HEADER PROTEIN BINDING 08-AUG-17 5Y59
TITLE CRYSTAL STRUCTURE OF KU80 AND SIR4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT DNA HELICASE II SUBUNIT 2;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: VWA DOMAIN, UNP RESIDUES 2-200;
COMPND 5 SYNONYM: ATP-DEPENDENT DNA HELICASE II SUBUNIT KU80,HIGH AFFINITY
COMPND 6 DNA-BINDING FACTOR SUBUNIT 2,YEAST KU80;
COMPND 7 EC: 3.6.4.12;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: SIR4P;
COMPND 11 CHAIN: C;
COMPND 12 FRAGMENT: KU BINDING MOTIF, UNP RESIDUES 104-115;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: YKU80, HDF2, YMR106C, YM9718.05C;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 15 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 16 ORGANISM_TAXID: 764100;
SOURCE 17 STRAIN: ZYMAFLORE VL3;
SOURCE 18 GENE: VL3_0944;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 21 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS TELOMERASE, TELOMERE, PROTEIN-PROTEIN COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR H.CHEN,J.XUE,J.WU,M.LEI
REVDAT 3 27-MAR-24 5Y59 1 REMARK
REVDAT 2 07-FEB-18 5Y59 1 JRNL
REVDAT 1 20-DEC-17 5Y59 0
JRNL AUTH H.CHEN,J.XUE,D.CHURIKOV,E.P.HASS,S.SHI,L.D.LEMON,P.LUCIANO,
JRNL AUTH 2 A.A.BERTUCH,D.C.ZAPPULLA,V.GELI,J.WU,M.LEI
JRNL TITL STRUCTURAL INSIGHTS INTO YEAST TELOMERASE RECRUITMENT TO
JRNL TITL 2 TELOMERES
JRNL REF CELL V. 172 331 2018
JRNL REFN ISSN 1097-4172
JRNL PMID 29290466
JRNL DOI 10.1016/J.CELL.2017.12.008
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 10957
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400
REMARK 3 FREE R VALUE TEST SET COUNT : 592
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 27.6438 - 3.8106 0.99 2950 171 0.1806 0.2234
REMARK 3 2 3.8106 - 3.0258 1.00 2889 152 0.2082 0.2473
REMARK 3 3 3.0258 - 2.6436 1.00 2838 161 0.2288 0.2812
REMARK 3 4 2.6436 - 2.4021 0.60 1688 108 0.2399 0.3198
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.010 1614
REMARK 3 ANGLE : 1.306 2178
REMARK 3 CHIRALITY : 0.064 265
REMARK 3 PLANARITY : 0.004 270
REMARK 3 DIHEDRAL : 14.323 610
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0297 19.5094 -10.3744
REMARK 3 T TENSOR
REMARK 3 T11: 0.2956 T22: 0.2879
REMARK 3 T33: 0.2707 T12: 0.0534
REMARK 3 T13: -0.0042 T23: -0.1254
REMARK 3 L TENSOR
REMARK 3 L11: 4.7665 L22: 3.2004
REMARK 3 L33: 7.0860 L12: 0.2482
REMARK 3 L13: -1.0613 L23: -0.7979
REMARK 3 S TENSOR
REMARK 3 S11: -0.0664 S12: 0.7438 S13: -0.3052
REMARK 3 S21: -0.2863 S22: 0.0240 S23: 0.0569
REMARK 3 S31: 1.0447 S32: 0.0024 S33: -0.0072
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8352 12.3659 -24.2123
REMARK 3 T TENSOR
REMARK 3 T11: 1.1272 T22: 1.1962
REMARK 3 T33: 0.8262 T12: 0.2334
REMARK 3 T13: 0.3262 T23: -0.5397
REMARK 3 L TENSOR
REMARK 3 L11: 6.7633 L22: 4.3891
REMARK 3 L33: 4.7056 L12: -1.1101
REMARK 3 L13: -0.1381 L23: 0.0254
REMARK 3 S TENSOR
REMARK 3 S11: -0.2583 S12: 0.4879 S13: -0.7157
REMARK 3 S21: 0.1321 S22: 0.3552 S23: -0.6571
REMARK 3 S31: 1.5709 S32: 0.8041 S33: 0.9229
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 5Y59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004695.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-16; 17-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SSRF; SSRF
REMARK 200 BEAMLINE : BL18U1; BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97851; 0.97851
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL; PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M; DECTRIS
REMARK 200 PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12169
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 18.00
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 11.40
REMARK 200 R MERGE FOR SHELL (I) : 0.88800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 2.0 M AMMONIUM SULFATE,
REMARK 280 PH 7.5, EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.64200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.28400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 55.28400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.64200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 THR B 143
REMARK 465 ASP B 144
REMARK 465 ASP B 166
REMARK 465 THR B 167
REMARK 465 GLN B 168
REMARK 465 GLU B 169
REMARK 465 GLU B 170
REMARK 465 ARG B 171
REMARK 465 LYS B 172
REMARK 465 LYS B 173
REMARK 465 SER B 200
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 GLN B 122 -139.11 57.67
REMARK 500 ASP B 141 95.99 -66.65
REMARK 500 CYS B 163 49.40 -107.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5Y58 RELATED DB: PDB
DBREF 5Y59 B 2 200 UNP Q04437 KU80_YEAST 2 200
DBREF 5Y59 C 104 115 UNP E7QD18 E7QD18_YEASZ 104 115
SEQRES 1 B 199 SER SER GLU SER THR THR PHE ILE VAL ASP VAL SER PRO
SEQRES 2 B 199 SER MET MET LYS ASN ASN ASN VAL SER LYS SER MET ALA
SEQRES 3 B 199 TYR LEU GLU TYR THR LEU LEU ASN LYS SER LYS LYS SER
SEQRES 4 B 199 ARG LYS THR ASP TRP ILE SER CYS TYR LEU ALA ASN CYS
SEQRES 5 B 199 PRO VAL SER GLU ASN SER GLN GLU ILE PRO ASN VAL PHE
SEQRES 6 B 199 GLN ILE GLN SER PHE LEU ALA PRO VAL THR THR THR ALA
SEQRES 7 B 199 THR ILE GLY PHE ILE LYS ARG LEU LYS GLN TYR CYS ASP
SEQRES 8 B 199 GLN HIS SER HIS ASP SER SER ASN GLU GLY LEU GLN SER
SEQRES 9 B 199 MET ILE GLN CYS LEU LEU VAL VAL SER LEU ASP ILE LYS
SEQRES 10 B 199 GLN GLN PHE GLN ALA ARG LYS ILE LEU LYS GLN ILE VAL
SEQRES 11 B 199 VAL PHE THR ASP ASN LEU ASP ASP LEU ASP ILE THR ASP
SEQRES 12 B 199 GLU GLU ILE ASP LEU LEU THR GLU GLU LEU SER THR ARG
SEQRES 13 B 199 ILE ILE LEU ILE ASP CYS GLY LYS ASP THR GLN GLU GLU
SEQRES 14 B 199 ARG LYS LYS SER ASN TRP LEU LYS LEU VAL GLU ALA ILE
SEQRES 15 B 199 PRO ASN SER ARG ILE TYR ASN MET ASN GLU LEU LEU VAL
SEQRES 16 B 199 GLU ILE THR SER
SEQRES 1 C 12 ASN SER LYS LEU LEU SER LEU LEU ARG SER LYS THR
HET SO4 B 301 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *35(H2 O)
HELIX 1 AA1 SER B 13 ASN B 19 1 7
HELIX 2 AA2 ASN B 20 ASN B 35 1 16
HELIX 3 AA3 SER B 37 LYS B 42 1 6
HELIX 4 AA4 THR B 76 SER B 95 1 20
HELIX 5 AA5 SER B 105 GLN B 122 1 18
HELIX 6 AA6 GLU B 146 LEU B 154 1 9
HELIX 7 AA7 ASN B 175 ILE B 183 1 9
HELIX 8 AA8 ASN B 192 LEU B 194 5 3
HELIX 9 AA9 SER C 105 THR C 115 1 11
SHEET 1 AA1 6 PHE B 66 LEU B 72 0
SHEET 2 AA1 6 TRP B 45 ALA B 51 -1 N ILE B 46 O LEU B 72
SHEET 3 AA1 6 GLU B 4 ASP B 11 1 N PHE B 8 O SER B 47
SHEET 4 AA1 6 LEU B 127 THR B 134 1 O LEU B 127 N SER B 5
SHEET 5 AA1 6 ARG B 157 ASP B 162 1 O ILE B 161 N VAL B 132
SHEET 6 AA1 6 ARG B 187 ASN B 190 1 O TYR B 189 N ASP B 162
CISPEP 1 ALA B 73 PRO B 74 0 5.66
SITE 1 AC1 4 ARG B 41 THR B 76 THR B 77 HOH B 419
CRYST1 79.472 79.472 82.926 90.00 90.00 120.00 P 31 2 1 6
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 0.012583 0.007265 0.000000 0.00000
SCALE2 0.000000 0.014530 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
