61.3133
REMARK 3 T TENSOR
REMARK 3 T11: 0.1625 T22: 0.1835
REMARK 3 T33: 0.1326 T12: 0.0168
REMARK 3 T13: -0.0233 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.2804 L22: 0.7015
REMARK 3 L33: 0.9156 L12: 0.2716
REMARK 3 L13: 0.2208 L23: -0.0112
REMARK 3 S TENSOR
REMARK 3 S11: 0.1085 S12: 0.0553 S13: 0.0170
REMARK 3 S21: 0.0681 S22: -0.0016 S23: -0.0027
REMARK 3 S31: 0.1686 S32: 0.1168 S33: -0.0959
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN C OR CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7169 3.7810 31.1190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1346 T22: 0.1069
REMARK 3 T33: 0.1159 T12: 0.0203
REMARK 3 T13: 0.0146 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.4660 L22: 0.3443
REMARK 3 L33: 0.5683 L12: 0.0270
REMARK 3 L13: 0.1011 L23: 0.0622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0450 S12: 0.0109 S13: 0.0039
REMARK 3 S21: -0.0394 S22: 0.0370 S23: -0.0190
REMARK 3 S31: 0.1382 S32: 0.1003 S33: -0.0640
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2XIG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-10.
REMARK 100 THE PDBE ID CODE IS EBI-44398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC (QUANTUM 315R)
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51362
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.85
REMARK 200 RESOLUTION RANGE LOW (A) : 47.96
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 4.1
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.1
REMARK 200 R MERGE FOR SHELL (I) : 0.39
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: ZN-SAD MODEL AT 2.15A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HPFUR2M PRE-LOADED WITH ZINC
REMARK 280 (2 EQ) AT 30 MG/ML WAS CRYSTALLIZED FROM 20% PEG 3350,
REMARK 280 100 MM NA CITRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 9140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.7 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.5 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 350
REMARK 350 BIOMOLECULE: 3
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: 2930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 78 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 78 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 78 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 78 TO SER
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 LEU A 23
REMARK 465 LYS A 24
REMARK 465 GLU A 149
REMARK 465 SER A 150
REMARK 465 GLU B 149
REMARK 465 SER B 150
REMARK 465 GLU D 149
REMARK 465 SER D 150
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 2 CG CD CE NZ
REMARK 470 ILE A 18 CG1 CG2 CD1
REMARK 470 LYS A 19 CG CD CE NZ
REMARK 470 ASN A 25 CG OD1 ND2
REMARK 470 LYS A 27 CD CE NZ
REMARK 470 GLU A 46 CD OE1 OE2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 LYS A 73 CE NZ
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 LYS A 125 CG CD CE NZ
REMARK 470 LYS B 2 CG CD CE NZ
REMARK 470 LYS B 19 CG CD CE NZ
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 SER B 78 OG
REMARK 470 LYS B 84 CG CD CE NZ
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 LYS C 2 CG CD CE NZ
REMARK 470 LYS C 24 CG CD CE NZ
REMARK 470 LYS C 27 CD CE NZ
REMARK 470 LYS C 55 CG CD CE NZ
REMARK 470 LYS D 19 CG CD CE NZ
REMARK 470 LYS D 24 CE NZ
REMARK 470 LYS D 27 CG CD CE NZ
REMARK 470 LYS D 55 CG CD CE NZ
REMARK 470 LYS D 84 CG CD CE NZ
REMARK 470 LYS D 125 CG CD CE NZ
REMARK 470 LYS D 126 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 SER B 83 -157.17 -144.18
REMARK 500 THR C 41 -164.38 -129.76
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 A1149 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 98 OD1
REMARK 620 2 HIS A 134 NE2 93.7
REMARK 620 3 ASP A 98 OD2 53.8 140.0
REMARK 620 4 HIS A 96 NE2 91.2 94.8 107.1
REMARK 620 5 GLU A 117 OE2 144.8 116.6 91.1 103.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1149 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 145 SG
REMARK 620 2 CYS D 102 SG 113.2
REMARK 620 3 CYS D 105 SG 106.8 107.6
REMARK 620 4 CYS D 142 SG 102.8 111.2 115.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1150 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 90 OE1
REMARK 620 2 HIS A 99 NE2 98.1
REMARK 620 3 HIS A 42 NE2 103.5 101.4
REMARK 620 4 GLU A 90 OE2 55.4 153.5 88.0
REMARK 620 5 HIS A 97 NE2 104.5 91.4 147.1 93.8
REMARK 620 6 GLU A 110 OE2 135.0 126.8 73.1 79.6 75.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1150 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 90 OE1
REMARK 620 2 GLU B 90 OE2 57.3
REMARK 620 3 HIS B 42 NE2 85.4 98.6
REMARK 620 4 HIS B 97 NE2 89.3 122.9 125.7
REMARK 620 5 HIS B 99 NE2 153.0 96.4 106.1 102.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1150 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 98 OD1
REMARK 620 2 ASP D 98 OD2 53.7
REMARK 620 3 GLU D 117 OE2 142.0 89.2
REMARK 620 4 HIS D 134 NE2 85.4 126.7 116.6
REMARK 620 5 HIS D 96 NE2 91.7 113.4 113.2 98.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1151 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 145 SG
REMARK 620 2 CYS A 102 SG 109.8
REMARK 620 3 CYS A 142 SG 107.7 112.9
REMARK 620 4 CYS A 105 SG 104.4 106.7 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1151 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 96 NE2
REMARK 620 2 ASP B 98 OD1 112.3
REMARK 620 3 ASP B 98 OD2 94.0 53.2
REMARK 620 4 GLU B 117 OE1 105.5 87.0 140.1
REMARK 620 5 HIS B 134 NE2 97.2 131.1 88.0 122.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1151 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 42 NE2
REMARK 620 2 GLU C 90 OE1 87.3
REMARK 620 3 GLU C 90 OE2 98.9 55.7
REMARK 620 4 HIS C 97 NE2 141.4 88.2 109.8
REMARK 620 5 HIS C 99 NE2 99.5 160.3 104.8 97.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1151 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 99 NE2
REMARK 620 2 GLU D 90 OE2 107.2
REMARK 620 3 HIS D 97 NE2 98.9 118.7
REMARK 620 4 HIS D 42 NE2 100.8 100.6 127.7
REMARK 620 5 GLU D 90 OE1 162.7 55.5 89.6 85.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1152 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 142 SG
REMARK 620 2 CYS B 102 SG 103.2
REMARK 620 3 CYS B 105 SG 118.5 113.0
REMARK 620 4 CYS B 145 SG 103.0 115.8 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1152 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 105 SG
REMARK 620 2 CYS C 142 SG 112.3
REMARK 620 3 CYS C 102 SG 109.6 109.6
REMARK 620 4 CYS C 145 SG 104.3 108.6 112.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 98 OD2
REMARK 620 2 HIS C 96 NE2 109.7
REMARK 620 3 GLU C 117 OE2 87.9 106.4
REMARK 620 4 ASP C 98 OD1 55.2 92.0 142.9
REMARK 620 5 HIS C 134 NE2 135.7 98.7 116.3 91.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C1152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C1153
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1151
DBREF 2XIG A 1 150 UNP O25671 FUR_HELPY 1 150
DBREF 2XIG B 1 150 UNP O25671 FUR_HELPY 1 150
DBREF 2XIG C 1 150 UNP O25671 FUR_HELPY 1 150
DBREF 2XIG D 1 150 UNP O25671 FUR_HELPY 1 150
SEQADV 2XIG SER A 78 UNP O25671 CYS 78 ENGINEERED MUTATION
SEQADV 2XIG SER A 150 UNP O25671 CYS 150 ENGINEERED MUTATION
SEQADV 2XIG SER B 78 UNP O25671 CYS 78 ENGINEERED MUTATION
SEQADV 2XIG SER B 150 UNP O25671 CYS 150 ENGINEERED MUTATION
SEQADV 2XIG SER C 78 UNP O25671 CYS 78 ENGINEERED MUTATION
SEQADV 2XIG SER C 150 UNP O25671 CYS 150 ENGINEERED MUTATION
SEQADV 2XIG SER D 78 UNP O25671 CYS 78 ENGINEERED MUTATION
SEQADV 2XIG SER D 150 UNP O25671 CYS 150 ENGINEERED MUTATION
SEQRES 1 A 150 MET LYS ARG LEU GLU THR LEU GLU SER ILE LEU GLU ARG
SEQRES 2 A 150 LEU ARG MET SER ILE LYS LYS ASN GLY LEU LYS ASN SER
SEQRES 3 A 150 LYS GLN ARG GLU GLU VAL VAL SER VAL LEU TYR ARG SER
SEQRES 4 A 150 GLY THR HIS LEU SER PRO GLU GLU ILE THR HIS SER ILE
SEQRES 5 A 150 ARG GLN LYS ASP LYS ASN THR SER ILE SER SER VAL TYR
SEQRES 6 A 150 ARG ILE LEU ASN PHE LEU GLU LYS GLU ASN PHE ILE SER
SEQRES 7 A 150 VAL LEU GLU THR SER LYS SER GLY ARG ARG TYR GLU ILE
SEQRES 8 A 150 ALA ALA LYS GLU HIS HIS ASP HIS ILE ILE CYS LEU HIS
SEQRES 9 A 150 CYS GLY LYS ILE ILE GLU PHE ALA ASP PRO GLU ILE GLU
SEQRES 10 A 150 ASN ARG GLN ASN GLU VAL VAL LYS LYS TYR GLN ALA LYS
SEQRES 11 A 150 LEU ILE SER HIS ASP MET LYS MET PHE VAL TRP CYS LYS
SEQRES 12 A 150 GLU CYS GLN GLU SER GLU SER
SEQRES 1 B 150 MET LYS ARG LEU GLU THR LEU GLU SER ILE LEU GLU ARG
SEQRES 2 B 150 LEU ARG MET SER ILE LYS LYS ASN GLY LEU LYS ASN SER
SEQRES 3 B 150 LYS GLN ARG GLU GLU VAL VAL SER VAL LEU TYR ARG SER
SEQRES 4 B 150 GLY THR HIS LEU SER PRO GLU GLU ILE THR HIS SER ILE
SEQRES 5 B 150 ARG GLN LYS ASP LYS ASN THR SER ILE SER SER VAL TYR
SEQRES 6 B 150 ARG ILE LEU ASN PHE LEU GLU LYS GLU ASN PHE ILE SER
SEQRES 7 B 150 VAL LEU GLU THR SER LYS SER GLY ARG ARG TYR GLU ILE
SEQRES 8 B 150 ALA ALA LYS GLU HIS HIS ASP HIS ILE ILE CYS LEU HIS
SEQRES 9 B 150 CYS GLY LYS ILE ILE GLU PHE ALA ASP PRO GLU ILE GLU
SEQRES 10 B 150 ASN ARG GLN ASN GLU VAL VAL LYS LYS TYR GLN ALA LYS
SEQRES 11 B 150 LEU ILE SER HIS ASP MET LYS MET PHE VAL TRP CYS LYS
SEQRES 12 B 150 GLU CYS GLN GLU SER GLU SER
SEQRES 1 C 150 MET LYS ARG LEU GLU THR LEU GLU SER ILE LEU GLU ARG
SEQRES 2 C 150 LEU ARG MET SER ILE LYS LYS ASN GLY LEU LYS ASN SER
SEQRES 3 C 150 LYS GLN ARG GLU GLU VAL VAL SER VAL LEU TYR ARG SER
SEQRES 4 C 150 GLY THR HIS LEU SER PRO GLU GLU ILE THR HIS SER ILE
SEQRES 5 C 150 ARG GLN LYS ASP LYS ASN THR SER ILE SER SER VAL TYR
SEQRES 6 C 150 ARG ILE LEU ASN PHE LEU GLU LYS GLU ASN PHE ILE SER
SEQRES 7 C 150 VAL LEU GLU THR SER LYS SER GLY ARG ARG TYR GLU ILE
SEQRES 8 C 150 ALA ALA LYS GLU HIS HIS ASP HIS ILE ILE CYS LEU HIS
SEQRES 9 C 150 CYS GLY LYS ILE ILE GLU PHE ALA ASP PRO GLU ILE GLU
SEQRES 10 C 150 ASN ARG GLN ASN GLU VAL VAL LYS LYS TYR GLN ALA LYS
SEQRES 11 C 150 LEU ILE SER HIS ASP MET LYS MET PHE VAL TRP CYS LYS
SEQRES 12 C 150 GLU CYS GLN GLU SER GLU SER
SEQRES 1 D 150 MET LYS ARG LEU GLU THR LEU GLU SER ILE LEU GLU ARG
SEQRES 2 D 150 LEU ARG MET SER ILE LYS LYS ASN GLY LEU LYS ASN SER
SEQRES 3 D 150 LYS GLN ARG GLU GLU VAL VAL SER VAL LEU TYR ARG SER
SEQRES 4 D 150 GLY THR HIS LEU SER PRO GLU GLU ILE THR HIS SER ILE
SEQRES 5 D 150 ARG GLN LYS ASP LYS ASN THR SER ILE SER SER VAL TYR
SEQRES 6 D 150 ARG ILE LEU ASN PHE LEU GLU LYS GLU ASN PHE ILE SER
SEQRES 7 D 150 VAL LEU GLU THR SER LYS SER GLY ARG ARG TYR GLU ILE
SEQRES 8 D 150 ALA ALA LYS GLU HIS HIS ASP HIS ILE ILE CYS LEU HIS
SEQRES 9 D 150 CYS GLY LYS ILE ILE GLU PHE ALA ASP PRO GLU ILE GLU
SEQRES 10 D 150 ASN ARG GLN ASN GLU VAL VAL LYS LYS TYR GLN ALA LYS
SEQRES 11 D 150 LEU ILE SER HIS ASP MET LYS MET PHE VAL TRP CYS LYS
SEQRES 12 D 150 GLU CYS GLN GLU SER GLU SER
HET CIT B1149 13
HET ZN A1149 1
HET ZN B1150 1
HET ZN C1151 1
HET ZN A1150 1
HET ZN B1151 1
HET ZN C1152 1
HET ZN B1152 1
HET ZN D1149 1
HET ZN C1153 1
HET ZN D1150 1
HET ZN D1151 1
HET ZN A1151 1
HETNAM CIT CITRIC ACID
HETNAM ZN ZINC ION
FORMUL 5 CIT C6 H8 O7
FORMUL 6 ZN 12(ZN 2+)
FORMUL 7 HOH *377(H2 O)
HELIX 1 1 THR A 6 ASN A 21 1 16
HELIX 2 2 ASN A 25 SER A 39 1 15
HELIX 3 3 SER A 44 ASP A 56 1 13
HELIX 4 4 SER A 60 GLU A 74 1 15
HELIX 5 5 ASP A 113 LYS A 126 1 14
HELIX 6 6 CYS A 142 GLU A 147 1 6
HELIX 7 7 THR B 6 GLY B 22 1 17
HELIX 8 8 ASN B 25 GLY B 40 1 16
HELIX 9 9 SER B 44 GLN B 54 1 11
HELIX 10 10 SER B 60 GLU B 74 1 15
HELIX 11 11 ASP B 113 LYS B 126 1 14
HELIX 12 12 CYS B 142 SER B 148 1 7
HELIX 13 13 THR C 6 ASN C 21 1 16
HELIX 14 14 SER C 26 SER C 39 1 14
HELIX 15 15 SER C 44 ARG C 53 1 10
HELIX 16 16 SER C 60 GLU C 74 1 15
HELIX 17 17 ASP C 113 TYR C 127 1 15
HELIX 18 18 CYS C 142 GLU C 147 1 6
HELIX 19 19 THR D 6 ASN D 21 1 16
HELIX 20 20 SER D 26 SER D 39 1 14
HELIX 21 21 SER D 44 ARG D 53 1 10
HELIX 22 22 SER D 60 GLU D 74 1 15
HELIX 23 23 ASP D 113 TYR D 127 1 15
HELIX 24 24 CYS D 142 SER D 148 1 7
SHEET 1 AA 2 ILE A 77 THR A 82 0
SHEET 2 AA 2 GLY A 86 ILE A 91 -1 O GLY A 86 N THR A 82
SHEET 1 AB 6 ILE A 108 PHE A 111 0
SHEET 2 AB 6 ASP A 98 CYS A 102 -1 O ASP A 98 N PHE A 111
SHEET 3 AB 6 LYS A 130 TRP A 141 1 O MET A 136 N HIS A 99
SHEET 4 AB 6 LYS B 130 TRP B 141 -1 O LYS B 130 N TRP A 141
SHEET 5 AB 6 ASP B 98 CYS B 102 1 O HIS B 99 N MET B 138
SHEET 6 AB 6 ILE B 108 PHE B 111 -1 O ILE B 109 N ILE B 100
SHEET 1 BA 2 ILE B 77 GLU B 81 0
SHEET 2 BA 2 ARG B 87 ILE B 91 -1 O ARG B 88 N LEU B 80
SHEET 1 CA 2 ILE C 77 THR C 82 0
SHEET 2 CA 2 GLY C 86 ILE C 91 -1 O GLY C 86 N THR C 82
SHEET 1 CB 6 ILE C 108 PHE C 111 0
SHEET 2 CB 6 ASP C 98 CYS C 102 -1 O ASP C 98 N PHE C 111
SHEET 3 CB 6 LYS C 130 TRP C 141 1 O MET C 136 N HIS C 99
SHEET 4 CB 6 LYS D 130 TRP D 141 -1 O LYS D 130 N TRP C 141
SHEET 5 CB 6 ASP D 98 CYS D 102 1 O HIS D 99 N MET D 138
SHEET 6 CB 6 ILE D 108 PHE D 111 -1 O ILE D 109 N ILE D 100
SHEET 1 DA 2 ILE D 77 GLU D 81 0
SHEET 2 DA 2 ARG D 87 ILE D 91 -1 O ARG D 88 N LEU D 80
LINK ZN ZN A1149 OD1 ASP A 98 1555 1555 2.62
LINK ZN ZN A1149 NE2 HIS A 134 1555 1555 2.14
LINK ZN ZN A1149 OD2 ASP A 98 1555 1555 2.12
LINK ZN ZN A1149 NE2 HIS A 96 1555 1555 2.08
LINK ZN ZN A1149 OE2 GLU A 117 1555 1555 2.15
LINK ZN ZN A1150 OE1 GLU A 90 1555 1555 2.26
LINK ZN ZN A1150 NE2 HIS A 99 1555 1555 2.19
LINK ZN ZN A1150 NE2 HIS A 42 1555 1555 2.14
LINK ZN ZN A1150 OE2 GLU A 90 1555 1555 2.46
LINK ZN ZN A1150 NE2 HIS A 97 1555 1555 2.16
LINK ZN ZN A1150 OE2 GLU A 110 1555 1555 2.64
LINK ZN ZN A1151 SG CYS A 145 1555 1555 2.35
LINK ZN ZN A1151 SG CYS A 102 1555 1555 2.38
LINK ZN ZN A1151 SG CYS A 142 1555 1555 2.37
LINK ZN ZN A1151 SG CYS A 105 1555 1555 2.31
LINK ZN ZN B1150 OE1 GLU B 90 1555 1555 2.44
LINK ZN ZN B1150 OE2 GLU B 90 1555 1555 2.13
LINK ZN ZN B1150 NE2 HIS B 42 1555 1555 2.10
LINK ZN ZN B1150 NE2 HIS B 97 1555 1555 2.11
LINK ZN ZN B1150 NE2 HIS B 99 1555 1555 2.21
LINK ZN ZN B1151 NE2 HIS B 96 1555 1555 2.11
LINK ZN ZN B1151 OD1 ASP B 98 1555 1555 2.17
LINK ZN ZN B1151 OD2 ASP B 98 1555 1555 2.66
LINK ZN ZN B1151 OE1 GLU B 117 1555 1555 2.11
LINK ZN ZN B1151 NE2 HIS B 134 1555 1555 2.11
LINK ZN ZN B1152 SG CYS B 102 1555 1555 2.33
LINK ZN ZN B1152 SG CYS B 142 1555 1555 2.18
LINK ZN ZN B1152 SG CYS B 145 1555 1555 2.40
LINK ZN ZN B1152 SG CYS B 105 1555 1555 2.41
LINK ZN ZN C1151 OE2 GLU C 90 1555 1555 2.04
LINK ZN ZN C1151 OE1 GLU C 90 1555 1555 2.57
LINK ZN ZN C1151 NE2 HIS C 97 1555 1555 2.10
LINK ZN ZN C1151 NE2 HIS C 99 1555 1555 2.10
LINK ZN ZN C1151 NE2 HIS C 42 1555 1555 2.18
LINK ZN ZN C1152 SG CYS C 105 1555 1555 2.33
LINK ZN ZN C1152 SG CYS C 142 1555 1555 2.45
LINK ZN ZN C1152 SG CYS C 102 1555 1555 2.38
LINK ZN ZN C1152 SG CYS C 145 1555 1555 2.38
LINK ZN ZN C1153 NE2 HIS C 134 1555 1555 2.04
LINK ZN ZN C1153 OD1 ASP C 98 1555 1555 2.53
LINK ZN ZN C1153 OE2 GLU C 117 1555 1555 2.02
LINK ZN ZN C1153 NE2 HIS C 96 1555 1555 2.14
LINK ZN ZN C1153 OD2 ASP C 98 1555 1555 2.14
LINK ZN ZN D1149 SG CYS D 145 1555 1555 2.39
LINK ZN ZN D1149 SG CYS D 142 1555 1555 2.37
LINK ZN ZN D1149 SG CYS D 105 1555 1555 2.28
LINK ZN ZN D1149 SG CYS D 102 1555 1555 2.42
LINK ZN ZN D1150 NE2 HIS D 96 1555 1555 2.06
LINK ZN ZN D1150 NE2 HIS D 134 1555 1555 2.12
LINK ZN ZN D1150 OE2 GLU D 117 1555 1555 2.10
LINK ZN ZN D1150 OD2 ASP D 98 1555 1555 2.09
LINK ZN ZN D1150 OD1 ASP D 98 1555 1555 2.66
LINK ZN ZN D1151 OE1 GLU D 90 1555 1555 2.54
LINK ZN ZN D1151 NE2 HIS D 42 1555 1555 2.05
LINK ZN ZN D1151 NE2 HIS D 97 1555 1555 2.08
LINK ZN ZN D1151 OE2 GLU D 90 1555 1555 2.09
LINK ZN ZN D1151 NE2 HIS D 99 1555 1555 2.10
SITE 1 AC1 8 LEU B 23 LYS B 24 ASN B 25 ARG B 29
SITE 2 AC1 8 ARG B 66 HOH B2054 ARG D 66 ASN D 69
SITE 1 AC2 4 HIS A 96 ASP A 98 GLU A 117 HIS A 134
SITE 1 AC3 4 HIS B 42 GLU B 90 HIS B 97 HIS B 99
SITE 1 AC4 4 HIS C 42 GLU C 90 HIS C 97 HIS C 99
SITE 1 AC5 5 HIS A 42 GLU A 90 HIS A 97 HIS A 99
SITE 2 AC5 5 GLU A 110
SITE 1 AC6 4 HIS B 96 ASP B 98 GLU B 117 HIS B 134
SITE 1 AC7 4 CYS C 102 CYS C 105 CYS C 142 CYS C 145
SITE 1 AC8 4 CYS B 102 CYS B 105 CYS B 142 CYS B 145
SITE 1 AC9 4 CYS D 102 CYS D 105 CYS D 142 CYS D 145
SITE 1 BC1 4 HIS C 96 ASP C 98 GLU C 117 HIS C 134
SITE 1 BC2 4 HIS D 96 ASP D 98 GLU D 117 HIS D 134
SITE 1 BC3 4 HIS D 42 GLU D 90 HIS D 97 HIS D 99
SITE 1 BC4 4 CYS A 102 CYS A 105 CYS A 142 CYS A 145
CRYST1 48.150 48.290 72.250 83.32 77.82 87.65 P 1 4
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 0.020768 -0.000852 -0.004416 0.00000
SCALE2 0.000000 0.020726 -0.002299 0.00000
SCALE3 0.000000 0.000000 0.014246 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
