HEADER HYDROLASE 01-JUL-11 3SP4
TITLE CRYSTAL STRUCTURE OF APRATAXIN ORTHOLOG HNT3 FROM SCHIZOSACCHAROMYCES
TITLE 2 POMBE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APRATAXIN-LIKE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 33-232;
COMPND 5 SYNONYM: HNT3 PROTEIN, HIT FAMILY PROTEIN 3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 284812;
SOURCE 5 STRAIN: ATCC 38366 / 972;
SOURCE 6 GENE: HNT3, SPCC18.09C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HIT DOMAIN, ZINC FINGER, DNA-BINDING PROTEIN, DNA DEADENYLASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GONG,D.ZHU,J.DING,C.DOU,X.REN,T.JIANG,D.WANG
REVDAT 2 03-JUL-13 3SP4 1 JRNL
REVDAT 1 12-OCT-11 3SP4 0
JRNL AUTH Y.GONG,D.ZHU,J.DING,C.DOU,X.REN,L.GU,T.JIANG,D.WANG
JRNL TITL CRYSTAL STRUCTURES OF APRATAXIN ORTHOLOG HNT3 REVEAL THE
JRNL TITL 2 MECHANISM FOR REVERSAL OF 5'-ADENYLATED DNA
JRNL REF NAT.STRUCT.MOL.BIOL. V. 18 1297 2011
JRNL REFN ISSN 1545-9993
JRNL PMID 21984208
JRNL DOI 10.1038/NSMB.2145
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.030
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 35510
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.430
REMARK 3 FREE R VALUE TEST SET COUNT : 1927
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 37.8648 - 4.3360 0.98 2725 156 0.1696 0.1769
REMARK 3 2 4.3360 - 3.4424 1.00 2630 151 0.1525 0.1807
REMARK 3 3 3.4424 - 3.0074 0.99 2586 149 0.1842 0.2130
REMARK 3 4 3.0074 - 2.7326 0.99 2550 146 0.1927 0.2478
REMARK 3 5 2.7326 - 2.5367 0.98 2524 143 0.1984 0.2233
REMARK 3 6 2.5367 - 2.3872 0.98 2509 144 0.1975 0.2742
REMARK 3 7 2.3872 - 2.2677 0.98 2495 143 0.1995 0.2513
REMARK 3 8 2.2677 - 2.1690 0.97 2490 143 0.2013 0.2611
REMARK 3 9 2.1690 - 2.0855 0.97 2458 145 0.1995 0.2533
REMARK 3 10 2.0855 - 2.0135 0.95 2431 138 0.1991 0.2592
REMARK 3 11 2.0135 - 1.9506 0.92 2323 130 0.2063 0.2911
REMARK 3 12 1.9506 - 1.8948 0.84 2124 123 0.2153 0.2660
REMARK 3 13 1.8948 - 1.8449 0.76 1941 110 0.2055 0.2904
REMARK 3 14 1.8449 - 1.7999 0.71 1797 106 0.2109 0.2759
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 : 0.32
REMARK 3 B_SOL : 32.44
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.030
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.25470
REMARK 3 B22 (A**2) : 11.20020
REMARK 3 B33 (A**2) : -9.94550
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 : 0.006 3453
REMARK 3 ANGLE : 0.975 4677
REMARK 3 CHIRALITY : 0.070 514
REMARK 3 PLANARITY : 0.004 591
REMARK 3 DIHEDRAL : 16.603 1280
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3SP4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB066477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36873
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.34700
REMARK 200 R SYM FOR SHELL (I) : 0.34700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 42.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M TRIS-HCL, PH8.0,
REMARK 280 0.1M LI2SO4 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.58850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.90450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.10050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.90450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.58850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.10050
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 29
REMARK 465 SER A 30
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 120 -85.87 -109.06
REMARK 500 PRO A 141 153.78 -45.55
REMARK 500 LEU B 120 -71.94 -112.75
REMARK 500 PRO B 141 150.43 -40.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 396 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH B 346 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH B 388 DISTANCE = 7.00 ANGSTROMS
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 B 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 221 OE2
REMARK 620 2 HIS B 217 NE2 107.3
REMARK 620 3 CYS B 203 SG 104.7 104.9
REMARK 620 4 CYS B 200 SG 111.2 109.1 119.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 221 OE2
REMARK 620 2 HIS A 217 NE2 104.4
REMARK 620 3 CYS A 203 SG 107.0 109.9
REMARK 620 4 CYS A 200 SG 113.6 105.7 115.5
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SPD RELATED DB: PDB
REMARK 900 THE HNT3 IN COMPLEX WITH DNA
REMARK 900 RELATED ID: 3SPL RELATED DB: PDB
REMARK 900 THE HNT3 IN COMPLEX WITH DNA AND AMP
DBREF 3SP4 A 33 232 UNP O74859 APTX_SCHPO 33 232
DBREF 3SP4 B 33 232 UNP O74859 APTX_SCHPO 33 232
SEQADV 3SP4 GLY A 29 UNP O74859 EXPRESSION TAG
SEQADV 3SP4 SER A 30 UNP O74859 EXPRESSION TAG
SEQADV 3SP4 HIS A 31 UNP O74859 EXPRESSION TAG
SEQADV 3SP4 MET A 32 UNP O74859 EXPRESSION TAG
SEQADV 3SP4 GLY B 29 UNP O74859 EXPRESSION TAG
SEQADV 3SP4 SER B 30 UNP O74859 EXPRESSION TAG
SEQADV 3SP4 HIS B 31 UNP O74859 EXPRESSION TAG
SEQADV 3SP4 MET B 32 UNP O74859 EXPRESSION TAG
SEQRES 1 A 204 GLY SER HIS MET SER PHE ARG ASP ASN LEU LYS VAL TYR
SEQRES 2 A 204 ILE GLU SER PRO GLU SER TYR LYS ASN VAL ILE TYR TYR
SEQRES 3 A 204 ASP ASP ASP VAL VAL LEU VAL ARG ASP MET PHE PRO LYS
SEQRES 4 A 204 SER LYS MET HIS LEU LEU LEU MET THR ARG ASP PRO HIS
SEQRES 5 A 204 LEU THR HIS VAL HIS PRO LEU GLU ILE MET MET LYS HIS
SEQRES 6 A 204 ARG SER LEU VAL GLU LYS LEU VAL SER TYR VAL GLN GLY
SEQRES 7 A 204 ASP LEU SER GLY LEU ILE PHE ASP GLU ALA ARG ASN CYS
SEQRES 8 A 204 LEU SER GLN GLN LEU THR ASN GLU ALA LEU CYS ASN TYR
SEQRES 9 A 204 ILE LYS VAL GLY PHE HIS ALA GLY PRO SER MET ASN ASN
SEQRES 10 A 204 LEU HIS LEU HIS ILE MET THR LEU ASP HIS VAL SER PRO
SEQRES 11 A 204 SER LEU LYS ASN SER ALA HIS TYR ILE SER PHE THR SER
SEQRES 12 A 204 PRO PHE PHE VAL LYS ILE ASP THR PRO THR SER ASN LEU
SEQRES 13 A 204 PRO THR ARG GLY THR LEU THR SER LEU PHE GLN GLU ASP
SEQRES 14 A 204 LEU LYS CYS TRP ARG CYS GLY GLU THR PHE GLY ARG HIS
SEQRES 15 A 204 PHE THR LYS LEU LYS ALA HIS LEU GLN GLU GLU TYR ASP
SEQRES 16 A 204 ASP TRP LEU ASP LYS SER VAL SER MET
SEQRES 1 B 204 GLY SER HIS MET SER PHE ARG ASP ASN LEU LYS VAL TYR
SEQRES 2 B 204 ILE GLU SER PRO GLU SER TYR LYS ASN VAL ILE TYR TYR
SEQRES 3 B 204 ASP ASP ASP VAL VAL LEU VAL ARG ASP MET PHE PRO LYS
SEQRES 4 B 204 SER LYS MET HIS LEU LEU LEU MET THR ARG ASP PRO HIS
SEQRES 5 B 204 LEU THR HIS VAL HIS PRO LEU GLU ILE MET MET LYS HIS
SEQRES 6 B 204 ARG SER LEU VAL GLU LYS LEU VAL SER TYR VAL GLN GLY
SEQRES 7 B 204 ASP LEU SER GLY LEU ILE PHE ASP GLU ALA ARG ASN CYS
SEQRES 8 B 204 LEU SER GLN GLN LEU THR ASN GLU ALA LEU CYS ASN TYR
SEQRES 9 B 204 ILE LYS VAL GLY PHE HIS ALA GLY PRO SER MET ASN ASN
SEQRES 10 B 204 LEU HIS LEU HIS ILE MET THR LEU ASP HIS VAL SER PRO
SEQRES 11 B 204 SER LEU LYS ASN SER ALA HIS TYR ILE SER PHE THR SER
SEQRES 12 B 204 PRO PHE PHE VAL LYS ILE ASP THR PRO THR SER ASN LEU
SEQRES 13 B 204 PRO THR ARG GLY THR LEU THR SER LEU PHE GLN GLU ASP
SEQRES 14 B 204 LEU LYS CYS TRP ARG CYS GLY GLU THR PHE GLY ARG HIS
SEQRES 15 B 204 PHE THR LYS LEU LYS ALA HIS LEU GLN GLU GLU TYR ASP
SEQRES 16 B 204 ASP TRP LEU ASP LYS SER VAL SER MET
HET ZN A 601 1
HET SO4 A 701 5
HET ZN B 601 1
HET SO4 B 701 5
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *406(H2 O)
HELIX 1 1 SER A 33 ASN A 37 5 5
HELIX 2 2 LEU A 38 SER A 44 1 7
HELIX 3 3 PRO A 45 TYR A 48 5 4
HELIX 4 4 HIS A 85 HIS A 93 1 9
HELIX 5 5 HIS A 93 GLY A 106 1 14
HELIX 6 6 LEU A 108 LEU A 120 1 13
HELIX 7 7 THR A 125 ASN A 131 1 7
HELIX 8 8 ASN A 162 SER A 171 1 10
HELIX 9 9 PRO A 180 LEU A 184 5 5
HELIX 10 10 THR A 186 GLU A 196 5 11
HELIX 11 11 HIS A 210 VAL A 230 1 21
HELIX 12 12 LEU B 38 SER B 44 1 7
HELIX 13 13 PRO B 45 TYR B 48 5 4
HELIX 14 14 HIS B 85 HIS B 93 1 9
HELIX 15 15 HIS B 93 GLY B 106 1 14
HELIX 16 16 LEU B 108 LEU B 120 1 13
HELIX 17 17 THR B 125 ASN B 131 1 7
HELIX 18 18 ASN B 162 SER B 171 1 10
HELIX 19 19 PRO B 180 LEU B 184 5 5
HELIX 20 20 THR B 186 LEU B 193 1 8
HELIX 21 21 PHE B 194 GLU B 196 5 3
HELIX 22 22 HIS B 210 VAL B 230 1 21
SHEET 1 A 6 VAL A 51 TYR A 54 0
SHEET 2 A 6 VAL A 58 ARG A 62 -1 O LEU A 60 N TYR A 53
SHEET 3 A 6 HIS A 71 THR A 76 -1 O LEU A 73 N VAL A 61
SHEET 4 A 6 LEU A 148 THR A 152 -1 O ILE A 150 N LEU A 72
SHEET 5 A 6 ILE A 133 HIS A 138 -1 N LYS A 134 O MET A 151
SHEET 6 A 6 PHE A 174 LYS A 176 -1 O VAL A 175 N PHE A 137
SHEET 1 B 6 VAL B 51 TYR B 54 0
SHEET 2 B 6 VAL B 58 ARG B 62 -1 O LEU B 60 N TYR B 53
SHEET 3 B 6 HIS B 71 THR B 76 -1 O MET B 75 N VAL B 59
SHEET 4 B 6 LEU B 148 THR B 152 -1 O ILE B 150 N LEU B 72
SHEET 5 B 6 ILE B 133 HIS B 138 -1 N LYS B 134 O MET B 151
SHEET 6 B 6 PHE B 174 LYS B 176 -1 O VAL B 175 N PHE B 137
SSBOND 1 CYS A 130 CYS B 130 1555 1555 2.04
LINK OE2 GLU B 221 ZN ZN B 601 1555 1555 1.93
LINK OE2 GLU A 221 ZN ZN A 601 1555 1555 2.05
LINK NE2 HIS B 217 ZN ZN B 601 1555 1555 2.10
LINK NE2 HIS A 217 ZN ZN A 601 1555 1555 2.10
LINK SG CYS B 203 ZN ZN B 601 1555 1555 2.30
LINK SG CYS A 203 ZN ZN A 601 1555 1555 2.31
LINK SG CYS B 200 ZN ZN B 601 1555 1555 2.33
LINK SG CYS A 200 ZN ZN A 601 1555 1555 2.35
SITE 1 AC1 4 CYS A 200 CYS A 203 HIS A 217 GLU A 221
SITE 1 AC2 5 HIS A 85 ALA A 139 GLY A 140 THR B 186
SITE 2 AC2 5 HOH B 248
SITE 1 AC3 4 CYS B 200 CYS B 203 HIS B 217 GLU B 221
SITE 1 AC4 7 HIS A 210 PHE A 211 THR A 212 SER B 121
SITE 2 AC4 7 GLN B 122 GLN B 123 HOH B 440
CRYST1 53.177 70.201 107.809 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018805 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014245 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009276 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
