HEADER HYDROLASE 07-NOV-07 3B9X
TITLE CRYSTAL STRUCTURE OF THE E. COLI PYRIMIDINE NUCLEOSIDE HYDROLASE YEIK
TITLE 2 IN COMPLEX WITH INOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIMIDINE-SPECIFIC RIBONUCLEOSIDE HYDROLASE RIHB;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CYTIDINE/URIDINE-SPECIFIC HYDROLASE;
COMPND 5 EC: 3.2.2.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: RIHB, YEIK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS OPEN (ALPHA, BETA) STRUCTURE, NH-FOLD, ENZYME-SUBSTRATE COMPLEX,
KEYWDS 2 PROTEIN-NUCLEOSIDE COMPLEX, GLYCOSIDASE, HYDROLASE, METAL-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR E.IOVANE,M.DEGANO
REVDAT 5 01-NOV-23 3B9X 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 3B9X 1 VERSN
REVDAT 3 24-FEB-09 3B9X 1 VERSN
REVDAT 2 22-APR-08 3B9X 1 JRNL
REVDAT 1 01-APR-08 3B9X 0
JRNL AUTH E.IOVANE,B.GIABBAI,L.MUZZOLINI,V.MATAFORA,A.FORNILI,
JRNL AUTH 2 C.MINICI,F.GIANNESE,M.DEGANO
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE SPECIFICITY IN GROUP I
JRNL TITL 2 NUCLEOSIDE HYDROLASES
JRNL REF BIOCHEMISTRY V. 47 4418 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18361502
JRNL DOI 10.1021/BI702448S
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.GIABBAI,M.DEGANO
REMARK 1 TITL CRYSTAL STRUCTURE TO 1.7 A OF THE ESCHERICHIA COLI
REMARK 1 TITL 2 PYRIMIDINE NUCLEOSIDE HYDROLASE YEIK, A NOVEL CANDIDATE FOR
REMARK 1 TITL 3 CANCER GENE THERAPY
REMARK 1 REF STRUCTURE V. 12 739 2004
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 15130467
REMARK 1 DOI 10.1016/J.STR.2004.03.018
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.DEGANO,S.C.ALMO,J.C.SACCHETTINI,V.L.SCHRAMM
REMARK 1 TITL TRYPANOSOMAL NUCLEOSIDE HYDROLASE. A NOVEL MECHANISM FROM
REMARK 1 TITL 2 THE STRUCTURE WITH A TRANSITION-STATE INHIBITOR
REMARK 1 REF BIOCHEMISTRY V. 37 6277 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9572842
REMARK 1 DOI 10.1021/BI973012E
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 48587
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1560
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3522
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9030
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 91
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.19000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : -1.16000
REMARK 3 B12 (A**2) : 0.54000
REMARK 3 B13 (A**2) : 0.51000
REMARK 3 B23 (A**2) : 0.02000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.447
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.266
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.205
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.481
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9313 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12690 ; 1.473 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1198 ; 6.368 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 362 ;36.082 ;25.221
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1521 ;15.107 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;17.026 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1494 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6947 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4426 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6437 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 415 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.130 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 62 ; 0.303 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.259 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6160 ; 2.516 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9696 ; 3.389 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3585 ; 3.759 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2993 ; 4.728 ; 7.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 77 1
REMARK 3 1 B 3 B 77 1
REMARK 3 1 C 3 C 77 1
REMARK 3 1 D 3 D 77 1
REMARK 3 2 A 239 A 310 1
REMARK 3 2 B 239 B 310 1
REMARK 3 2 C 239 C 309 1
REMARK 3 2 D 239 D 310 1
REMARK 3 3 A 221 A 238 4
REMARK 3 3 B 221 B 238 4
REMARK 3 3 C 237 C 238 4
REMARK 3 3 D 221 D 238 4
REMARK 3 4 A 201 A 220 1
REMARK 3 4 B 201 B 220 1
REMARK 3 4 C 201 C 218 1
REMARK 3 4 D 201 D 220 1
REMARK 3 5 A 78 A 101 6
REMARK 3 5 B 78 B 101 6
REMARK 3 5 C 78 C 101 6
REMARK 3 5 D 78 D 101 6
REMARK 3 6 A 102 A 174 1
REMARK 3 6 B 102 B 174 1
REMARK 3 6 C 102 C 174 1
REMARK 3 6 D 102 D 174 1
REMARK 3 7 A 176 A 199 1
REMARK 3 7 B 176 B 199 1
REMARK 3 7 C 176 C 199 1
REMARK 3 7 D 176 D 199 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1940 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1940 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1940 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1940 ; 0.05 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 14 ; 0.32 ; 0.20
REMARK 3 MEDIUM POSITIONAL 1 B (A): 14 ; 0.20 ; 0.20
REMARK 3 MEDIUM POSITIONAL 1 C (A): 14 ; 0.32 ; 0.20
REMARK 3 MEDIUM POSITIONAL 1 D (A): 14 ; 0.13 ; 0.20
REMARK 3 LOOSE POSITIONAL 1 A (A): 132 ; 0.37 ; 0.20
REMARK 3 LOOSE POSITIONAL 1 B (A): 132 ; 0.31 ; 0.20
REMARK 3 LOOSE POSITIONAL 1 C (A): 132 ; 0.40 ; 0.20
REMARK 3 LOOSE POSITIONAL 1 D (A): 132 ; 0.41 ; 0.20
REMARK 3 TIGHT THERMAL 1 A (A**2): 1940 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1940 ; 0.18 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1940 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1940 ; 0.18 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 14 ; 3.77 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 14 ; 1.34 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 14 ; 1.76 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 14 ; 1.22 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 132 ; 11.33 ; 25.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 132 ; 5.85 ; 25.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 132 ; 12.33 ; 25.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 132 ; 5.10 ; 25.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3B9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50148
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
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) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.25500
REMARK 200 R SYM FOR SHELL (I) : 0.23500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1Q8F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.2M NACL, 24% PEG
REMARK 280 4000, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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
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: 9910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 THR A 312
REMARK 465 HIS A 313
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASP B 79
REMARK 465 ASN B 80
REMARK 465 ILE B 81
REMARK 465 HIS B 82
REMARK 465 GLY B 83
REMARK 465 LYS B 311
REMARK 465 THR B 312
REMARK 465 HIS B 313
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ASP C 79
REMARK 465 ASN C 80
REMARK 465 ILE C 81
REMARK 465 HIS C 82
REMARK 465 GLY C 83
REMARK 465 ASP C 84
REMARK 465 ILE C 219
REMARK 465 MET C 220
REMARK 465 ASN C 221
REMARK 465 PHE C 222
REMARK 465 THR C 223
REMARK 465 LEU C 224
REMARK 465 LYS C 225
REMARK 465 THR C 226
REMARK 465 GLN C 227
REMARK 465 PHE C 228
REMARK 465 GLU C 229
REMARK 465 ASN C 230
REMARK 465 TYR C 231
REMARK 465 GLY C 232
REMARK 465 LEU C 233
REMARK 465 ALA C 234
REMARK 465 GLY C 235
REMARK 465 GLY C 236
REMARK 465 ILE C 310
REMARK 465 LYS C 311
REMARK 465 THR C 312
REMARK 465 HIS C 313
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 ASP D 79
REMARK 465 ASN D 80
REMARK 465 THR D 312
REMARK 465 HIS D 313
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU B 257 O HOH B 471 2.09
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 60 77.40 -103.52
REMARK 500 MET A 72 -47.78 -136.05
REMARK 500 LEU A 87 50.92 -151.44
REMARK 500 ALA A 153 126.21 -177.47
REMARK 500 ASP A 170 80.25 -155.95
REMARK 500 THR A 195 39.87 -94.85
REMARK 500 VAL A 238 56.58 -99.14
REMARK 500 ASN A 249 100.67 -161.52
REMARK 500 ASN B 60 78.06 -102.29
REMARK 500 MET B 72 -44.52 -134.76
REMARK 500 LEU B 87 48.87 -155.23
REMARK 500 GLU B 93 171.65 -54.23
REMARK 500 ALA B 153 128.99 -171.07
REMARK 500 ASP B 170 77.50 -159.43
REMARK 500 THR B 195 44.20 -97.84
REMARK 500 VAL B 238 73.98 -113.70
REMARK 500 ASN B 249 97.00 -162.27
REMARK 500 MET C 72 -40.40 -144.01
REMARK 500 LEU C 87 57.18 -152.22
REMARK 500 ASP C 170 79.67 -159.86
REMARK 500 THR C 195 45.58 -94.65
REMARK 500 PRO C 199 -37.67 -39.66
REMARK 500 ASN C 249 97.38 -160.80
REMARK 500 ASP C 294 94.10 -69.10
REMARK 500 ASN D 60 79.52 -106.42
REMARK 500 MET D 72 -47.20 -141.01
REMARK 500 LEU D 87 53.82 -153.09
REMARK 500 ASP D 170 77.25 -161.72
REMARK 500 THR D 195 41.57 -96.84
REMARK 500 THR D 223 26.38 -79.12
REMARK 500 VAL D 238 61.95 -106.54
REMARK 500 ASN D 249 96.46 -162.83
REMARK 500 ILE D 291 -60.02 -108.02
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 CA A 400 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 11 OD1
REMARK 620 2 ASP A 16 OD1 68.5
REMARK 620 3 ASP A 16 OD2 84.1 51.5
REMARK 620 4 VAL A 124 O 90.7 93.3 143.8
REMARK 620 5 ASP A 240 OD2 143.7 75.4 76.9 87.0
REMARK 620 6 NOS A 401 O3' 136.8 143.6 136.1 66.0 74.0
REMARK 620 7 NOS A 401 O2' 112.8 120.6 69.3 143.5 89.1 78.1
REMARK 620 8 HOH A 502 O 74.4 141.2 114.4 98.4 141.7 73.8 64.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 400 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 11 OD1
REMARK 620 2 ASP B 16 OD1 69.2
REMARK 620 3 ASP B 16 OD2 85.2 50.1
REMARK 620 4 VAL B 124 O 90.9 90.0 138.4
REMARK 620 5 ASP B 240 OD2 139.9 71.3 74.4 82.6
REMARK 620 6 NOS B 401 O3' 145.5 135.6 128.5 69.2 67.6
REMARK 620 7 NOS B 401 O2' 134.9 117.0 72.3 131.6 71.0 63.4
REMARK 620 8 HOH B 404 O 80.2 149.1 132.4 87.2 138.5 71.2 86.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 400 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 11 OD1
REMARK 620 2 ASP C 16 OD1 66.5
REMARK 620 3 ASP C 16 OD2 85.9 50.4
REMARK 620 4 VAL C 124 O 85.3 81.7 130.5
REMARK 620 5 ASP C 240 OD2 134.7 70.3 76.9 75.5
REMARK 620 6 NOS C 401 O3' 151.2 131.8 122.8 77.4 62.6
REMARK 620 7 NOS C 401 O2' 137.1 124.5 78.2 134.5 80.0 57.3
REMARK 620 8 HOH C 433 O 78.6 144.5 135.5 89.8 140.4 78.5 85.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 400 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 11 OD1
REMARK 620 2 ASP D 16 OD1 71.4
REMARK 620 3 ASP D 16 OD2 87.7 53.6
REMARK 620 4 VAL D 124 O 90.5 91.9 144.0
REMARK 620 5 ASP D 240 OD2 144.9 74.6 79.1 81.9
REMARK 620 6 NOS D 401 O2' 130.0 127.3 77.3 128.3 78.8
REMARK 620 7 NOS D 401 O3' 137.7 141.0 131.3 67.6 70.0 60.7
REMARK 620 8 HOH D 417 O 71.9 142.8 119.5 93.9 142.6 74.9 74.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NOS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NOS B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NOS C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NOS D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM D 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q8F RELATED DB: PDB
REMARK 900 E.COLI PYRIMIDINE-SPECIFIC NUCLEOSIDE HYDROLASE YEIK BOUND TO
REMARK 900 GLYCEROL
REMARK 900 RELATED ID: 2MAS RELATED DB: PDB
REMARK 900 PROTOZOAN NON-SPECIFIC (IU) NUCLEOSIDE HYDROLASE IN COMPLEX WITH
REMARK 900 TRANSITION STATE INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS FEEL THAT THE CONFLICT REPRESENTS A MUTATION IN
REMARK 999 THE DEPOSITED SEQUENCE.
DBREF 3B9X A 1 313 UNP P33022 RIHB_ECOLI 1 313
DBREF 3B9X B 1 313 UNP P33022 RIHB_ECOLI 1 313
DBREF 3B9X C 1 313 UNP P33022 RIHB_ECOLI 1 313
DBREF 3B9X D 1 313 UNP P33022 RIHB_ECOLI 1 313
SEQADV 3B9X MET A -19 UNP P33022 INITIATING METHIONINE
SEQADV 3B9X GLY A -18 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER A -17 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER A -16 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS A -15 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS A -14 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS A -13 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS A -12 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS A -11 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS A -10 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER A -9 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER A -8 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY A -7 UNP P33022 EXPRESSION TAG
SEQADV 3B9X LEU A -6 UNP P33022 EXPRESSION TAG
SEQADV 3B9X VAL A -5 UNP P33022 EXPRESSION TAG
SEQADV 3B9X PRO A -4 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ARG A -3 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY A -2 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER A -1 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS A 0 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ASP A 84 UNP P33022 GLU 84 SEE REMARK 999
SEQADV 3B9X MET B -19 UNP P33022 INITIATING METHIONINE
SEQADV 3B9X GLY B -18 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER B -17 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER B -16 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS B -15 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS B -14 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS B -13 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS B -12 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS B -11 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS B -10 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER B -9 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER B -8 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY B -7 UNP P33022 EXPRESSION TAG
SEQADV 3B9X LEU B -6 UNP P33022 EXPRESSION TAG
SEQADV 3B9X VAL B -5 UNP P33022 EXPRESSION TAG
SEQADV 3B9X PRO B -4 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ARG B -3 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY B -2 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER B -1 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS B 0 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ASP B 84 UNP P33022 GLU 84 SEE REMARK 999
SEQADV 3B9X MET C -19 UNP P33022 INITIATING METHIONINE
SEQADV 3B9X GLY C -18 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER C -17 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER C -16 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS C -15 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS C -14 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS C -13 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS C -12 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS C -11 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS C -10 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER C -9 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER C -8 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY C -7 UNP P33022 EXPRESSION TAG
SEQADV 3B9X LEU C -6 UNP P33022 EXPRESSION TAG
SEQADV 3B9X VAL C -5 UNP P33022 EXPRESSION TAG
SEQADV 3B9X PRO C -4 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ARG C -3 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY C -2 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER C -1 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS C 0 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ASP C 84 UNP P33022 GLU 84 SEE REMARK 999
SEQADV 3B9X MET D -19 UNP P33022 INITIATING METHIONINE
SEQADV 3B9X GLY D -18 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER D -17 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER D -16 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS D -15 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS D -14 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS D -13 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS D -12 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS D -11 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS D -10 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER D -9 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER D -8 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY D -7 UNP P33022 EXPRESSION TAG
SEQADV 3B9X LEU D -6 UNP P33022 EXPRESSION TAG
SEQADV 3B9X VAL D -5 UNP P33022 EXPRESSION TAG
SEQADV 3B9X PRO D -4 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ARG D -3 UNP P33022 EXPRESSION TAG
SEQADV 3B9X GLY D -2 UNP P33022 EXPRESSION TAG
SEQADV 3B9X SER D -1 UNP P33022 EXPRESSION TAG
SEQADV 3B9X HIS D 0 UNP P33022 EXPRESSION TAG
SEQADV 3B9X ASP D 84 UNP P33022 GLU 84 SEE REMARK 999
SEQRES 1 A 333 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 333 LEU VAL PRO ARG GLY SER HIS MET GLU LYS ARG LYS ILE
SEQRES 3 A 333 ILE LEU ASP CYS ASP PRO GLY HIS ASP ASP ALA ILE ALA
SEQRES 4 A 333 ILE MET MET ALA ALA LYS HIS PRO ALA ILE ASP LEU LEU
SEQRES 5 A 333 GLY ILE THR ILE VAL ALA GLY ASN GLN THR LEU ASP LYS
SEQRES 6 A 333 THR LEU ILE ASN GLY LEU ASN VAL CYS GLN LYS LEU GLU
SEQRES 7 A 333 ILE ASN VAL PRO VAL TYR ALA GLY MET PRO GLN PRO ILE
SEQRES 8 A 333 MET ARG GLN GLN ILE VAL ALA ASP ASN ILE HIS GLY ASP
SEQRES 9 A 333 THR GLY LEU ASP GLY PRO VAL PHE GLU PRO LEU THR ARG
SEQRES 10 A 333 GLN ALA GLU SER THR HIS ALA VAL LYS TYR ILE ILE ASP
SEQRES 11 A 333 THR LEU MET ALA SER ASP GLY ASP ILE THR LEU VAL PRO
SEQRES 12 A 333 VAL GLY PRO LEU SER ASN ILE ALA VAL ALA MET ARG MET
SEQRES 13 A 333 GLN PRO ALA ILE LEU PRO LYS ILE ARG GLU ILE VAL LEU
SEQRES 14 A 333 MET GLY GLY ALA TYR GLY THR GLY ASN PHE THR PRO SER
SEQRES 15 A 333 ALA GLU PHE ASN ILE PHE ALA ASP PRO GLU ALA ALA ARG
SEQRES 16 A 333 VAL VAL PHE THR SER GLY VAL PRO LEU VAL MET MET GLY
SEQRES 17 A 333 LEU ASP LEU THR ASN GLN THR VAL CYS THR PRO ASP VAL
SEQRES 18 A 333 ILE ALA ARG MET GLU ARG ALA GLY GLY PRO ALA GLY GLU
SEQRES 19 A 333 LEU PHE SER ASP ILE MET ASN PHE THR LEU LYS THR GLN
SEQRES 20 A 333 PHE GLU ASN TYR GLY LEU ALA GLY GLY PRO VAL HIS ASP
SEQRES 21 A 333 ALA THR CYS ILE GLY TYR LEU ILE ASN PRO ASP GLY ILE
SEQRES 22 A 333 LYS THR GLN GLU MET TYR VAL GLU VAL ASP VAL ASN SER
SEQRES 23 A 333 GLY PRO CYS TYR GLY ARG THR VAL CYS ASP GLU LEU GLY
SEQRES 24 A 333 VAL LEU GLY LYS PRO ALA ASN THR LYS VAL GLY ILE THR
SEQRES 25 A 333 ILE ASP THR ASP TRP PHE TRP GLY LEU VAL GLU GLU CYS
SEQRES 26 A 333 VAL ARG GLY TYR ILE LYS THR HIS
SEQRES 1 B 333 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 333 LEU VAL PRO ARG GLY SER HIS MET GLU LYS ARG LYS ILE
SEQRES 3 B 333 ILE LEU ASP CYS ASP PRO GLY HIS ASP ASP ALA ILE ALA
SEQRES 4 B 333 ILE MET MET ALA ALA LYS HIS PRO ALA ILE ASP LEU LEU
SEQRES 5 B 333 GLY ILE THR ILE VAL ALA GLY ASN GLN THR LEU ASP LYS
SEQRES 6 B 333 THR LEU ILE ASN GLY LEU ASN VAL CYS GLN LYS LEU GLU
SEQRES 7 B 333 ILE ASN VAL PRO VAL TYR ALA GLY MET PRO GLN PRO ILE
SEQRES 8 B 333 MET ARG GLN GLN ILE VAL ALA ASP ASN ILE HIS GLY ASP
SEQRES 9 B 333 THR GLY LEU ASP GLY PRO VAL PHE GLU PRO LEU THR ARG
SEQRES 10 B 333 GLN ALA GLU SER THR HIS ALA VAL LYS TYR ILE ILE ASP
SEQRES 11 B 333 THR LEU MET ALA SER ASP GLY ASP ILE THR LEU VAL PRO
SEQRES 12 B 333 VAL GLY PRO LEU SER ASN ILE ALA VAL ALA MET ARG MET
SEQRES 13 B 333 GLN PRO ALA ILE LEU PRO LYS ILE ARG GLU ILE VAL LEU
SEQRES 14 B 333 MET GLY GLY ALA TYR GLY THR GLY ASN PHE THR PRO SER
SEQRES 15 B 333 ALA GLU PHE ASN ILE PHE ALA ASP PRO GLU ALA ALA ARG
SEQRES 16 B 333 VAL VAL PHE THR SER GLY VAL PRO LEU VAL MET MET GLY
SEQRES 17 B 333 LEU ASP LEU THR ASN GLN THR VAL CYS THR PRO ASP VAL
SEQRES 18 B 333 ILE ALA ARG MET GLU ARG ALA GLY GLY PRO ALA GLY GLU
SEQRES 19 B 333 LEU PHE SER ASP ILE MET ASN PHE THR LEU LYS THR GLN
SEQRES 20 B 333 PHE GLU ASN TYR GLY LEU ALA GLY GLY PRO VAL HIS ASP
SEQRES 21 B 333 ALA THR CYS ILE GLY TYR LEU ILE ASN PRO ASP GLY ILE
SEQRES 22 B 333 LYS THR GLN GLU MET TYR VAL GLU VAL ASP VAL ASN SER
SEQRES 23 B 333 GLY PRO CYS TYR GLY ARG THR VAL CYS ASP GLU LEU GLY
SEQRES 24 B 333 VAL LEU GLY LYS PRO ALA ASN THR LYS VAL GLY ILE THR
SEQRES 25 B 333 ILE ASP THR ASP TRP PHE TRP GLY LEU VAL GLU GLU CYS
SEQRES 26 B 333 VAL ARG GLY TYR ILE LYS THR HIS
SEQRES 1 C 333 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 333 LEU VAL PRO ARG GLY SER HIS MET GLU LYS ARG LYS ILE
SEQRES 3 C 333 ILE LEU ASP CYS ASP PRO GLY HIS ASP ASP ALA ILE ALA
SEQRES 4 C 333 ILE MET MET ALA ALA LYS HIS PRO ALA ILE ASP LEU LEU
SEQRES 5 C 333 GLY ILE THR ILE VAL ALA GLY ASN GLN THR LEU ASP LYS
SEQRES 6 C 333 THR LEU ILE ASN GLY LEU ASN VAL CYS GLN LYS LEU GLU
SEQRES 7 C 333 ILE ASN VAL PRO VAL TYR ALA GLY MET PRO GLN PRO ILE
SEQRES 8 C 333 MET ARG GLN GLN ILE VAL ALA ASP ASN ILE HIS GLY ASP
SEQRES 9 C 333 THR GLY LEU ASP GLY PRO VAL PHE GLU PRO LEU THR ARG
SEQRES 10 C 333 GLN ALA GLU SER THR HIS ALA VAL LYS TYR ILE ILE ASP
SEQRES 11 C 333 THR LEU MET ALA SER ASP GLY ASP ILE THR LEU VAL PRO
SEQRES 12 C 333 VAL GLY PRO LEU SER ASN ILE ALA VAL ALA MET ARG MET
SEQRES 13 C 333 GLN PRO ALA ILE LEU PRO LYS ILE ARG GLU ILE VAL LEU
SEQRES 14 C 333 MET GLY GLY ALA TYR GLY THR GLY ASN PHE THR PRO SER
SEQRES 15 C 333 ALA GLU PHE ASN ILE PHE ALA ASP PRO GLU ALA ALA ARG
SEQRES 16 C 333 VAL VAL PHE THR SER GLY VAL PRO LEU VAL MET MET GLY
SEQRES 17 C 333 LEU ASP LEU THR ASN GLN THR VAL CYS THR PRO ASP VAL
SEQRES 18 C 333 ILE ALA ARG MET GLU ARG ALA GLY GLY PRO ALA GLY GLU
SEQRES 19 C 333 LEU PHE SER ASP ILE MET ASN PHE THR LEU LYS THR GLN
SEQRES 20 C 333 PHE GLU ASN TYR GLY LEU ALA GLY GLY PRO VAL HIS ASP
SEQRES 21 C 333 ALA THR CYS ILE GLY TYR LEU ILE ASN PRO ASP GLY ILE
SEQRES 22 C 333 LYS THR GLN GLU MET TYR VAL GLU VAL ASP VAL ASN SER
SEQRES 23 C 333 GLY PRO CYS TYR GLY ARG THR VAL CYS ASP GLU LEU GLY
SEQRES 24 C 333 VAL LEU GLY LYS PRO ALA ASN THR LYS VAL GLY ILE THR
SEQRES 25 C 333 ILE ASP THR ASP TRP PHE TRP GLY LEU VAL GLU GLU CYS
SEQRES 26 C 333 VAL ARG GLY TYR ILE LYS THR HIS
SEQRES 1 D 333 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 333 LEU VAL PRO ARG GLY SER HIS MET GLU LYS ARG LYS ILE
SEQRES 3 D 333 ILE LEU ASP CYS ASP PRO GLY HIS ASP ASP ALA ILE ALA
SEQRES 4 D 333 ILE MET MET ALA ALA LYS HIS PRO ALA ILE ASP LEU LEU
SEQRES 5 D 333 GLY ILE THR ILE VAL ALA GLY ASN GLN THR LEU ASP LYS
SEQRES 6 D 333 THR LEU ILE ASN GLY LEU ASN VAL CYS GLN LYS LEU GLU
SEQRES 7 D 333 ILE ASN VAL PRO VAL TYR ALA GLY MET PRO GLN PRO ILE
SEQRES 8 D 333 MET ARG GLN GLN ILE VAL ALA ASP ASN ILE HIS GLY ASP
SEQRES 9 D 333 THR GLY LEU ASP GLY PRO VAL PHE GLU PRO LEU THR ARG
SEQRES 10 D 333 GLN ALA GLU SER THR HIS ALA VAL LYS TYR ILE ILE ASP
SEQRES 11 D 333 THR LEU MET ALA SER ASP GLY ASP ILE THR LEU VAL PRO
SEQRES 12 D 333 VAL GLY PRO LEU SER ASN ILE ALA VAL ALA MET ARG MET
SEQRES 13 D 333 GLN PRO ALA ILE LEU PRO LYS ILE ARG GLU ILE VAL LEU
SEQRES 14 D 333 MET GLY GLY ALA TYR GLY THR GLY ASN PHE THR PRO SER
SEQRES 15 D 333 ALA GLU PHE ASN ILE PHE ALA ASP PRO GLU ALA ALA ARG
SEQRES 16 D 333 VAL VAL PHE THR SER GLY VAL PRO LEU VAL MET MET GLY
SEQRES 17 D 333 LEU ASP LEU THR ASN GLN THR VAL CYS THR PRO ASP VAL
SEQRES 18 D 333 ILE ALA ARG MET GLU ARG ALA GLY GLY PRO ALA GLY GLU
SEQRES 19 D 333 LEU PHE SER ASP ILE MET ASN PHE THR LEU LYS THR GLN
SEQRES 20 D 333 PHE GLU ASN TYR GLY LEU ALA GLY GLY PRO VAL HIS ASP
SEQRES 21 D 333 ALA THR CYS ILE GLY TYR LEU ILE ASN PRO ASP GLY ILE
SEQRES 22 D 333 LYS THR GLN GLU MET TYR VAL GLU VAL ASP VAL ASN SER
SEQRES 23 D 333 GLY PRO CYS TYR GLY ARG THR VAL CYS ASP GLU LEU GLY
SEQRES 24 D 333 VAL LEU GLY LYS PRO ALA ASN THR LYS VAL GLY ILE THR
SEQRES 25 D 333 ILE ASP THR ASP TRP PHE TRP GLY LEU VAL GLU GLU CYS
SEQRES 26 D 333 VAL ARG GLY TYR ILE LYS THR HIS
HET CA A 400 1
HET NOS A 401 19
HET CA B 400 1
HET NOS B 401 19
HET CA C 400 1
HET NOS C 401 19
HET CA D 400 1
HET NOS D 401 19
HET TAM D 402 11
HETNAM CA CALCIUM ION
HETNAM NOS INOSINE
HETNAM TAM TRIS(HYDROXYETHYL)AMINOMETHANE
FORMUL 5 CA 4(CA 2+)
FORMUL 6 NOS 4(C10 H12 N4 O5)
FORMUL 13 TAM C7 H17 N O3
FORMUL 14 HOH *331(H2 O)
HELIX 1 1 GLY A 13 HIS A 26 1 14
HELIX 2 2 THR A 42 LEU A 57 1 16
HELIX 3 3 ALA A 78 GLY A 83 1 6
HELIX 4 4 HIS A 103 SER A 115 1 13
HELIX 5 5 LEU A 127 GLN A 137 1 11
HELIX 6 6 PRO A 138 LEU A 141 5 4
HELIX 7 7 GLU A 164 ALA A 169 1 6
HELIX 8 8 ASP A 170 THR A 179 1 10
HELIX 9 9 GLY A 188 ASN A 193 1 6
HELIX 10 10 THR A 198 GLY A 209 1 12
HELIX 11 11 GLY A 209 GLY A 232 1 24
HELIX 12 12 ASP A 240 ASN A 249 1 10
HELIX 13 13 ASP A 294 GLY A 308 1 15
HELIX 14 14 GLY B 13 HIS B 26 1 14
HELIX 15 15 THR B 42 LEU B 57 1 16
HELIX 16 16 HIS B 103 SER B 115 1 13
HELIX 17 17 LEU B 127 GLN B 137 1 11
HELIX 18 18 PRO B 138 PRO B 142 5 5
HELIX 19 19 GLU B 164 ALA B 169 1 6
HELIX 20 20 ASP B 170 THR B 179 1 10
HELIX 21 21 GLY B 188 ASN B 193 1 6
HELIX 22 22 THR B 198 GLY B 209 1 12
HELIX 23 23 GLY B 209 GLY B 232 1 24
HELIX 24 24 ASP B 240 ASN B 249 1 10
HELIX 25 25 ASP B 294 GLY B 308 1 15
HELIX 26 26 GLY C 13 HIS C 26 1 14
HELIX 27 27 THR C 42 LEU C 57 1 16
HELIX 28 28 HIS C 103 SER C 115 1 13
HELIX 29 29 LEU C 127 GLN C 137 1 11
HELIX 30 30 PRO C 138 PRO C 142 5 5
HELIX 31 31 GLU C 164 ALA C 169 1 6
HELIX 32 32 ASP C 170 THR C 179 1 10
HELIX 33 33 GLY C 188 ASN C 193 1 6
HELIX 34 34 THR C 198 GLY C 209 1 12
HELIX 35 35 GLY C 209 ASP C 218 1 10
HELIX 36 36 ASP C 240 ASN C 249 1 10
HELIX 37 37 ASP C 294 GLY C 308 1 15
HELIX 38 38 GLY D 13 HIS D 26 1 14
HELIX 39 39 THR D 42 LEU D 57 1 16
HELIX 40 40 HIS D 103 SER D 115 1 13
HELIX 41 41 LEU D 127 GLN D 137 1 11
HELIX 42 42 PRO D 138 PRO D 142 5 5
HELIX 43 43 GLU D 164 ALA D 169 1 6
HELIX 44 44 ASP D 170 THR D 179 1 10
HELIX 45 45 GLY D 188 ASN D 193 1 6
HELIX 46 46 THR D 198 GLY D 209 1 12
HELIX 47 47 GLY D 209 THR D 223 1 15
HELIX 48 48 LEU D 224 GLY D 232 1 9
HELIX 49 49 ASP D 240 ASN D 249 1 10
HELIX 50 50 ASP D 294 GLY D 308 1 15
SHEET 1 A 9 VAL A 63 ALA A 65 0
SHEET 2 A 9 ILE A 29 ILE A 36 1 N ILE A 34 O TYR A 64
SHEET 3 A 9 ARG A 4 CYS A 10 1 N ARG A 4 O ASP A 30
SHEET 4 A 9 THR A 120 PRO A 123 1 O VAL A 122 N ILE A 7
SHEET 5 A 9 GLU A 146 MET A 150 1 O VAL A 148 N LEU A 121
SHEET 6 A 9 LEU A 184 MET A 187 1 O MET A 187 N LEU A 149
SHEET 7 A 9 THR A 287 ILE A 293 1 O LYS A 288 N MET A 186
SHEET 8 A 9 ILE A 253 VAL A 262 -1 N LYS A 254 O THR A 292
SHEET 9 A 9 THR A 273 ASP A 276 -1 O VAL A 274 N GLU A 261
SHEET 1 B 2 VAL A 196 CYS A 197 0
SHEET 2 B 2 GLY A 236 PRO A 237 -1 O GLY A 236 N CYS A 197
SHEET 1 C 8 VAL B 63 ALA B 65 0
SHEET 2 C 8 ILE B 29 ILE B 36 1 N ILE B 34 O TYR B 64
SHEET 3 C 8 ARG B 4 CYS B 10 1 N ARG B 4 O ASP B 30
SHEET 4 C 8 ILE B 119 PRO B 123 1 O VAL B 122 N ILE B 7
SHEET 5 C 8 ILE B 144 MET B 150 1 O VAL B 148 N LEU B 121
SHEET 6 C 8 LEU B 184 MET B 187 1 O VAL B 185 N ILE B 147
SHEET 7 C 8 THR B 287 ILE B 293 1 O GLY B 290 N MET B 186
SHEET 8 C 8 ILE B 253 MET B 258 -1 N LYS B 254 O THR B 292
SHEET 1 D 2 VAL B 260 VAL B 262 0
SHEET 2 D 2 THR B 273 CYS B 275 -1 O VAL B 274 N GLU B 261
SHEET 1 E 8 VAL C 63 ALA C 65 0
SHEET 2 E 8 ILE C 29 ILE C 36 1 N ILE C 36 O TYR C 64
SHEET 3 E 8 ARG C 4 CYS C 10 1 N ILE C 6 O ASP C 30
SHEET 4 E 8 ILE C 119 PRO C 123 1 O THR C 120 N LYS C 5
SHEET 5 E 8 ILE C 144 MET C 150 1 O MET C 150 N PRO C 123
SHEET 6 E 8 LEU C 184 MET C 187 1 O VAL C 185 N LEU C 149
SHEET 7 E 8 THR C 287 ILE C 293 1 O LYS C 288 N MET C 186
SHEET 8 E 8 ILE C 253 MET C 258 -1 N LYS C 254 O THR C 292
SHEET 1 F 2 VAL C 260 VAL C 262 0
SHEET 2 F 2 THR C 273 CYS C 275 -1 O VAL C 274 N GLU C 261
SHEET 1 G 8 VAL D 63 ALA D 65 0
SHEET 2 G 8 ILE D 29 ILE D 36 1 N ILE D 34 O TYR D 64
SHEET 3 G 8 ARG D 4 CYS D 10 1 N ILE D 6 O ASP D 30
SHEET 4 G 8 ILE D 119 PRO D 123 1 O THR D 120 N LYS D 5
SHEET 5 G 8 ILE D 144 MET D 150 1 O VAL D 148 N LEU D 121
SHEET 6 G 8 LEU D 184 MET D 187 1 O MET D 187 N LEU D 149
SHEET 7 G 8 THR D 287 ILE D 293 1 O GLY D 290 N MET D 186
SHEET 8 G 8 ILE D 253 MET D 258 -1 N LYS D 254 O THR D 292
SHEET 1 H 2 VAL D 196 CYS D 197 0
SHEET 2 H 2 GLY D 236 PRO D 237 -1 O GLY D 236 N CYS D 197
SHEET 1 I 2 VAL D 260 ASP D 263 0
SHEET 2 I 2 ARG D 272 CYS D 275 -1 O VAL D 274 N GLU D 261
LINK OD1 ASP A 11 CA CA A 400 1555 1555 2.55
LINK OD1 ASP A 16 CA CA A 400 1555 1555 2.44
LINK OD2 ASP A 16 CA CA A 400 1555 1555 2.75
LINK O VAL A 124 CA CA A 400 1555 1555 2.37
LINK OD2 ASP A 240 CA CA A 400 1555 1555 2.55
LINK CA CA A 400 O3' NOS A 401 1555 1555 2.25
LINK CA CA A 400 O2' NOS A 401 1555 1555 2.18
LINK CA CA A 400 O HOH A 502 1555 1555 2.70
LINK OD1 ASP B 11 CA CA B 400 1555 1555 2.43
LINK OD1 ASP B 16 CA CA B 400 1555 1555 2.46
LINK OD2 ASP B 16 CA CA B 400 1555 1555 2.80
LINK O VAL B 124 CA CA B 400 1555 1555 2.36
LINK OD2 ASP B 240 CA CA B 400 1555 1555 2.64
LINK CA CA B 400 O3' NOS B 401 1555 1555 2.74
LINK CA CA B 400 O2' NOS B 401 1555 1555 2.44
LINK CA CA B 400 O HOH B 404 1555 1555 2.64
LINK OD1 ASP C 11 CA CA C 400 1555 1555 2.49
LINK OD1 ASP C 16 CA CA C 400 1555 1555 2.65
LINK OD2 ASP C 16 CA CA C 400 1555 1555 2.60
LINK O VAL C 124 CA CA C 400 1555 1555 2.55
LINK OD2 ASP C 240 CA CA C 400 1555 1555 2.70
LINK CA CA C 400 O3' NOS C 401 1555 1555 2.90
LINK CA CA C 400 O2' NOS C 401 1555 1555 2.63
LINK CA CA C 400 O HOH C 433 1555 1555 2.42
LINK OD1 ASP D 11 CA CA D 400 1555 1555 2.51
LINK OD1 ASP D 16 CA CA D 400 1555 1555 2.42
LINK OD2 ASP D 16 CA CA D 400 1555 1555 2.56
LINK O VAL D 124 CA CA D 400 1555 1555 2.44
LINK OD2 ASP D 240 CA CA D 400 1555 1555 2.45
LINK CA CA D 400 O2' NOS D 401 1555 1555 2.32
LINK CA CA D 400 O3' NOS D 401 1555 1555 2.67
LINK CA CA D 400 O HOH D 417 1555 1555 2.72
CISPEP 1 PRO A 12 GLY A 13 0 -12.08
CISPEP 2 PRO B 12 GLY B 13 0 -15.54
CISPEP 3 PRO C 12 GLY C 13 0 -10.00
CISPEP 4 PRO D 12 GLY D 13 0 -13.83
SITE 1 AC1 4 ASP A 11 ASP A 16 ASP A 240 HOH A 502
SITE 1 AC2 5 ASP B 11 ASP B 16 ASN B 40 ASP B 240
SITE 2 AC2 5 HOH B 404
SITE 1 AC3 5 ASP C 11 ASP C 16 ASN C 40 ASP C 240
SITE 2 AC3 5 HOH C 433
SITE 1 AC4 5 ASP D 11 ASP D 16 ASN D 40 ASP D 240
SITE 2 AC4 5 HOH D 417
SITE 1 AC5 15 ASP A 15 ASP A 16 ASN A 40 ILE A 81
SITE 2 AC5 15 HIS A 82 MET A 150 ASN A 158 GLU A 164
SITE 3 AC5 15 PHE A 165 ASN A 166 GLN A 227 TYR A 231
SITE 4 AC5 15 HIS A 239 ASP A 240 HOH A 502
SITE 1 AC6 11 ASP B 15 ASP B 16 ASN B 40 MET B 150
SITE 2 AC6 11 ASN B 158 GLU B 164 PHE B 165 ASN B 166
SITE 3 AC6 11 GLN B 227 TYR B 231 ASP B 240
SITE 1 AC7 9 ASP C 15 ASP C 16 ASN C 40 ALA C 78
SITE 2 AC7 9 MET C 150 ASN C 158 GLU C 164 ASN C 166
SITE 3 AC7 9 ASP C 240
SITE 1 AC8 15 ASP D 15 ASP D 16 ASN D 40 ALA D 78
SITE 2 AC8 15 ILE D 81 HIS D 82 MET D 150 ASN D 158
SITE 3 AC8 15 GLU D 164 PHE D 165 ASN D 166 GLN D 227
SITE 4 AC8 15 TYR D 231 ASP D 240 HOH D 417
SITE 1 AC9 6 MET C 136 GLN C 137 LEU D 43 GLY D 66
SITE 2 AC9 6 PRO D 68 HIS D 103
CRYST1 45.112 82.406 90.163 67.90 79.59 89.65 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 0.022167 -0.000135 -0.004350 0.00000
SCALE2 0.000000 0.012135 -0.005007 0.00000
SCALE3 0.000000 0.000000 0.012199 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
