HEADER HYDROLASE/HYDROLASE INHIBITOR 29-DEC-09 3L85
TITLE CRYSTAL STRUCTURE OF HUMAN NUDT5 COMPLEXED WITH 8-OXO-DGMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-SUGAR PYROPHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 14-208;
COMPND 5 SYNONYM: NUDT5, NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF 5, NUDIX
COMPND 6 MOTIF 5, YSA1H;
COMPND 7 EC: 3.6.1.13;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NUDT5, HSPC115;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B(+)
KEYWDS NUDIX MOTIF, MAGNESIUM, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ARIMORI,Y.YAMAGATA
REVDAT 4 01-NOV-23 3L85 1 REMARK
REVDAT 3 05-JUN-13 3L85 1 JRNL
REVDAT 2 09-NOV-11 3L85 1 JRNL VERSN HEADER
REVDAT 1 12-JAN-11 3L85 0
JRNL AUTH T.ARIMORI,H.TAMAOKI,T.NAKAMURA,H.KAMIYA,S.IKEMIZU,Y.TAKAGI,
JRNL AUTH 2 T.ISHIBASHI,H.HARASHIMA,M.SEKIGUCHI,Y.YAMAGATA
JRNL TITL DIVERSE SUBSTRATE RECOGNITION AND HYDROLYSIS MECHANISMS OF
JRNL TITL 2 HUMAN NUDT5
JRNL REF NUCLEIC ACIDS RES. V. 39 8972 2011
JRNL REFN ISSN 0305-1048
JRNL PMID 21768126
JRNL DOI 10.1093/NAR/GKR575
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 3 NUMBER OF REFLECTIONS : 14057
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 706
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 45.5320 - 3.9340 0.97 3221 178 0.1820 0.2160
REMARK 3 2 3.9340 - 3.1220 0.96 3121 150 0.2030 0.2390
REMARK 3 3 3.1220 - 2.7280 0.89 2840 144 0.2490 0.3400
REMARK 3 4 2.7280 - 2.4780 0.75 2369 137 0.2840 0.3630
REMARK 3 5 2.4780 - 2.3010 0.57 1800 97 0.2980 0.3270
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 : 0.39
REMARK 3 B_SOL : 43.47
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 2.040
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.84900
REMARK 3 B22 (A**2) : 7.77400
REMARK 3 B33 (A**2) : 2.07500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.18400
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 : 0.003 3132
REMARK 3 ANGLE : 0.621 4263
REMARK 3 CHIRALITY : 0.038 485
REMARK 3 PLANARITY : 0.002 550
REMARK 3 DIHEDRAL : 15.677 1165
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 3L85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000056953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15339
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 90.8
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.42600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2DSC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 0.8M NAH2PO4/1.2M
REMARK 280 K2HPO4 , PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 56.32750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.00400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.32750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.00400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 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 20 77.02 -119.54
REMARK 500 THR A 53 33.31 -89.22
REMARK 500 ASP A 133 73.80 -166.31
REMARK 500 PRO A 158 107.80 -56.19
REMARK 500 ASP A 177 30.60 -161.08
REMARK 500 HIS A 190 15.35 53.55
REMARK 500 TRP B 46 121.99 -171.18
REMARK 500 THR B 53 20.85 -75.00
REMARK 500 GLN B 57 -168.09 -116.03
REMARK 500 ASP B 133 78.26 -156.90
REMARK 500 LEU B 136 -62.07 -124.48
REMARK 500 ALA B 156 -72.87 -52.55
REMARK 500 LYS B 161 77.48 -112.44
REMARK 500 ASP B 164 98.89 -65.01
REMARK 500 ASP B 177 26.06 -142.47
REMARK 500 LEU B 191 134.13 -176.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 8OG A 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8OG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8OG A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AC9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH 8-OXO-DGDP AND MANGANESE
REMARK 900 RELATED ID: 3ACA RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH 8-OXO-DADP AND MANGANESE
DBREF 3L85 A 14 208 UNP Q9UKK9 NUDT5_HUMAN 14 208
DBREF 3L85 B 14 208 UNP Q9UKK9 NUDT5_HUMAN 14 208
SEQRES 1 A 195 LYS GLN TYR ILE ILE SER GLU GLU LEU ILE SER GLU GLY
SEQRES 2 A 195 LYS TRP VAL LYS LEU GLU LYS THR THR TYR MET ASP PRO
SEQRES 3 A 195 THR GLY LYS THR ARG THR TRP GLU SER VAL LYS ARG THR
SEQRES 4 A 195 THR ARG LYS GLU GLN THR ALA ASP GLY VAL ALA VAL ILE
SEQRES 5 A 195 PRO VAL LEU GLN ARG THR LEU HIS TYR GLU CYS ILE VAL
SEQRES 6 A 195 LEU VAL LYS GLN PHE ARG PRO PRO MET GLY GLY TYR CYS
SEQRES 7 A 195 ILE GLU PHE PRO ALA GLY LEU ILE ASP ASP GLY GLU THR
SEQRES 8 A 195 PRO GLU ALA ALA ALA LEU ARG GLU LEU GLU GLU GLU THR
SEQRES 9 A 195 GLY TYR LYS GLY ASP ILE ALA GLU CYS SER PRO ALA VAL
SEQRES 10 A 195 CYS MET ASP PRO GLY LEU SER ASN CYS THR ILE HIS ILE
SEQRES 11 A 195 VAL THR VAL THR ILE ASN GLY ASP ASP ALA GLU ASN ALA
SEQRES 12 A 195 ARG PRO LYS PRO LYS PRO GLY ASP GLY GLU PHE VAL GLU
SEQRES 13 A 195 VAL ILE SER LEU PRO LYS ASN ASP LEU LEU GLN ARG LEU
SEQRES 14 A 195 ASP ALA LEU VAL ALA GLU GLU HIS LEU THR VAL ASP ALA
SEQRES 15 A 195 ARG VAL TYR SER TYR ALA LEU ALA LEU LYS HIS ALA ASN
SEQRES 1 B 195 LYS GLN TYR ILE ILE SER GLU GLU LEU ILE SER GLU GLY
SEQRES 2 B 195 LYS TRP VAL LYS LEU GLU LYS THR THR TYR MET ASP PRO
SEQRES 3 B 195 THR GLY LYS THR ARG THR TRP GLU SER VAL LYS ARG THR
SEQRES 4 B 195 THR ARG LYS GLU GLN THR ALA ASP GLY VAL ALA VAL ILE
SEQRES 5 B 195 PRO VAL LEU GLN ARG THR LEU HIS TYR GLU CYS ILE VAL
SEQRES 6 B 195 LEU VAL LYS GLN PHE ARG PRO PRO MET GLY GLY TYR CYS
SEQRES 7 B 195 ILE GLU PHE PRO ALA GLY LEU ILE ASP ASP GLY GLU THR
SEQRES 8 B 195 PRO GLU ALA ALA ALA LEU ARG GLU LEU GLU GLU GLU THR
SEQRES 9 B 195 GLY TYR LYS GLY ASP ILE ALA GLU CYS SER PRO ALA VAL
SEQRES 10 B 195 CYS MET ASP PRO GLY LEU SER ASN CYS THR ILE HIS ILE
SEQRES 11 B 195 VAL THR VAL THR ILE ASN GLY ASP ASP ALA GLU ASN ALA
SEQRES 12 B 195 ARG PRO LYS PRO LYS PRO GLY ASP GLY GLU PHE VAL GLU
SEQRES 13 B 195 VAL ILE SER LEU PRO LYS ASN ASP LEU LEU GLN ARG LEU
SEQRES 14 B 195 ASP ALA LEU VAL ALA GLU GLU HIS LEU THR VAL ASP ALA
SEQRES 15 B 195 ARG VAL TYR SER TYR ALA LEU ALA LEU LYS HIS ALA ASN
HET 8OG A 1 24
HET 8OG A 2 13
HETNAM 8OG 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETSYN 8OG 8-OXO-7,8-DIHYDRO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
FORMUL 3 8OG 2(C10 H14 N5 O8 P)
FORMUL 5 HOH *75(H2 O)
HELIX 1 1 PRO A 85 GLY A 88 5 4
HELIX 2 2 THR A 104 GLY A 118 1 15
HELIX 3 3 ASP A 152 ALA A 156 5 5
HELIX 4 4 ASP A 177 GLU A 189 1 13
HELIX 5 5 ALA A 195 ASN A 208 1 14
HELIX 6 6 PRO B 85 GLY B 88 5 4
HELIX 7 7 THR B 104 THR B 117 1 14
HELIX 8 8 ASP B 152 ALA B 156 5 5
HELIX 9 9 ASP B 177 GLU B 189 1 13
HELIX 10 10 ASP B 194 ASN B 208 1 15
SHEET 1 A 3 TYR A 16 GLU A 25 0
SHEET 2 A 3 VAL A 29 MET A 37 -1 O THR A 35 N ILE A 18
SHEET 3 A 3 THR A 43 ARG A 51 -1 O TRP A 46 N THR A 34
SHEET 1 B 9 ASP A 122 CYS A 131 0
SHEET 2 B 9 THR A 140 ASN A 149 -1 O THR A 145 N ALA A 124
SHEET 3 B 9 GLY A 61 GLN A 69 1 N GLN A 69 O ILE A 148
SHEET 4 B 9 CYS A 76 ARG A 84 -1 O CYS A 76 N LEU A 68
SHEET 5 B 9 GLY A 89 GLU A 93 -1 O GLY A 89 N ARG A 84
SHEET 6 B 9 THR A 192 ASP A 194 1 O ASP A 194 N ILE A 92
SHEET 7 B 9 VAL B 130 CYS B 131 1 O CYS B 131 N VAL A 193
SHEET 8 B 9 THR B 140 ASN B 149 -1 O ILE B 141 N VAL B 130
SHEET 9 B 9 ASP B 122 CYS B 126 -1 N ASP B 122 O THR B 147
SHEET 1 C 4 ALA A 96 LEU A 98 0
SHEET 2 C 4 GLY A 61 GLN A 69 -1 N VAL A 49 O GLY A 97
SHEET 3 C 4 CYS A 76 ARG A 84 -1 O CYS A 76 N LEU A 68
SHEET 4 C 4 GLU A 169 PRO A 174 -1 O ILE A 171 N LEU A 79
SHEET 1 D 5 ASP B 122 CYS B 126 0
SHEET 2 D 5 THR B 140 ASN B 149 -1 O THR B 147 N ASP B 122
SHEET 3 D 5 GLY B 61 GLN B 69 1 N VAL B 67 O VAL B 146
SHEET 4 D 5 CYS B 76 ARG B 84 -1 O VAL B 78 N PRO B 66
SHEET 5 D 5 GLU B 169 PRO B 174 -1 O LEU B 173 N ILE B 77
SHEET 1 E 5 ALA B 96 LEU B 98 0
SHEET 2 E 5 GLY B 61 GLN B 69 -1 N VAL B 49 O GLY B 97
SHEET 3 E 5 CYS B 76 ARG B 84 -1 O VAL B 78 N PRO B 66
SHEET 4 E 5 GLY B 89 GLU B 93 -1 O GLY B 89 N ARG B 84
SHEET 5 E 5 THR B 192 VAL B 193 1 O THR B 192 N TYR B 90
SHEET 1 F 3 TYR B 16 GLU B 25 0
SHEET 2 F 3 VAL B 29 MET B 37 -1 O LYS B 33 N GLU B 21
SHEET 3 F 3 THR B 43 ARG B 51 -1 O TRP B 46 N THR B 34
SITE 1 AC1 8 TRP A 46 GLU A 47 HOH A 303 TRP B 28
SITE 2 AC1 8 ARG B 51 ARG B 84 ALA B 96 GLY B 97
SITE 1 AC2 4 TRP A 28 THR B 45 TRP B 46 GLU B 47
CRYST1 112.655 40.008 98.470 90.00 121.53 90.00 C 1 2 1 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 0.008877 0.000000 0.005446 0.00000
SCALE2 0.000000 0.024995 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011914 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
