HEADER HYDROLASE 22-JUN-11 3SKD
TITLE CRYSTAL STRUCTURE OF THE THERMUS THERMOPHILUS CAS3 HD DOMAIN IN THE
TITLE 2 PRESENCE OF NI2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN TTHB187;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: TTHB187;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: T7EXPRESS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHAT2
KEYWDS CRISPR, CAS, HD DOMAIN, NUCLEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BAILEY,S.MULEPATI
REVDAT 5 28-FEB-24 3SKD 1 REMARK SEQADV LINK
REVDAT 4 19-OCT-11 3SKD 1 JRNL
REVDAT 3 10-AUG-11 3SKD 1 JRNL
REVDAT 2 27-JUL-11 3SKD 1 REMARK
REVDAT 1 20-JUL-11 3SKD 0
JRNL AUTH S.MULEPATI,S.BAILEY
JRNL TITL STRUCTURAL AND BIOCHEMICAL ANALYSIS OF NUCLEASE DOMAIN OF
JRNL TITL 2 CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEAT
JRNL TITL 3 (CRISPR)-ASSOCIATED PROTEIN 3 (CAS3).
JRNL REF J.BIOL.CHEM. V. 286 31896 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21775431
JRNL DOI 10.1074/JBC.M111.270017
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6_288
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1638
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 35.3670 - 4.5759 1.00 2534 118 0.1905 0.2296
REMARK 3 2 4.5759 - 3.6332 1.00 2541 117 0.1544 0.1674
REMARK 3 3 3.6332 - 3.1742 1.00 2545 130 0.1557 0.1933
REMARK 3 4 3.1742 - 2.8842 1.00 2484 134 0.1690 0.2201
REMARK 3 5 2.8842 - 2.6775 1.00 2506 155 0.1621 0.1625
REMARK 3 6 2.6775 - 2.5197 1.00 2500 161 0.1628 0.2296
REMARK 3 7 2.5197 - 2.3935 1.00 2518 149 0.1615 0.1740
REMARK 3 8 2.3935 - 2.2894 1.00 2515 132 0.1822 0.2167
REMARK 3 9 2.2894 - 2.2013 1.00 2518 115 0.1903 0.2562
REMARK 3 10 2.2013 - 2.1253 1.00 2526 143 0.2004 0.1781
REMARK 3 11 2.1253 - 2.0589 1.00 2532 140 0.2016 0.2830
REMARK 3 12 2.0589 - 2.0000 1.00 2502 144 0.2399 0.3076
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 : 0.44
REMARK 3 B_SOL : 43.48
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.49720
REMARK 3 B22 (A**2) : -3.49720
REMARK 3 B33 (A**2) : 6.99440
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 : 0.016 1887
REMARK 3 ANGLE : 1.483 2565
REMARK 3 CHIRALITY : 0.085 267
REMARK 3 PLANARITY : 0.008 336
REMARK 3 DIHEDRAL : 14.998 687
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4349 40.1225 16.4270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1473 T22: 0.1310
REMARK 3 T33: 0.1256 T12: -0.0117
REMARK 3 T13: -0.0159 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 1.0641 L22: 0.4100
REMARK 3 L33: 0.5309 L12: 0.2371
REMARK 3 L13: 0.0481 L23: 0.3504
REMARK 3 S TENSOR
REMARK 3 S11: 0.0158 S12: 0.0026 S13: -0.0618
REMARK 3 S21: 0.0429 S22: -0.0144 S23: 0.0010
REMARK 3 S31: 0.0520 S32: -0.0121 S33: -0.0000
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 3SKD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066309.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17751
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.998
REMARK 200 RESOLUTION RANGE LOW (A) : 35.362
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 11.50
REMARK 200 R MERGE FOR SHELL (I) : 0.70500
REMARK 200 R SYM FOR SHELL (I) : 0.70500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, PH 4.2, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 103.00550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 154.50825
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.50275
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 103.00550
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 51.50275
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 154.50825
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 340 LIES ON A SPECIAL POSITION.
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 MET A -4
REMARK 465 SER A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 GLY A 81
REMARK 465 TRP A 82
REMARK 465 GLU A 83
REMARK 465 GLU A 84
REMARK 465 GLY A 85
REMARK 465 LYS A 86
REMARK 465 GLU A 87
REMARK 465 ARG A 88
REMARK 465 VAL A 89
REMARK 465 GLN A 90
REMARK 465 ARG A 91
REMARK 465 ALA A 92
REMARK 465 GLY A 93
REMARK 465 LEU A 94
REMARK 465 PRO A 95
REMARK 465 PHE A 96
REMARK 465 GLY A 97
REMARK 465 GLU A 98
REMARK 465 LEU A 99
REMARK 465 LEU A 100
REMARK 465 ASP A 101
REMARK 465 SER A 183
REMARK 465 GLN A 184
REMARK 465 GLY A 185
REMARK 465 ASN A 186
REMARK 465 GLY A 187
REMARK 465 GLU A 188
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 175 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 16 144.24 -173.07
REMARK 500 PHE A 245 -70.97 -108.04
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 NI A 261 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 24 NE2
REMARK 620 2 HIS A 69 NE2 95.6
REMARK 620 3 ASP A 70 OD2 91.0 88.3
REMARK 620 4 ASP A 205 OD1 93.2 82.5 170.2
REMARK 620 5 HOH A 262 O 84.7 168.0 103.7 85.6
REMARK 620 6 HOH A 344 O 172.1 91.8 86.6 90.4 88.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 261
DBREF 3SKD A 6 260 UNP Q53VY2 Q53VY2_THET8 6 260
SEQADV 3SKD MET A -4 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD SER A -3 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD HIS A -2 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD HIS A -1 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD HIS A 0 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD HIS A 1 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD HIS A 2 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD HIS A 3 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD SER A 4 UNP Q53VY2 EXPRESSION TAG
SEQADV 3SKD MET A 5 UNP Q53VY2 EXPRESSION TAG
SEQRES 1 A 265 MET SER HIS HIS HIS HIS HIS HIS SER MET ALA ALA LEU
SEQRES 2 A 265 ALA LEU TRP ALA LYS SER GLY ASN PRO PHE HIS PRO LEU
SEQRES 3 A 265 LEU ALA HIS MET LEU ASP THR ALA ALA VAL ALA LEU ALA
SEQRES 4 A 265 VAL LEU ARG MET GLU PRO PRO ARG THR ARG ALA LEU TYR
SEQRES 5 A 265 ALA GLU ASP TRP GLY LEU PRO GLU GLU GLY ALA LEU ALA
SEQRES 6 A 265 TRP ALA ALA ALA LEU VAL GLY LEU HIS ASP LEU GLY LYS
SEQRES 7 A 265 ALA SER PRO VAL PHE GLN ALA GLY TRP GLU GLU GLY LYS
SEQRES 8 A 265 GLU ARG VAL GLN ARG ALA GLY LEU PRO PHE GLY GLU LEU
SEQRES 9 A 265 LEU ASP TRP VAL ALA HIS GLY VAL PHE THR GLU LEU PHE
SEQRES 10 A 265 LEU ARG ARG LEU LEU LYS GLU LYS GLY LEU PRO GLU ARG
SEQRES 11 A 265 ALA ALA ASN ASP LEU ALA ALA ALA LEU GLY ALA HIS HIS
SEQRES 12 A 265 GLY PHE PRO ALA ASN ALA GLU GLU LYS SER ARG ALA ARG
SEQRES 13 A 265 ARG HIS LEU ARG THR GLU ASP PRO LEU TRP LYS GLU ALA
SEQRES 14 A 265 ARG ARG TRP LEU LEU GLU GLU VAL PHE ARG ARG LEU GLY
SEQRES 15 A 265 ALA PRO LEU PRO PRO SER GLN GLY ASN GLY GLU ALA ARG
SEQRES 16 A 265 PRO GLU ALA VAL LEU ARG VAL MET ALA LEU ALA SER PHE
SEQRES 17 A 265 ALA ASP TRP VAL ALA SER ASP PRO SER LEU PHE PRO TYR
SEQRES 18 A 265 GLY ARG ASP PRO ARG ARG GLY ASP TYR LEU LYS GLU ALA
SEQRES 19 A 265 LEU ARG LEU ALA GLN GLU ALA LEU ASN ARG LEU GLY TRP
SEQRES 20 A 265 PRO ALA PHE ALA LYS ALA GLN ARG ARG GLU PHE GLY GLU
SEQRES 21 A 265 LEU PHE PRO TYR ILE
HET NI A 261 1
HETNAM NI NICKEL (II) ION
FORMUL 2 NI NI 2+
FORMUL 3 HOH *108(H2 O)
HELIX 1 1 SER A 4 ALA A 12 1 9
HELIX 2 2 PRO A 20 GLU A 39 1 20
HELIX 3 3 PRO A 40 GLY A 52 1 13
HELIX 4 4 PRO A 54 LEU A 68 1 15
HELIX 5 5 HIS A 69 ALA A 74 5 6
HELIX 6 6 SER A 75 GLN A 79 5 5
HELIX 7 7 ALA A 104 LYS A 120 1 17
HELIX 8 8 PRO A 123 LEU A 134 1 12
HELIX 9 9 ASN A 143 GLU A 157 1 15
HELIX 10 10 PRO A 159 GLY A 177 1 19
HELIX 11 11 ARG A 190 SER A 209 1 20
HELIX 12 12 ASP A 224 TRP A 242 1 19
SHEET 1 A 2 ALA A 248 GLU A 252 0
SHEET 2 A 2 GLU A 255 TYR A 259 -1 O TYR A 259 N ALA A 248
LINK NE2 HIS A 24 NI NI A 261 1555 1555 2.31
LINK NE2 HIS A 69 NI NI A 261 1555 1555 2.26
LINK OD2 ASP A 70 NI NI A 261 1555 1555 2.00
LINK OD1 ASP A 205 NI NI A 261 1555 1555 2.23
LINK NI NI A 261 O HOH A 262 1555 1555 1.98
LINK NI NI A 261 O HOH A 344 1555 1555 2.36
SITE 1 AC1 6 HIS A 24 HIS A 69 ASP A 70 ASP A 205
SITE 2 AC1 6 HOH A 262 HOH A 344
CRYST1 48.638 48.638 206.011 90.00 90.00 90.00 P 43 2 2 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 0.020560 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004854 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
