HEADER VIRAL PROTEIN 22-JAN-15 4XSD
TITLE COMPLEX STRUCTURE OF THYMIDYLATE SYNTHASE FROM VARICELLA ZOSTER VIRUS
TITLE 2 WITH A DUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TSASE;
COMPND 5 EC: 2.1.1.45;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VARICELLA-ZOSTER VIRUS (STRAIN OKA VACCINE);
SOURCE 3 ORGANISM_COMMON: HHV-3;
SOURCE 4 ORGANISM_TAXID: 341980;
SOURCE 5 STRAIN: OKA VACCINE;
SOURCE 6 GENE: ORF13;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS VZV, THYMIDYLATE SYNTHASE, HERPESVIRUS, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HEW
REVDAT 2 10-JAN-24 4XSD 1 REMARK
REVDAT 1 16-DEC-15 4XSD 0
JRNL AUTH K.HEW,S.L.DAHLROTH,S.VEERAPPAN,L.X.PAN,T.CORNVIK,P.NORDLUND
JRNL TITL STRUCTURE OF THE VARICELLA ZOSTER VIRUS THYMIDYLATE SYNTHASE
JRNL TITL 2 ESTABLISHES FUNCTIONAL AND STRUCTURAL SIMILARITIES AS THE
JRNL TITL 3 HUMAN ENZYME AND POTENTIATES ITSELF AS A TARGET OF
JRNL TITL 4 BRIVUDINE.
JRNL REF PLOS ONE V. 10 43947 2015
JRNL REFN ESSN 1932-6203
JRNL PMID 26630264
JRNL DOI 10.1371/JOURNAL.PONE.0143947
REMARK 2
REMARK 2 RESOLUTION. 2.90 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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 48187
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2419
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 19.4937 - 7.3337 0.96 2797 128 0.2143 0.2338
REMARK 3 2 7.3337 - 5.8734 0.89 2603 130 0.2473 0.2857
REMARK 3 3 5.8734 - 5.1466 0.94 2727 81 0.2429 0.2482
REMARK 3 4 5.1466 - 4.6832 0.94 2727 108 0.2140 0.2527
REMARK 3 5 4.6832 - 4.3515 0.94 2763 122 0.2099 0.2494
REMARK 3 6 4.3515 - 4.0974 0.94 2732 146 0.2148 0.2475
REMARK 3 7 4.0974 - 3.8939 0.93 2684 171 0.2328 0.2731
REMARK 3 8 3.8939 - 3.7257 0.93 2743 156 0.2399 0.3102
REMARK 3 9 3.7257 - 3.5831 0.95 2758 130 0.2428 0.2876
REMARK 3 10 3.5831 - 3.4602 0.92 2715 190 0.2491 0.3233
REMARK 3 11 3.4602 - 3.3526 0.93 2680 125 0.2599 0.2588
REMARK 3 12 3.3526 - 3.2572 0.93 2711 120 0.2614 0.2909
REMARK 3 13 3.2572 - 3.1718 0.89 2614 165 0.2750 0.3188
REMARK 3 14 3.1718 - 3.0947 0.90 2638 147 0.2896 0.3149
REMARK 3 15 3.0947 - 3.0246 0.89 2601 123 0.2918 0.3601
REMARK 3 16 3.0246 - 2.9605 0.90 2592 128 0.2934 0.3185
REMARK 3 17 2.9605 - 2.9015 0.88 2569 172 0.2964 0.3186
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.004 9074
REMARK 3 ANGLE : 0.882 12322
REMARK 3 CHIRALITY : 0.032 1332
REMARK 3 PLANARITY : 0.004 1565
REMARK 3 DIHEDRAL : 14.297 3306
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 4XSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49612
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4XSE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8, 40% PEG 300, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,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 59.44000
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 29.72000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -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 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 VAL A -5
REMARK 465 ASP A -4
REMARK 465 LEU A -3
REMARK 465 GLY A -2
REMARK 465 THR A -1
REMARK 465 GLU A 0
REMARK 465 ASN A 1
REMARK 465 LEU A 2
REMARK 465 TYR A 3
REMARK 465 PHE A 4
REMARK 465 GLN A 5
REMARK 465 SER A 6
REMARK 465 MET A 7
REMARK 465 THR A 8
REMARK 465 LYS A 9
REMARK 465 VAL A 10
REMARK 465 PRO A 11
REMARK 465 GLY A 12
REMARK 465 PHE A 13
REMARK 465 THR A 14
REMARK 465 ASP A 98
REMARK 465 ILE A 99
REMARK 465 TYR A 100
REMARK 465 GLY A 101
REMARK 465 SER A 102
REMARK 465 SER A 103
REMARK 465 LYS A 104
REMARK 465 PHE A 105
REMARK 465 LEU A 106
REMARK 465 ASN A 107
REMARK 465 ARG A 108
REMARK 465 ASN A 109
REMARK 465 GLY A 110
REMARK 465 PHE A 111
REMARK 465 HIS A 112
REMARK 465 LYS A 113
REMARK 465 ARG A 114
REMARK 465 HIS A 115
REMARK 465 THR A 116
REMARK 465 MET 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 HIS B -9
REMARK 465 SER B -8
REMARK 465 SER B -7
REMARK 465 GLY B -6
REMARK 465 VAL B -5
REMARK 465 ASP B -4
REMARK 465 LEU B -3
REMARK 465 GLY B -2
REMARK 465 THR B -1
REMARK 465 GLU B 0
REMARK 465 ASN B 1
REMARK 465 LEU B 2
REMARK 465 TYR B 3
REMARK 465 PHE B 4
REMARK 465 GLN B 5
REMARK 465 SER B 6
REMARK 465 MET B 7
REMARK 465 THR B 8
REMARK 465 LYS B 9
REMARK 465 VAL B 10
REMARK 465 PRO B 11
REMARK 465 GLY B 12
REMARK 465 PHE B 13
REMARK 465 ARG B 38
REMARK 465 THR B 39
REMARK 465 ASP B 136
REMARK 465 CYS B 137
REMARK 465 GLN B 138
REMARK 465 MET 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 HIS C -9
REMARK 465 SER C -8
REMARK 465 SER C -7
REMARK 465 GLY C -6
REMARK 465 VAL C -5
REMARK 465 ASP C -4
REMARK 465 LEU C -3
REMARK 465 GLY C -2
REMARK 465 THR C -1
REMARK 465 GLU C 0
REMARK 465 ASN C 1
REMARK 465 LEU C 2
REMARK 465 TYR C 3
REMARK 465 PHE C 4
REMARK 465 GLN C 5
REMARK 465 SER C 6
REMARK 465 MET C 7
REMARK 465 THR C 8
REMARK 465 LYS C 9
REMARK 465 VAL C 10
REMARK 465 PRO C 11
REMARK 465 GLY C 12
REMARK 465 PHE C 13
REMARK 465 THR C 14
REMARK 465 LEU C 15
REMARK 465 TYR C 100
REMARK 465 GLY C 101
REMARK 465 SER C 102
REMARK 465 SER C 103
REMARK 465 LYS C 104
REMARK 465 PHE C 105
REMARK 465 LEU C 106
REMARK 465 ASN C 107
REMARK 465 ARG C 108
REMARK 465 ASN C 109
REMARK 465 GLY C 110
REMARK 465 PHE C 111
REMARK 465 HIS C 112
REMARK 465 LYS C 113
REMARK 465 ARG C 114
REMARK 465 HIS C 115
REMARK 465 THR C 116
REMARK 465 GLY C 117
REMARK 465 MET 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 HIS D -9
REMARK 465 SER D -8
REMARK 465 SER D -7
REMARK 465 GLY D -6
REMARK 465 VAL D -5
REMARK 465 ASP D -4
REMARK 465 LEU D -3
REMARK 465 GLY D -2
REMARK 465 THR D -1
REMARK 465 GLU D 0
REMARK 465 ASN D 1
REMARK 465 LEU D 2
REMARK 465 TYR D 3
REMARK 465 PHE D 4
REMARK 465 GLN D 5
REMARK 465 SER D 6
REMARK 465 MET D 7
REMARK 465 THR D 8
REMARK 465 LYS D 9
REMARK 465 VAL D 10
REMARK 465 PRO D 11
REMARK 465 GLY D 12
REMARK 465 PHE D 13
REMARK 465 ARG D 38
REMARK 465 THR D 39
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 OH TYR C 21 O MET C 207 2.08
REMARK 500 ND2 ASN C 214 O4 UMP C 1001 2.09
REMARK 500 OH TYR D 21 O MET D 207 2.09
REMARK 500 OH TYR A 21 O MET A 207 2.13
REMARK 500 OH TYR B 21 O MET B 207 2.13
REMARK 500 ND2 ASN D 214 O4 UMP D 1001 2.13
REMARK 500 N LYS A 135 OH TYR A 141 2.14
REMARK 500 OH TYR C 201 OE1 GLN D 188 2.15
REMARK 500 OG SER C 45 OD2 ASP C 242 2.15
REMARK 500 OG SER D 45 OD1 ASP D 242 2.16
REMARK 500 OG1 THR B 116 OD2 ASP C 278 2.17
REMARK 500 OG1 THR D 16 O ARG D 52 2.17
REMARK 500 O THR A 151 OG1 THR A 155 2.17
REMARK 500 NE ARG C 164 OP1 UMP D 1001 2.18
REMARK 500 OE2 GLU C 18 OG1 THR C 64 2.18
REMARK 500 NH1 ARG B 259 O PRO B 293 2.19
REMARK 500 NH1 ARG B 163 OP2 UMP A 1001 2.19
REMARK 500 O THR A 16 NE2 GLN A 20 2.19
REMARK 500 O ASP A 147 OG1 THR A 151 2.19
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 57 -7.71 70.26
REMARK 500 LYS A 135 -72.05 -112.19
REMARK 500 GLN A 143 -11.52 69.75
REMARK 500 THR A 158 -70.26 -90.29
REMARK 500 LEU A 180 137.36 -177.99
REMARK 500 LEU A 209 -72.00 -101.72
REMARK 500 PRO A 291 -169.81 -70.99
REMARK 500 LEU B 15 -65.15 -129.86
REMARK 500 THR B 16 -5.35 85.14
REMARK 500 PRO B 60 58.15 -69.11
REMARK 500 TRP B 69 -61.28 -90.11
REMARK 500 LEU B 119 -61.66 -94.47
REMARK 500 GLN B 143 -5.29 81.07
REMARK 500 LEU B 186 163.02 177.00
REMARK 500 LEU B 209 -65.63 -131.27
REMARK 500 PRO C 60 58.21 -66.12
REMARK 500 ASP C 93 -1.52 85.20
REMARK 500 LYS C 135 -70.48 -111.80
REMARK 500 GLN C 143 -13.48 78.24
REMARK 500 LEU C 209 -62.24 -126.26
REMARK 500 ILE C 270 -71.52 -74.17
REMARK 500 ASP C 275 175.29 170.13
REMARK 500 ILE C 276 -70.68 -75.25
REMARK 500 LEU D 15 -72.31 -130.99
REMARK 500 THR D 16 -13.84 81.34
REMARK 500 ASN D 57 -2.66 68.20
REMARK 500 LYS D 135 -66.82 -129.97
REMARK 500 GLN D 143 -4.51 67.51
REMARK 500 SER D 162 156.30 178.80
REMARK 500 LEU D 180 137.99 -178.92
REMARK 500 LEU D 209 -61.73 -130.81
REMARK 500 PRO D 265 -175.23 -64.39
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 UMP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP D 1001
DBREF 4XSD A 8 295 UNP Q4JQW2 TYSY_VZVO 8 295
DBREF 4XSD B 8 295 UNP Q4JQW2 TYSY_VZVO 8 295
DBREF 4XSD C 8 295 UNP Q4JQW2 TYSY_VZVO 8 295
DBREF 4XSD D 8 295 UNP Q4JQW2 TYSY_VZVO 8 295
SEQADV 4XSD MET A -15 UNP Q4JQW2 INITIATING METHIONINE
SEQADV 4XSD HIS A -14 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS A -13 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS A -12 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS A -11 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS A -10 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS A -9 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER A -8 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER A -7 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY A -6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD VAL A -5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASP A -4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU A -3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY A -2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD THR A -1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLU A 0 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASN A 1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU A 2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD TYR A 3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD PHE A 4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLN A 5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER A 6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD MET A 7 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD MET B -15 UNP Q4JQW2 INITIATING METHIONINE
SEQADV 4XSD HIS B -14 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS B -13 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS B -12 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS B -11 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS B -10 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS B -9 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER B -8 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER B -7 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY B -6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD VAL B -5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASP B -4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU B -3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY B -2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD THR B -1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLU B 0 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASN B 1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU B 2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD TYR B 3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD PHE B 4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLN B 5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER B 6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD MET B 7 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD MET C -15 UNP Q4JQW2 INITIATING METHIONINE
SEQADV 4XSD HIS C -14 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS C -13 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS C -12 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS C -11 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS C -10 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS C -9 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER C -8 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER C -7 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY C -6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD VAL C -5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASP C -4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU C -3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY C -2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD THR C -1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLU C 0 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASN C 1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU C 2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD TYR C 3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD PHE C 4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLN C 5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER C 6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD MET C 7 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD MET D -15 UNP Q4JQW2 INITIATING METHIONINE
SEQADV 4XSD HIS D -14 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS D -13 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS D -12 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS D -11 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS D -10 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD HIS D -9 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER D -8 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER D -7 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY D -6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD VAL D -5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASP D -4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU D -3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLY D -2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD THR D -1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLU D 0 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD ASN D 1 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD LEU D 2 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD TYR D 3 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD PHE D 4 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD GLN D 5 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD SER D 6 UNP Q4JQW2 EXPRESSION TAG
SEQADV 4XSD MET D 7 UNP Q4JQW2 EXPRESSION TAG
SEQRES 1 A 311 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 311 GLY THR GLU ASN LEU TYR PHE GLN SER MET THR LYS VAL
SEQRES 3 A 311 PRO GLY PHE THR LEU THR GLY GLU LEU GLN TYR LEU LYS
SEQRES 4 A 311 GLN VAL ASP ASP ILE LEU ARG TYR GLY VAL ARG LYS ARG
SEQRES 5 A 311 ASP ARG THR GLY ILE GLY THR LEU SER LEU PHE GLY MET
SEQRES 6 A 311 GLN ALA ARG TYR ASN LEU ARG ASN GLU PHE PRO LEU LEU
SEQRES 7 A 311 THR THR LYS ARG VAL PHE TRP ARG ALA VAL VAL GLU GLU
SEQRES 8 A 311 LEU LEU TRP PHE ILE ARG GLY SER THR ASP SER LYS GLU
SEQRES 9 A 311 LEU ALA ALA LYS ASP ILE HIS ILE TRP ASP ILE TYR GLY
SEQRES 10 A 311 SER SER LYS PHE LEU ASN ARG ASN GLY PHE HIS LYS ARG
SEQRES 11 A 311 HIS THR GLY ASP LEU GLY PRO ILE TYR GLY PHE GLN TRP
SEQRES 12 A 311 ARG HIS PHE GLY ALA GLU TYR LYS ASP CYS GLN SER ASN
SEQRES 13 A 311 TYR LEU GLN GLN GLY ILE ASP GLN LEU GLN THR VAL ILE
SEQRES 14 A 311 ASP THR ILE LYS THR ASN PRO GLU SER ARG ARG MET ILE
SEQRES 15 A 311 ILE SER SER TRP ASN PRO LYS ASP ILE PRO LEU MET VAL
SEQRES 16 A 311 LEU PRO PRO CYS HIS THR LEU CYS GLN PHE TYR VAL ALA
SEQRES 17 A 311 ASN GLY GLU LEU SER CYS GLN VAL TYR GLN ARG SER GLY
SEQRES 18 A 311 ASP MET GLY LEU GLY VAL PRO PHE ASN ILE ALA GLY TYR
SEQRES 19 A 311 ALA LEU LEU THR TYR ILE VAL ALA HIS VAL THR GLY LEU
SEQRES 20 A 311 LYS THR GLY ASP LEU ILE HIS THR MET GLY ASP ALA HIS
SEQRES 21 A 311 ILE TYR LEU ASN HIS ILE ASP ALA LEU LYS VAL GLN LEU
SEQRES 22 A 311 ALA ARG SER PRO LYS PRO PHE PRO CYS LEU LYS ILE ILE
SEQRES 23 A 311 ARG ASN VAL THR ASP ILE ASN ASP PHE LYS TRP ASP ASP
SEQRES 24 A 311 PHE GLN LEU ASP GLY TYR ASN PRO HIS PRO PRO LEU
SEQRES 1 B 311 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 311 GLY THR GLU ASN LEU TYR PHE GLN SER MET THR LYS VAL
SEQRES 3 B 311 PRO GLY PHE THR LEU THR GLY GLU LEU GLN TYR LEU LYS
SEQRES 4 B 311 GLN VAL ASP ASP ILE LEU ARG TYR GLY VAL ARG LYS ARG
SEQRES 5 B 311 ASP ARG THR GLY ILE GLY THR LEU SER LEU PHE GLY MET
SEQRES 6 B 311 GLN ALA ARG TYR ASN LEU ARG ASN GLU PHE PRO LEU LEU
SEQRES 7 B 311 THR THR LYS ARG VAL PHE TRP ARG ALA VAL VAL GLU GLU
SEQRES 8 B 311 LEU LEU TRP PHE ILE ARG GLY SER THR ASP SER LYS GLU
SEQRES 9 B 311 LEU ALA ALA LYS ASP ILE HIS ILE TRP ASP ILE TYR GLY
SEQRES 10 B 311 SER SER LYS PHE LEU ASN ARG ASN GLY PHE HIS LYS ARG
SEQRES 11 B 311 HIS THR GLY ASP LEU GLY PRO ILE TYR GLY PHE GLN TRP
SEQRES 12 B 311 ARG HIS PHE GLY ALA GLU TYR LYS ASP CYS GLN SER ASN
SEQRES 13 B 311 TYR LEU GLN GLN GLY ILE ASP GLN LEU GLN THR VAL ILE
SEQRES 14 B 311 ASP THR ILE LYS THR ASN PRO GLU SER ARG ARG MET ILE
SEQRES 15 B 311 ILE SER SER TRP ASN PRO LYS ASP ILE PRO LEU MET VAL
SEQRES 16 B 311 LEU PRO PRO CYS HIS THR LEU CYS GLN PHE TYR VAL ALA
SEQRES 17 B 311 ASN GLY GLU LEU SER CYS GLN VAL TYR GLN ARG SER GLY
SEQRES 18 B 311 ASP MET GLY LEU GLY VAL PRO PHE ASN ILE ALA GLY TYR
SEQRES 19 B 311 ALA LEU LEU THR TYR ILE VAL ALA HIS VAL THR GLY LEU
SEQRES 20 B 311 LYS THR GLY ASP LEU ILE HIS THR MET GLY ASP ALA HIS
SEQRES 21 B 311 ILE TYR LEU ASN HIS ILE ASP ALA LEU LYS VAL GLN LEU
SEQRES 22 B 311 ALA ARG SER PRO LYS PRO PHE PRO CYS LEU LYS ILE ILE
SEQRES 23 B 311 ARG ASN VAL THR ASP ILE ASN ASP PHE LYS TRP ASP ASP
SEQRES 24 B 311 PHE GLN LEU ASP GLY TYR ASN PRO HIS PRO PRO LEU
SEQRES 1 C 311 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 311 GLY THR GLU ASN LEU TYR PHE GLN SER MET THR LYS VAL
SEQRES 3 C 311 PRO GLY PHE THR LEU THR GLY GLU LEU GLN TYR LEU LYS
SEQRES 4 C 311 GLN VAL ASP ASP ILE LEU ARG TYR GLY VAL ARG LYS ARG
SEQRES 5 C 311 ASP ARG THR GLY ILE GLY THR LEU SER LEU PHE GLY MET
SEQRES 6 C 311 GLN ALA ARG TYR ASN LEU ARG ASN GLU PHE PRO LEU LEU
SEQRES 7 C 311 THR THR LYS ARG VAL PHE TRP ARG ALA VAL VAL GLU GLU
SEQRES 8 C 311 LEU LEU TRP PHE ILE ARG GLY SER THR ASP SER LYS GLU
SEQRES 9 C 311 LEU ALA ALA LYS ASP ILE HIS ILE TRP ASP ILE TYR GLY
SEQRES 10 C 311 SER SER LYS PHE LEU ASN ARG ASN GLY PHE HIS LYS ARG
SEQRES 11 C 311 HIS THR GLY ASP LEU GLY PRO ILE TYR GLY PHE GLN TRP
SEQRES 12 C 311 ARG HIS PHE GLY ALA GLU TYR LYS ASP CYS GLN SER ASN
SEQRES 13 C 311 TYR LEU GLN GLN GLY ILE ASP GLN LEU GLN THR VAL ILE
SEQRES 14 C 311 ASP THR ILE LYS THR ASN PRO GLU SER ARG ARG MET ILE
SEQRES 15 C 311 ILE SER SER TRP ASN PRO LYS ASP ILE PRO LEU MET VAL
SEQRES 16 C 311 LEU PRO PRO CYS HIS THR LEU CYS GLN PHE TYR VAL ALA
SEQRES 17 C 311 ASN GLY GLU LEU SER CYS GLN VAL TYR GLN ARG SER GLY
SEQRES 18 C 311 ASP MET GLY LEU GLY VAL PRO PHE ASN ILE ALA GLY TYR
SEQRES 19 C 311 ALA LEU LEU THR TYR ILE VAL ALA HIS VAL THR GLY LEU
SEQRES 20 C 311 LYS THR GLY ASP LEU ILE HIS THR MET GLY ASP ALA HIS
SEQRES 21 C 311 ILE TYR LEU ASN HIS ILE ASP ALA LEU LYS VAL GLN LEU
SEQRES 22 C 311 ALA ARG SER PRO LYS PRO PHE PRO CYS LEU LYS ILE ILE
SEQRES 23 C 311 ARG ASN VAL THR ASP ILE ASN ASP PHE LYS TRP ASP ASP
SEQRES 24 C 311 PHE GLN LEU ASP GLY TYR ASN PRO HIS PRO PRO LEU
SEQRES 1 D 311 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 311 GLY THR GLU ASN LEU TYR PHE GLN SER MET THR LYS VAL
SEQRES 3 D 311 PRO GLY PHE THR LEU THR GLY GLU LEU GLN TYR LEU LYS
SEQRES 4 D 311 GLN VAL ASP ASP ILE LEU ARG TYR GLY VAL ARG LYS ARG
SEQRES 5 D 311 ASP ARG THR GLY ILE GLY THR LEU SER LEU PHE GLY MET
SEQRES 6 D 311 GLN ALA ARG TYR ASN LEU ARG ASN GLU PHE PRO LEU LEU
SEQRES 7 D 311 THR THR LYS ARG VAL PHE TRP ARG ALA VAL VAL GLU GLU
SEQRES 8 D 311 LEU LEU TRP PHE ILE ARG GLY SER THR ASP SER LYS GLU
SEQRES 9 D 311 LEU ALA ALA LYS ASP ILE HIS ILE TRP ASP ILE TYR GLY
SEQRES 10 D 311 SER SER LYS PHE LEU ASN ARG ASN GLY PHE HIS LYS ARG
SEQRES 11 D 311 HIS THR GLY ASP LEU GLY PRO ILE TYR GLY PHE GLN TRP
SEQRES 12 D 311 ARG HIS PHE GLY ALA GLU TYR LYS ASP CYS GLN SER ASN
SEQRES 13 D 311 TYR LEU GLN GLN GLY ILE ASP GLN LEU GLN THR VAL ILE
SEQRES 14 D 311 ASP THR ILE LYS THR ASN PRO GLU SER ARG ARG MET ILE
SEQRES 15 D 311 ILE SER SER TRP ASN PRO LYS ASP ILE PRO LEU MET VAL
SEQRES 16 D 311 LEU PRO PRO CYS HIS THR LEU CYS GLN PHE TYR VAL ALA
SEQRES 17 D 311 ASN GLY GLU LEU SER CYS GLN VAL TYR GLN ARG SER GLY
SEQRES 18 D 311 ASP MET GLY LEU GLY VAL PRO PHE ASN ILE ALA GLY TYR
SEQRES 19 D 311 ALA LEU LEU THR TYR ILE VAL ALA HIS VAL THR GLY LEU
SEQRES 20 D 311 LYS THR GLY ASP LEU ILE HIS THR MET GLY ASP ALA HIS
SEQRES 21 D 311 ILE TYR LEU ASN HIS ILE ASP ALA LEU LYS VAL GLN LEU
SEQRES 22 D 311 ALA ARG SER PRO LYS PRO PHE PRO CYS LEU LYS ILE ILE
SEQRES 23 D 311 ARG ASN VAL THR ASP ILE ASN ASP PHE LYS TRP ASP ASP
SEQRES 24 D 311 PHE GLN LEU ASP GLY TYR ASN PRO HIS PRO PRO LEU
HET UMP A1001 20
HET UMP B1001 20
HET UMP C1001 20
HET UMP D1001 20
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETSYN UMP DUMP
FORMUL 5 UMP 4(C9 H13 N2 O8 P)
FORMUL 9 HOH *9(H2 O)
HELIX 1 AA1 GLU A 18 LEU A 29 1 12
HELIX 2 AA2 PHE A 68 GLY A 82 1 15
HELIX 3 AA3 SER A 86 ALA A 91 1 6
HELIX 4 AA4 ILE A 122 HIS A 129 1 8
HELIX 5 AA5 ASP A 147 ASN A 159 1 13
HELIX 6 AA6 ASP A 174 MET A 178 5 5
HELIX 7 AA7 LEU A 209 THR A 229 1 21
HELIX 8 AA8 ASN A 248 LEU A 257 1 10
HELIX 9 AA9 ASP A 275 PHE A 279 5 5
HELIX 10 AB1 LYS A 280 ASP A 282 5 3
HELIX 11 AB2 GLY B 17 GLY B 32 1 16
HELIX 12 AB3 PHE B 68 ARG B 81 1 14
HELIX 13 AB4 SER B 86 ALA B 91 1 6
HELIX 14 AB5 SER B 102 ASN B 107 1 6
HELIX 15 AB6 ILE B 122 HIS B 129 1 8
HELIX 16 AB7 ASP B 147 ASN B 159 1 13
HELIX 17 AB8 GLY B 210 GLY B 230 1 21
HELIX 18 AB9 HIS B 249 ALA B 258 1 10
HELIX 19 AC1 LYS B 280 PHE B 284 5 5
HELIX 20 AC2 GLU C 18 TYR C 31 1 14
HELIX 21 AC3 TRP C 69 ARG C 81 1 13
HELIX 22 AC4 SER C 86 ALA C 91 1 6
HELIX 23 AC5 ILE C 122 HIS C 129 1 8
HELIX 24 AC6 ASP C 147 ASN C 159 1 13
HELIX 25 AC7 LEU C 209 GLY C 230 1 22
HELIX 26 AC8 HIS C 249 LEU C 257 1 9
HELIX 27 AC9 GLY D 17 GLY D 32 1 16
HELIX 28 AD1 PHE D 68 ARG D 81 1 14
HELIX 29 AD2 TRP D 97 SER D 102 1 6
HELIX 30 AD3 SER D 102 GLY D 110 1 9
HELIX 31 AD4 ILE D 122 HIS D 129 1 8
HELIX 32 AD5 ASP D 147 ASN D 159 1 13
HELIX 33 AD6 LEU D 209 THR D 229 1 21
HELIX 34 AD7 HIS D 249 LEU D 257 1 9
SHEET 1 AA1 4 VAL A 33 ARG A 36 0
SHEET 2 AA1 4 GLY A 42 LEU A 46 -1 O SER A 45 N VAL A 33
SHEET 3 AA1 4 LYS A 232 TYR A 246 -1 O ALA A 243 N LEU A 46
SHEET 4 AA1 4 MET A 49 ASN A 54 -1 N TYR A 53 O LEU A 236
SHEET 1 AA2 6 VAL A 33 ARG A 36 0
SHEET 2 AA2 6 GLY A 42 LEU A 46 -1 O SER A 45 N VAL A 33
SHEET 3 AA2 6 LYS A 232 TYR A 246 -1 O ALA A 243 N LEU A 46
SHEET 4 AA2 6 GLU A 195 ASP A 206 1 N GLN A 202 O THR A 239
SHEET 5 AA2 6 HIS A 184 ALA A 192 -1 N THR A 185 O TYR A 201
SHEET 6 AA2 6 ILE A 166 SER A 168 -1 N ILE A 167 O CYS A 187
SHEET 1 AA3 2 CYS A 266 ILE A 269 0
SHEET 2 AA3 2 PHE A 284 ASP A 287 -1 O GLN A 285 N LYS A 268
SHEET 1 AA4 4 VAL B 33 ARG B 36 0
SHEET 2 AA4 4 GLY B 42 LEU B 46 -1 O SER B 45 N VAL B 33
SHEET 3 AA4 4 LYS B 232 TYR B 246 -1 O ILE B 245 N LEU B 44
SHEET 4 AA4 4 MET B 49 ASN B 54 -1 N ALA B 51 O HIS B 238
SHEET 1 AA5 6 VAL B 33 ARG B 36 0
SHEET 2 AA5 6 GLY B 42 LEU B 46 -1 O SER B 45 N VAL B 33
SHEET 3 AA5 6 LYS B 232 TYR B 246 -1 O ILE B 245 N LEU B 44
SHEET 4 AA5 6 GLU B 195 ASP B 206 1 N GLN B 202 O GLY B 241
SHEET 5 AA5 6 HIS B 184 ALA B 192 -1 N TYR B 190 O SER B 197
SHEET 6 AA5 6 ILE B 166 SER B 168 -1 N ILE B 167 O CYS B 187
SHEET 1 AA6 4 VAL C 33 ARG C 36 0
SHEET 2 AA6 4 GLY C 42 LEU C 46 -1 O THR C 43 N LYS C 35
SHEET 3 AA6 4 LYS C 232 TYR C 246 -1 O ILE C 245 N LEU C 44
SHEET 4 AA6 4 MET C 49 ASN C 54 -1 N TYR C 53 O LEU C 236
SHEET 1 AA7 6 VAL C 33 ARG C 36 0
SHEET 2 AA7 6 GLY C 42 LEU C 46 -1 O THR C 43 N LYS C 35
SHEET 3 AA7 6 LYS C 232 TYR C 246 -1 O ILE C 245 N LEU C 44
SHEET 4 AA7 6 GLU C 195 ASP C 206 1 N GLN C 202 O GLY C 241
SHEET 5 AA7 6 HIS C 184 ALA C 192 -1 N TYR C 190 O SER C 197
SHEET 6 AA7 6 ILE C 166 SER C 168 -1 N ILE C 167 O CYS C 187
SHEET 1 AA8 2 CYS C 266 ILE C 269 0
SHEET 2 AA8 2 PHE C 284 ASP C 287 -1 O ASP C 287 N CYS C 266
SHEET 1 AA9 4 VAL D 33 LYS D 35 0
SHEET 2 AA9 4 THR D 43 LEU D 46 -1 O SER D 45 N VAL D 33
SHEET 3 AA9 4 LYS D 232 TYR D 246 -1 O ILE D 245 N LEU D 44
SHEET 4 AA9 4 MET D 49 ASN D 54 -1 N ALA D 51 O HIS D 238
SHEET 1 AB1 6 VAL D 33 LYS D 35 0
SHEET 2 AB1 6 THR D 43 LEU D 46 -1 O SER D 45 N VAL D 33
SHEET 3 AB1 6 LYS D 232 TYR D 246 -1 O ILE D 245 N LEU D 44
SHEET 4 AB1 6 GLU D 195 ASP D 206 1 N GLN D 202 O GLY D 241
SHEET 5 AB1 6 LEU D 186 ALA D 192 -1 N TYR D 190 O SER D 197
SHEET 6 AB1 6 ILE D 166 SER D 168 -1 N ILE D 167 O CYS D 187
SHEET 1 AB2 2 CYS D 266 ILE D 269 0
SHEET 2 AB2 2 PHE D 284 ASP D 287 -1 O GLN D 285 N LYS D 268
SITE 1 AC1 14 ARG A 38 CYS A 183 HIS A 184 GLN A 202
SITE 2 AC1 14 ARG A 203 SER A 204 GLY A 205 ASP A 206
SITE 3 AC1 14 GLY A 210 ASN A 214 HIS A 244 TYR A 246
SITE 4 AC1 14 ARG B 163 ARG B 164
SITE 1 AC2 11 ARG A 163 ARG A 164 CYS B 183 GLN B 202
SITE 2 AC2 11 ARG B 203 GLY B 205 ASP B 206 ASN B 214
SITE 3 AC2 11 HIS B 244 TYR B 246 HOH B1101
SITE 1 AC3 11 ARG C 38 CYS C 183 ARG C 203 GLY C 205
SITE 2 AC3 11 ASP C 206 GLY C 210 VAL C 211 ASN C 214
SITE 3 AC3 11 TYR C 246 ARG D 163 ARG D 164
SITE 1 AC4 12 ARG C 163 ARG C 164 CYS D 183 HIS D 184
SITE 2 AC4 12 GLN D 202 ARG D 203 SER D 204 GLY D 205
SITE 3 AC4 12 ASP D 206 ASN D 214 HIS D 244 TYR D 246
CRYST1 150.170 150.170 89.160 90.00 90.00 120.00 P 32 12
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 0.006659 0.003845 0.000000 0.00000
SCALE2 0.000000 0.007689 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
