HEADER HYDROLASE/RNA 26-NOV-10 2XZL
TITLE UPF1-RNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT HELICASE NAM7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CH DOMAIN AND HELICASE DOMAIN, RESIDUES 54-850;
COMPND 5 SYNONYM: UP FRAMESHIFT FACTOR 1, NONSENSE-MEDIATED MRNA DECAY PROTEIN
COMPND 6 1, NUCLEAR ACCOMODATION OF MITOCHONDRIA 7 PROTEIN, UP-FRAMESHIFT
COMPND 7 SUPPRESSOR 1;
COMPND 8 EC: 3.6.4.13;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: 5- R(*UP*UP*UP*UP*UP*UP*UP*UP*U) -3;
COMPND 12 CHAIN: B;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630
KEYWDS HYDROLASE-RNA COMPLEX, NMD, RNA DEGRADATION, ALLOSTERIC REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CHAKRABARTI,U.JAYACHANDRAN,F.BONNEAU,F.FIORINI,C.BASQUIN,S.DOMCKE,
AUTHOR 2 H.LE HIR,E.CONTI
REVDAT 2 20-DEC-23 2XZL 1 REMARK LINK
REVDAT 1 30-MAR-11 2XZL 0
JRNL AUTH S.CHAKRABARTI,U.JAYACHANDRAN,F.BONNEAU,F.FIORINI,C.BASQUIN,
JRNL AUTH 2 S.DOMCKE,H.LE HIR,E.CONTI
JRNL TITL MOLECULAR MECHANISMS FOR THE RNA-DEPENDENT ATPASE ACTIVITY
JRNL TITL 2 OF UPF1 AND ITS REGULATION BY UPF2.
JRNL REF MOL.CELL V. 41 693 2011
JRNL REFN ISSN 1097-2765
JRNL PMID 21419344
JRNL DOI 10.1016/J.MOLCEL.2011.02.010
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 41.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 33972
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1725
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 41.8883 - 5.1678 0.94 3174 177 0.1984 0.2275
REMARK 3 2 5.1678 - 4.1030 0.97 3157 204 0.1566 0.1823
REMARK 3 3 4.1030 - 3.5847 0.98 3243 170 0.1750 0.2122
REMARK 3 4 3.5847 - 3.2570 0.98 3215 185 0.2012 0.2488
REMARK 3 5 3.2570 - 3.0237 0.98 3247 175 0.2151 0.3016
REMARK 3 6 3.0237 - 2.8454 0.98 3215 172 0.2235 0.2717
REMARK 3 7 2.8454 - 2.7030 0.98 3265 167 0.2234 0.3128
REMARK 3 8 2.7030 - 2.5853 0.99 3257 160 0.2168 0.2832
REMARK 3 9 2.5853 - 2.4858 0.99 3233 152 0.2106 0.2521
REMARK 3 10 2.4858 - 2.4000 0.99 3241 163 0.2145 0.2687
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 41.69
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27860
REMARK 3 B22 (A**2) : -0.17500
REMARK 3 B33 (A**2) : 0.45360
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.07570
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 : 0.002 6059
REMARK 3 ANGLE : 0.667 8237
REMARK 3 CHIRALITY : 0.047 970
REMARK 3 PLANARITY : 0.003 1002
REMARK 3 DIHEDRAL : 13.700 2208
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: RESIDUES 138-143, 157-159, 213-224 261
REMARK 3 -262 AND 283-291 ARE DISORDERED
REMARK 4
REMARK 4 2XZL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1290046404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : LN2-COOLED DYNAMICALLY BENDABLE
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33993
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 53.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
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) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: PDB ENTRY 2WJV
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES PH 6.0, 200MM AMMONIUM
REMARK 280 ACETATE, 20% PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 57.05850
REMARK 290 SMTRY3 2 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: 7120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.9 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 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 GLY A 49
REMARK 465 ALA A 50
REMARK 465 ALA A 51
REMARK 465 SER A 52
REMARK 465 MET A 53
REMARK 465 SER A 54
REMARK 465 PRO A 55
REMARK 465 SER A 56
REMARK 465 ALA A 57
REMARK 465 SER A 58
REMARK 465 ASP A 59
REMARK 465 ALA A 138
REMARK 465 LYS A 139
REMARK 465 SER A 140
REMARK 465 GLU A 141
REMARK 465 ALA A 142
REMARK 465 VAL A 143
REMARK 465 ASN A 157
REMARK 465 ALA A 158
REMARK 465 ASN A 159
REMARK 465 ILE A 213
REMARK 465 ASN A 214
REMARK 465 ASP A 215
REMARK 465 ILE A 216
REMARK 465 ASP A 217
REMARK 465 ALA A 218
REMARK 465 PRO A 219
REMARK 465 GLU A 220
REMARK 465 GLU A 221
REMARK 465 GLN A 222
REMARK 465 GLU A 223
REMARK 465 ALA A 224
REMARK 465 ALA A 261
REMARK 465 LEU A 262
REMARK 465 LEU A 283
REMARK 465 SER A 284
REMARK 465 THR A 285
REMARK 465 PHE A 286
REMARK 465 GLU A 287
REMARK 465 SER A 288
REMARK 465 ASN A 289
REMARK 465 GLU A 290
REMARK 465 LEU A 291
REMARK 465 SER A 323
REMARK 465 PHE A 324
REMARK 465 GLN A 325
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 68 OD1 OD2
REMARK 470 LYS A 71 CD CE NZ
REMARK 470 ASP A 114 CG OD1 OD2
REMARK 470 VAL A 119 CG1 CG2
REMARK 470 GLU A 121 OE1 OE2
REMARK 470 TYR A 123 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 124 CG OD1 ND2
REMARK 470 LYS A 128 NZ
REMARK 470 VAL A 136 CG1 CG2
REMARK 470 SER A 137 OG
REMARK 470 VAL A 144 CG1 CG2
REMARK 470 THR A 155 OG1 CG2
REMARK 470 LYS A 156 CG CD CE NZ
REMARK 470 TRP A 160 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 160 CZ3 CH2
REMARK 470 ASP A 161 CG OD1 OD2
REMARK 470 THR A 162 OG1 CG2
REMARK 470 ASP A 163 CG OD1 OD2
REMARK 470 GLN A 164 CD OE1 NE2
REMARK 470 GLU A 170 CD OE1 OE2
REMARK 470 ASP A 171 OD1 OD2
REMARK 470 LYS A 187 CE NZ
REMARK 470 ARG A 191 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 ARG A 206 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 208 CG OD1 ND2
REMARK 470 LYS A 209 CD CE NZ
REMARK 470 ASP A 210 CG OD1 OD2
REMARK 470 THR A 212 OG1 CG2
REMARK 470 LEU A 230 CG CD1 CD2
REMARK 470 GLN A 233 CD OE1 NE2
REMARK 470 LEU A 256 CD1 CD2
REMARK 470 LYS A 257 CD CE NZ
REMARK 470 GLU A 258 OE1 OE2
REMARK 470 GLN A 260 CG CD OE1 NE2
REMARK 470 GLU A 263 CD OE1 OE2
REMARK 470 LEU A 271 CD1 CD2
REMARK 470 ASN A 275 OD1 ND2
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 VAL A 293 CG1 CG2
REMARK 470 GLU A 298 OE1 OE2
REMARK 470 GLU A 312 CG CD OE1 OE2
REMARK 470 ARG A 319 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 320 CD1 CD2
REMARK 470 ASN A 322 CG OD1 ND2
REMARK 470 ASP A 326 CG OD1 OD2
REMARK 470 PHE A 328 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 331 CD OE1 OE2
REMARK 470 LYS A 333 CE NZ
REMARK 470 SER A 335 OG
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 THR A 337 OG1 CG2
REMARK 470 GLU A 350 CD OE1 OE2
REMARK 470 ASP A 363 CG OD1 OD2
REMARK 470 LYS A 372 CG CD CE NZ
REMARK 470 GLN A 387 CG CD OE1 NE2
REMARK 470 ASP A 390 CG OD1 OD2
REMARK 470 ASP A 394 CG OD1 OD2
REMARK 470 LYS A 399 CG CD CE NZ
REMARK 470 GLU A 400 CG CD OE1 OE2
REMARK 470 ASN A 405 CG OD1 ND2
REMARK 470 ASN A 415 OD1 ND2
REMARK 470 LYS A 478 CD CE NZ
REMARK 470 ASP A 489 CG OD1 OD2
REMARK 470 GLU A 491 CG CD OE1 OE2
REMARK 470 ASN A 496 OD1 ND2
REMARK 470 ARG A 505 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 508 CG CD CE NZ
REMARK 470 LYS A 512 CG CD CE NZ
REMARK 470 LYS A 516 CE NZ
REMARK 470 LYS A 518 CD CE NZ
REMARK 470 ASP A 519 CG OD1 OD2
REMARK 470 GLU A 520 CD OE1 OE2
REMARK 470 LYS A 530 CG CD CE NZ
REMARK 470 ARG A 531 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 534 CG CD CE NZ
REMARK 470 LYS A 538 CD CE NZ
REMARK 470 GLU A 542 CD OE1 OE2
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 LYS A 560 CG CD CE NZ
REMARK 470 ASP A 563 CG OD1 OD2
REMARK 470 LYS A 565 CG CD CE NZ
REMARK 470 GLU A 573 CD OE1 OE2
REMARK 470 GLU A 581 CD OE1 OE2
REMARK 470 ARG A 609 CD NE CZ NH1 NH2
REMARK 470 LYS A 610 CG CD CE NZ
REMARK 470 LYS A 617 CE NZ
REMARK 470 ARG A 633 CD NE CZ NH1 NH2
REMARK 470 GLU A 654 CD OE1 OE2
REMARK 470 GLU A 664 CG CD OE1 OE2
REMARK 470 LYS A 672 CD CE NZ
REMARK 470 ARG A 690 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 733 CG CD OE1 OE2
REMARK 470 ASP A 752 CG OD1 OD2
REMARK 470 LYS A 756 CE NZ
REMARK 470 GLU A 782 CG CD OE1 OE2
REMARK 470 GLN A 783 CG CD OE1 NE2
REMARK 470 ARG A 790 CD NE CZ NH1 NH2
REMARK 470 ARG A 817 NE CZ NH1 NH2
REMARK 470 GLU A 830 CD OE1 OE2
REMARK 470 ASP A 840 CG OD1 OD2
REMARK 470 GLN A 848 CG CD OE1 NE2
REMARK 470 VAL A 850 CG1 CG2
REMARK 470 U B 9 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 U B 9 C1' N1 C2 O2 N3 C4 O4
REMARK 470 U B 9 C5 C6
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 ASP A 117 90.42 -61.83
REMARK 500 ASN A 124 -81.85 -68.69
REMARK 500 ASP A 210 -164.96 -125.72
REMARK 500 SER A 259 -161.45 -110.11
REMARK 500 HIS A 264 78.23 -118.50
REMARK 500 ASN A 275 31.34 72.47
REMARK 500 PRO A 404 150.23 -48.14
REMARK 500 LEU A 562 59.37 -93.34
REMARK 500 VAL A 587 39.58 -92.00
REMARK 500 VAL A 778 -52.77 75.87
REMARK 500 ALA A 780 104.82 -162.19
REMARK 500 ASN A 841 59.86 -146.43
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 1PE A 1857
REMARK 610 1PE A 1858
REMARK 610 1PE A 1859
REMARK 610 1PE A 1860
REMARK 610 1PE A 1861
REMARK 610 1PE A 1862
REMARK 610 1PE A 1863
REMARK 610 1PE A 1864
REMARK 610 1PE A 1865
REMARK 610 1PE A 1866
REMARK 610 1PE A 1867
REMARK 610 1PE A 1868
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 ZN A1851 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 62 SG
REMARK 620 2 CYS A 65 SG 115.9
REMARK 620 3 CYS A 84 SG 111.2 108.5
REMARK 620 4 HIS A 94 ND1 113.7 111.5 93.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1852 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 76 SG
REMARK 620 2 CYS A 79 SG 107.9
REMARK 620 3 HIS A 98 NE2 115.5 90.2
REMARK 620 4 HIS A 104 ND1 101.1 125.4 117.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1853 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 122 SG
REMARK 620 2 CYS A 125 SG 120.9
REMARK 620 3 CYS A 148 SG 106.4 100.3
REMARK 620 4 CYS A 152 SG 94.3 112.5 124.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1856 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 437 OG1
REMARK 620 2 ADP A1854 O2B 88.1
REMARK 620 3 HOH A2038 O 88.6 171.4
REMARK 620 4 HOH A2047 O 86.1 77.8 94.0
REMARK 620 5 HOH A2090 O 93.4 88.4 99.8 166.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ALF A1855 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A1854 O1B
REMARK 620 2 ALF A1855 F1 93.0
REMARK 620 3 ALF A1855 F2 90.6 89.6
REMARK 620 4 ALF A1855 F3 88.0 90.8 178.5
REMARK 620 5 ALF A1855 F4 88.8 178.3 90.2 89.3
REMARK 620 6 HOH A2051 O 164.1 102.8 91.3 90.0 75.5
REMARK 620 N 1 2 3 4 5
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1851
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1852
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1853
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1854
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 1855
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1856
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1857
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1858
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1859
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1860
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1861
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1862
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1863
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1864
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1865
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1866
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1867
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1868
DBREF 2XZL A 54 850 UNP P30771 NAM7_YEAST 54 850
DBREF 2XZL B 1 9 PDB 2XZL 2XZL 1 9
SEQADV 2XZL GLY A 49 UNP P30771 EXPRESSION TAG
SEQADV 2XZL ALA A 50 UNP P30771 EXPRESSION TAG
SEQADV 2XZL ALA A 51 UNP P30771 EXPRESSION TAG
SEQADV 2XZL SER A 52 UNP P30771 EXPRESSION TAG
SEQADV 2XZL MET A 53 UNP P30771 EXPRESSION TAG
SEQRES 1 A 802 GLY ALA ALA SER MET SER PRO SER ALA SER ASP ASN SER
SEQRES 2 A 802 CYS ALA TYR CYS GLY ILE ASP SER ALA LYS CYS VAL ILE
SEQRES 3 A 802 LYS CYS ASN SER CYS LYS LYS TRP PHE CYS ASN THR LYS
SEQRES 4 A 802 ASN GLY THR SER SER SER HIS ILE VAL ASN HIS LEU VAL
SEQRES 5 A 802 LEU SER HIS HIS ASN VAL VAL SER LEU HIS PRO ASP SER
SEQRES 6 A 802 ASP LEU GLY ASP THR VAL LEU GLU CYS TYR ASN CYS GLY
SEQRES 7 A 802 ARG LYS ASN VAL PHE LEU LEU GLY PHE VAL SER ALA LYS
SEQRES 8 A 802 SER GLU ALA VAL VAL VAL LEU LEU CYS ARG ILE PRO CYS
SEQRES 9 A 802 ALA GLN THR LYS ASN ALA ASN TRP ASP THR ASP GLN TRP
SEQRES 10 A 802 GLN PRO LEU ILE GLU ASP ARG GLN LEU LEU SER TRP VAL
SEQRES 11 A 802 ALA GLU GLN PRO THR GLU GLU GLU LYS LEU LYS ALA ARG
SEQRES 12 A 802 LEU ILE THR PRO SER GLN ILE SER LYS LEU GLU ALA LYS
SEQRES 13 A 802 TRP ARG SER ASN LYS ASP ALA THR ILE ASN ASP ILE ASP
SEQRES 14 A 802 ALA PRO GLU GLU GLN GLU ALA ILE PRO PRO LEU LEU LEU
SEQRES 15 A 802 ARG TYR GLN ASP ALA TYR GLU TYR GLN ARG SER TYR GLY
SEQRES 16 A 802 PRO LEU ILE LYS LEU GLU ALA ASP TYR ASP LYS GLN LEU
SEQRES 17 A 802 LYS GLU SER GLN ALA LEU GLU HIS ILE SER VAL SER TRP
SEQRES 18 A 802 SER LEU ALA LEU ASN ASN ARG HIS LEU ALA SER PHE THR
SEQRES 19 A 802 LEU SER THR PHE GLU SER ASN GLU LEU LYS VAL ALA ILE
SEQRES 20 A 802 GLY ASP GLU MET ILE LEU TRP TYR SER GLY MET GLN HIS
SEQRES 21 A 802 PRO ASP TRP GLU GLY ARG GLY TYR ILE VAL ARG LEU PRO
SEQRES 22 A 802 ASN SER PHE GLN ASP THR PHE THR LEU GLU LEU LYS PRO
SEQRES 23 A 802 SER LYS THR PRO PRO PRO THR HIS LEU THR THR GLY PHE
SEQRES 24 A 802 THR ALA GLU PHE ILE TRP LYS GLY THR SER TYR ASP ARG
SEQRES 25 A 802 MET GLN ASP ALA LEU LYS LYS PHE ALA ILE ASP LYS LYS
SEQRES 26 A 802 SER ILE SER GLY TYR LEU TYR TYR LYS ILE LEU GLY HIS
SEQRES 27 A 802 GLN VAL VAL ASP ILE SER PHE ASP VAL PRO LEU PRO LYS
SEQRES 28 A 802 GLU PHE SER ILE PRO ASN PHE ALA GLN LEU ASN SER SER
SEQRES 29 A 802 GLN SER ASN ALA VAL SER HIS VAL LEU GLN ARG PRO LEU
SEQRES 30 A 802 SER LEU ILE GLN GLY PRO PRO GLY THR GLY LYS THR VAL
SEQRES 31 A 802 THR SER ALA THR ILE VAL TYR HIS LEU SER LYS ILE HIS
SEQRES 32 A 802 LYS ASP ARG ILE LEU VAL CYS ALA PRO SER ASN VAL ALA
SEQRES 33 A 802 VAL ASP HIS LEU ALA ALA LYS LEU ARG ASP LEU GLY LEU
SEQRES 34 A 802 LYS VAL VAL ARG LEU THR ALA LYS SER ARG GLU ASP VAL
SEQRES 35 A 802 GLU SER SER VAL SER ASN LEU ALA LEU HIS ASN LEU VAL
SEQRES 36 A 802 GLY ARG GLY ALA LYS GLY GLU LEU LYS ASN LEU LEU LYS
SEQRES 37 A 802 LEU LYS ASP GLU VAL GLY GLU LEU SER ALA SER ASP THR
SEQRES 38 A 802 LYS ARG PHE VAL LYS LEU VAL ARG LYS THR GLU ALA GLU
SEQRES 39 A 802 ILE LEU ASN LYS ALA ASP VAL VAL CYS CYS THR CYS VAL
SEQRES 40 A 802 GLY ALA GLY ASP LYS ARG LEU ASP THR LYS PHE ARG THR
SEQRES 41 A 802 VAL LEU ILE ASP GLU SER THR GLN ALA SER GLU PRO GLU
SEQRES 42 A 802 CYS LEU ILE PRO ILE VAL LYS GLY ALA LYS GLN VAL ILE
SEQRES 43 A 802 LEU VAL GLY ASP HIS GLN GLN LEU GLY PRO VAL ILE LEU
SEQRES 44 A 802 GLU ARG LYS ALA ALA ASP ALA GLY LEU LYS GLN SER LEU
SEQRES 45 A 802 PHE GLU ARG LEU ILE SER LEU GLY HIS VAL PRO ILE ARG
SEQRES 46 A 802 LEU GLU VAL GLN TYR ARG MET ASN PRO TYR LEU SER GLU
SEQRES 47 A 802 PHE PRO SER ASN MET PHE TYR GLU GLY SER LEU GLN ASN
SEQRES 48 A 802 GLY VAL THR ILE GLU GLN ARG THR VAL PRO ASN SER LYS
SEQRES 49 A 802 PHE PRO TRP PRO ILE ARG GLY ILE PRO MET MET PHE TRP
SEQRES 50 A 802 ALA ASN TYR GLY ARG GLU GLU ILE SER ALA ASN GLY THR
SEQRES 51 A 802 SER PHE LEU ASN ARG ILE GLU ALA MET ASN CYS GLU ARG
SEQRES 52 A 802 ILE ILE THR LYS LEU PHE ARG ASP GLY VAL LYS PRO GLU
SEQRES 53 A 802 GLN ILE GLY VAL ILE THR PRO TYR GLU GLY GLN ARG ALA
SEQRES 54 A 802 TYR ILE LEU GLN TYR MET GLN MET ASN GLY SER LEU ASP
SEQRES 55 A 802 LYS ASP LEU TYR ILE LYS VAL GLU VAL ALA SER VAL ASP
SEQRES 56 A 802 ALA PHE GLN GLY ARG GLU LYS ASP TYR ILE ILE LEU SER
SEQRES 57 A 802 CYS VAL ARG ALA ASN GLU GLN GLN ALA ILE GLY PHE LEU
SEQRES 58 A 802 ARG ASP PRO ARG ARG LEU ASN VAL GLY LEU THR ARG ALA
SEQRES 59 A 802 LYS TYR GLY LEU VAL ILE LEU GLY ASN PRO ARG SER LEU
SEQRES 60 A 802 ALA ARG ASN THR LEU TRP ASN HIS LEU LEU ILE HIS PHE
SEQRES 61 A 802 ARG GLU LYS GLY CYS LEU VAL GLU GLY THR LEU ASP ASN
SEQRES 62 A 802 LEU GLN LEU CYS THR VAL GLN LEU VAL
SEQRES 1 B 9 U U U U U U U U U
HET ZN A1851 1
HET ZN A1852 1
HET ZN A1853 1
HET ADP A1854 27
HET ALF A1855 5
HET MG A1856 1
HET 1PE A1857 10
HET 1PE A1858 13
HET 1PE A1859 7
HET 1PE A1860 7
HET 1PE A1861 10
HET 1PE A1862 7
HET 1PE A1863 7
HET 1PE A1864 7
HET 1PE A1865 7
HET 1PE A1866 7
HET 1PE A1867 7
HET 1PE A1868 7
HETNAM ZN ZINC ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM ALF TETRAFLUOROALUMINATE ION
HETNAM MG MAGNESIUM ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 ZN 3(ZN 2+)
FORMUL 6 ADP C10 H15 N5 O10 P2
FORMUL 7 ALF AL F4 1-
FORMUL 8 MG MG 2+
FORMUL 9 1PE 12(C10 H22 O6)
FORMUL 21 HOH *96(H2 O)
HELIX 1 1 SER A 93 HIS A 103 1 11
HELIX 2 2 ASP A 161 TRP A 165 5 5
HELIX 3 3 GLU A 185 ALA A 190 5 6
HELIX 4 4 THR A 194 ARG A 206 1 13
HELIX 5 5 ASP A 234 GLU A 258 1 25
HELIX 6 6 GLY A 355 ASP A 371 1 17
HELIX 7 7 SER A 376 GLY A 385 1 10
HELIX 8 8 ASN A 410 LEU A 421 1 12
HELIX 9 9 GLY A 435 LYS A 452 1 18
HELIX 10 10 SER A 461 LEU A 475 1 15
HELIX 11 11 ALA A 484 GLU A 488 5 5
HELIX 12 12 VAL A 494 LEU A 497 5 4
HELIX 13 13 ALA A 498 ARG A 505 1 8
HELIX 14 14 GLY A 509 GLY A 522 1 14
HELIX 15 15 SER A 525 LYS A 546 1 22
HELIX 16 16 VAL A 555 ASP A 559 5 5
HELIX 17 17 GLU A 573 ALA A 577 5 5
HELIX 18 18 SER A 578 VAL A 587 1 10
HELIX 19 19 GLU A 608 ALA A 614 1 7
HELIX 20 20 SER A 619 LEU A 627 1 9
HELIX 21 21 ASN A 641 TYR A 653 1 13
HELIX 22 22 ASN A 702 ASP A 719 1 18
HELIX 23 23 LYS A 722 GLU A 724 5 3
HELIX 24 24 TYR A 732 GLY A 747 1 16
HELIX 25 25 ASP A 750 LYS A 756 1 7
HELIX 26 26 VAL A 762 GLN A 766 1 5
HELIX 27 27 ILE A 786 ARG A 790 5 5
HELIX 28 28 ASP A 791 THR A 800 1 10
HELIX 29 29 ASN A 811 ALA A 816 1 6
HELIX 30 30 ASN A 818 GLY A 832 1 15
SHEET 1 AA 3 TRP A 82 CYS A 84 0
SHEET 2 AA 3 VAL A 73 CYS A 76 -1 O ILE A 74 N PHE A 83
SHEET 3 AA 3 VAL A 107 LEU A 109 -1 O SER A 108 N LYS A 75
SHEET 1 AB 3 VAL A 145 CYS A 148 0
SHEET 2 AB 3 LEU A 133 VAL A 136 -1 O GLY A 134 N LEU A 147
SHEET 3 AB 3 GLN A 166 PRO A 167 -1 O GLN A 166 N PHE A 135
SHEET 1 AC 6 VAL A 267 LEU A 271 0
SHEET 2 AC 6 HIS A 277 PHE A 281 -1 O LEU A 278 N SER A 270
SHEET 3 AC 6 PHE A 328 LEU A 332 -1 O PHE A 328 N PHE A 281
SHEET 4 AC 6 TRP A 311 ARG A 319 -1 O TYR A 316 N GLU A 331
SHEET 5 AC 6 GLU A 298 TYR A 303 -1 O MET A 299 N GLY A 315
SHEET 6 AC 6 PHE A 347 PHE A 351 -1 O THR A 348 N TRP A 302
SHEET 1 AD 7 VAL A 479 ARG A 481 0
SHEET 2 AD 7 VAL A 549 THR A 553 1 O VAL A 549 N VAL A 480
SHEET 3 AD 7 ILE A 455 ALA A 459 1 O ILE A 455 N VAL A 550
SHEET 4 AD 7 THR A 568 ILE A 571 1 O THR A 568 N LEU A 456
SHEET 5 AD 7 GLN A 592 GLY A 597 1 O GLN A 592 N VAL A 569
SHEET 6 AD 7 LEU A 425 GLN A 429 1 O SER A 426 N LEU A 595
SHEET 7 AD 7 ILE A 632 ARG A 633 1 O ILE A 632 N GLN A 429
SHEET 1 AE 2 VAL A 636 GLN A 637 0
SHEET 2 AE 2 GLN A 658 ASN A 659 1 O GLN A 658 N GLN A 637
SHEET 1 AF 7 GLU A 758 SER A 761 0
SHEET 2 AF 7 ILE A 726 THR A 730 1 O ILE A 726 N GLU A 758
SHEET 3 AF 7 LYS A 770 SER A 776 1 O TYR A 772 N GLY A 727
SHEET 4 AF 7 ALA A 802 GLY A 810 1 N LYS A 803 O LYS A 770
SHEET 5 AF 7 MET A 682 ALA A 686 1 O MET A 683 N ILE A 808
SHEET 6 AF 7 LEU A 834 THR A 838 1 O VAL A 835 N ALA A 686
SHEET 7 AF 7 ASN A 841 LEU A 844 -1 O ASN A 841 N THR A 838
SHEET 1 AG 2 GLU A 692 ILE A 693 0
SHEET 2 AG 2 PHE A 700 LEU A 701 -1 O LEU A 701 N GLU A 692
LINK SG CYS A 62 ZN ZN A1851 1555 1555 2.47
LINK SG CYS A 65 ZN ZN A1851 1555 1555 2.57
LINK SG CYS A 76 ZN ZN A1852 1555 1555 2.52
LINK SG CYS A 79 ZN ZN A1852 1555 1555 2.66
LINK SG CYS A 84 ZN ZN A1851 1555 1555 2.56
LINK ND1 HIS A 94 ZN ZN A1851 1555 1555 2.20
LINK NE2 HIS A 98 ZN ZN A1852 1555 1555 2.21
LINK ND1 HIS A 104 ZN ZN A1852 1555 1555 2.27
LINK SG CYS A 122 ZN ZN A1853 1555 1555 2.66
LINK SG CYS A 125 ZN ZN A1853 1555 1555 2.59
LINK SG CYS A 148 ZN ZN A1853 1555 1555 2.65
LINK SG CYS A 152 ZN ZN A1853 1555 1555 2.56
LINK OG1 THR A 437 MG MG A1856 1555 1555 2.40
LINK O1B ADP A1854 AL ALF A1855 1555 1555 2.16
LINK O2B ADP A1854 MG MG A1856 1555 1555 2.52
LINK AL ALF A1855 O HOH A2051 1555 1555 2.25
LINK MG MG A1856 O HOH A2038 1555 1555 2.55
LINK MG MG A1856 O HOH A2047 1555 1555 2.77
LINK MG MG A1856 O HOH A2090 1555 1555 2.51
CISPEP 1 ILE A 150 PRO A 151 0 3.43
SITE 1 AC1 4 CYS A 62 CYS A 65 CYS A 84 HIS A 94
SITE 1 AC2 4 CYS A 76 CYS A 79 HIS A 98 HIS A 104
SITE 1 AC3 4 CYS A 122 CYS A 125 CYS A 148 CYS A 152
SITE 1 AC4 15 GLN A 408 GLN A 413 GLY A 433 THR A 434
SITE 2 AC4 15 GLY A 435 LYS A 436 THR A 437 VAL A 438
SITE 3 AC4 15 TYR A 638 ARG A 639 GLU A 769 ALF A1855
SITE 4 AC4 15 MG A1856 HOH A2090 HOH A2091
SITE 1 AC5 11 PRO A 432 GLY A 433 LYS A 436 GLN A 601
SITE 2 AC5 11 ARG A 639 GLY A 767 ARG A 801 ADP A1854
SITE 3 AC5 11 MG A1856 HOH A2047 HOH A2051
SITE 1 AC6 6 THR A 437 ADP A1854 ALF A1855 HOH A2038
SITE 2 AC6 6 HOH A2047 HOH A2090
SITE 1 AC7 3 GLY A 377 TYR A 381 ARG A 678
SITE 1 AC8 5 GLY A 720 LYS A 722 GLN A 725 ASP A 771
SITE 2 AC8 5 TYR A 804
SITE 1 AC9 10 ALA A 369 ILE A 370 SER A 671 LYS A 672
SITE 2 AC9 10 PHE A 673 TRP A 675 PRO A 676 ILE A 677
SITE 3 AC9 10 ARG A 678 1PE A1863
SITE 1 BC1 5 PHE A 647 ASN A 650 MET A 651 HIS A 823
SITE 2 BC1 5 HIS A 827
SITE 1 BC2 3 GLN A 362 ASN A 841 GLN A 843
SITE 1 BC3 7 ARG A 829 LEU A 834 LEU A 844 CYS A 845
SITE 2 BC3 7 VAL A 847 LEU A 849 HOH A2086
SITE 1 BC4 9 ASN A 641 ILE A 663 THR A 667 TRP A 675
SITE 2 BC4 9 ILE A 677 GLY A 679 ILE A 680 PRO A 681
SITE 3 BC4 9 1PE A1859
SITE 1 BC5 9 HIS A 419 ARG A 423 LEU A 425 SER A 426
SITE 2 BC5 9 LEU A 427 HIS A 629 VAL A 630 PRO A 631
SITE 3 BC5 9 ILE A 632
SITE 1 BC6 5 PHE A 393 HIS A 451 ASP A 453 LYS A 591
SITE 2 BC6 5 GLN A 592
SITE 1 BC7 5 SER A 412 ASN A 415 ALA A 416 ILE A 632
SITE 2 BC7 5 ARG A 633
SITE 1 BC8 5 LYS A 367 ASP A 371 LYS A 373 THR A 564
SITE 2 BC8 5 LYS A 588
SITE 1 BC9 4 LYS A 372 ILE A 375 SER A 376 GLY A 589
CRYST1 64.135 114.117 65.730 90.00 110.24 90.00 P 1 21 1 2
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 0.015592 0.000000 0.005749 0.00000
SCALE2 0.000000 0.008763 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016215 0.00000
(ATOM LINES ARE NOT SHOWN.)
END