HEADER TRANSFERASE 14-JUL-17 5XZV
TITLE CRYSTAL STRUCTURE OF RAD53 1-466 IN COMPLEX WITH AMP-PNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE RAD53;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-466;
COMPND 5 SYNONYM: CHEK2 HOMOLOG,SERINE-PROTEIN KINASE 1;
COMPND 6 EC: 2.7.12.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: RAD53, MEC2, SAD1, SPK1, YPL153C, P2588;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE/THREONINE-PROTEIN KINASE, FHA DOMAIN, CHECKPOINT KINASE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.WENG,M.D.TSAI
REVDAT 2 27-MAR-24 5XZV 1 REMARK
REVDAT 1 11-OCT-17 5XZV 0
JRNL AUTH E.S.CHEN,J.H.WENG,Y.H.CHEN,S.C.WANG,X.X.LIU,W.C.HUANG,
JRNL AUTH 2 T.MATSUI,Y.KAWANO,J.H.LIAO,L.H.LIM,Y.BESSHO,K.F.HUANG,
JRNL AUTH 3 W.J.WU,M.D.TSAI
JRNL TITL PHOSPHO-PRIMING CONFERS FUNCTIONALLY RELEVANT SPECIFICITIES
JRNL TITL 2 FOR RAD53 KINASE AUTOPHOSPHORYLATION
JRNL REF BIOCHEMISTRY V. 56 5112 2017
JRNL REFN ISSN 1520-4995
JRNL PMID 28858528
JRNL DOI 10.1021/ACS.BIOCHEM.7B00689
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 3 NUMBER OF REFLECTIONS : 17877
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.273
REMARK 3 R VALUE (WORKING SET) : 0.272
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 902
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 28.8843 - 5.6221 1.00 3405 161 0.2572 0.2552
REMARK 3 2 5.6221 - 4.4677 1.00 3258 177 0.2529 0.2679
REMARK 3 3 4.4677 - 3.9045 1.00 3231 173 0.2635 0.2709
REMARK 3 4 3.9045 - 3.5482 1.00 3240 171 0.2935 0.3349
REMARK 3 5 3.5482 - 3.2943 0.78 2486 141 0.3179 0.3448
REMARK 3 6 3.2943 - 3.1003 0.43 1355 79 0.3300 0.3744
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.30
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 : 0.011 5519
REMARK 3 ANGLE : 1.668 7494
REMARK 3 CHIRALITY : 0.089 906
REMARK 3 PLANARITY : 0.010 953
REMARK 3 DIHEDRAL : 16.391 1888
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 5XZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300004404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-16; 24-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 110; 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSRRC; SPRING-8
REMARK 200 BEAMLINE : BL15A1; BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000; 1.00000
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; PIXEL
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE; DECTRIS
REMARK 200 PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20517
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 0.84800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM CACODYLATE BUFFER, 0.4M NACL,
REMARK 280 1.5M (NH4)2SO4, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 93.86933
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 46.93467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.93467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 93.86933
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 3
REMARK 465 ILE A 4
REMARK 465 THR A 5
REMARK 465 GLN A 6
REMARK 465 PRO A 7
REMARK 465 THR A 8
REMARK 465 GLN A 9
REMARK 465 GLN A 10
REMARK 465 SER A 11
REMARK 465 THR A 12
REMARK 465 GLN A 13
REMARK 465 ALA A 14
REMARK 465 THR A 15
REMARK 465 GLY A 79
REMARK 465 ASN A 80
REMARK 465 ILE A 81
REMARK 465 SER A 82
REMARK 465 ARG A 83
REMARK 465 LEU A 84
REMARK 465 GLY A 135
REMARK 465 VAL A 136
REMARK 465 GLU A 137
REMARK 465 SER A 165
REMARK 465 ASN A 166
REMARK 465 LEU A 167
REMARK 465 LYS A 168
REMARK 465 ASN A 169
REMARK 465 THR A 170
REMARK 465 SER A 171
REMARK 465 LYS A 172
REMARK 465 ILE A 173
REMARK 465 ALA A 174
REMARK 465 SER A 175
REMARK 465 PRO A 176
REMARK 465 GLY A 177
REMARK 465 LEU A 178
REMARK 465 THR A 179
REMARK 465 SER A 180
REMARK 465 SER A 181
REMARK 465 THR A 182
REMARK 465 ALA A 183
REMARK 465 SER A 184
REMARK 465 SER A 185
REMARK 465 MET A 186
REMARK 465 VAL A 187
REMARK 465 ALA A 188
REMARK 465 ASN A 189
REMARK 465 VAL A 345
REMARK 465 GLN A 346
REMARK 465 GLY A 347
REMARK 465 ASN A 348
REMARK 465 GLY A 349
REMARK 465 SER A 350
REMARK 465 PHE A 351
REMARK 465 MET A 352
REMARK 465 LYS A 353
REMARK 465 THR A 354
REMARK 465 PHE A 355
REMARK 465 CYS A 356
REMARK 465 GLY A 357
REMARK 465 THR A 358
REMARK 465 ARG A 368
REMARK 465 GLY A 369
REMARK 465 LYS A 370
REMARK 465 ASP A 371
REMARK 465 THR A 372
REMARK 465 SER A 373
REMARK 465 VAL A 374
REMARK 465 SER A 375
REMARK 465 PRO A 376
REMARK 465 ASP A 377
REMARK 465 GLU A 378
REMARK 465 TYR A 379
REMARK 465 GLU A 380
REMARK 465 GLU A 381
REMARK 465 ARG A 382
REMARK 465 SER A 409
REMARK 465 GLY A 410
REMARK 465 TYR A 425
REMARK 465 HIS A 426
REMARK 465 GLU A 427
REMARK 465 GLY A 428
REMARK 465 PRO A 429
REMARK 465 LEU A 447
REMARK 465 GLN A 448
REMARK 465 VAL A 449
REMARK 465 ARG A 454
REMARK 465 SER A 455
REMARK 465 ILE A 466
REMARK 465 VAL A 467
REMARK 465 ASP A 468
REMARK 465 SER A 469
REMARK 465 SER A 470
REMARK 465 ASN A 471
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASN B 3
REMARK 465 ILE B 4
REMARK 465 THR B 5
REMARK 465 GLN B 6
REMARK 465 PRO B 7
REMARK 465 THR B 8
REMARK 465 GLN B 9
REMARK 465 GLN B 10
REMARK 465 SER B 11
REMARK 465 THR B 12
REMARK 465 GLN B 13
REMARK 465 ALA B 14
REMARK 465 THR B 15
REMARK 465 GLN B 16
REMARK 465 ARG B 17
REMARK 465 PHE B 18
REMARK 465 LEU B 19
REMARK 465 ILE B 20
REMARK 465 GLU B 21
REMARK 465 LYS B 22
REMARK 465 PHE B 23
REMARK 465 SER B 24
REMARK 465 GLN B 25
REMARK 465 GLU B 26
REMARK 465 GLN B 27
REMARK 465 ILE B 28
REMARK 465 GLY B 29
REMARK 465 GLU B 30
REMARK 465 ASN B 31
REMARK 465 GLY B 135
REMARK 465 VAL B 136
REMARK 465 GLU B 137
REMARK 465 SER B 138
REMARK 465 ASP B 139
REMARK 465 ASN B 158
REMARK 465 LYS B 159
REMARK 465 VAL B 160
REMARK 465 ASP B 161
REMARK 465 ARG B 162
REMARK 465 ILE B 163
REMARK 465 ARG B 164
REMARK 465 SER B 165
REMARK 465 ASN B 166
REMARK 465 LEU B 167
REMARK 465 LYS B 168
REMARK 465 ASN B 169
REMARK 465 THR B 170
REMARK 465 SER B 171
REMARK 465 LYS B 172
REMARK 465 ILE B 173
REMARK 465 ALA B 174
REMARK 465 SER B 175
REMARK 465 PRO B 176
REMARK 465 GLY B 177
REMARK 465 LEU B 178
REMARK 465 THR B 179
REMARK 465 SER B 180
REMARK 465 SER B 181
REMARK 465 THR B 182
REMARK 465 ALA B 183
REMARK 465 SER B 184
REMARK 465 SER B 185
REMARK 465 MET B 186
REMARK 465 VAL B 187
REMARK 465 ALA B 188
REMARK 465 VAL B 234
REMARK 465 ILE B 235
REMARK 465 GLY B 236
REMARK 465 ASN B 237
REMARK 465 ALA B 343
REMARK 465 LYS B 344
REMARK 465 VAL B 345
REMARK 465 GLN B 346
REMARK 465 GLY B 347
REMARK 465 ASN B 348
REMARK 465 GLY B 349
REMARK 465 SER B 350
REMARK 465 PHE B 351
REMARK 465 MET B 352
REMARK 465 LYS B 353
REMARK 465 GLY B 369
REMARK 465 LYS B 370
REMARK 465 ASP B 371
REMARK 465 THR B 372
REMARK 465 SER B 373
REMARK 465 VAL B 374
REMARK 465 SER B 375
REMARK 465 PRO B 376
REMARK 465 ASP B 377
REMARK 465 GLU B 378
REMARK 465 TYR B 379
REMARK 465 GLU B 380
REMARK 465 GLU B 381
REMARK 465 ARG B 382
REMARK 465 ASP B 468
REMARK 465 SER B 469
REMARK 465 SER B 470
REMARK 465 ASN B 471
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 GLN A 16 CG CD OE1 NE2
REMARK 470 ARG A 17 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 18 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 20 CG1 CG2 CD1
REMARK 470 GLU A 21 CG CD OE1 OE2
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 PHE A 23 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 26 CG CD OE1 OE2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 ARG A 70 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 87 CG CD CE NZ
REMARK 470 THR A 106 OG1 CG2
REMARK 470 ASN A 107 CG OD1 ND2
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 GLU A 117 CG CD OE1 OE2
REMARK 470 LYS A 118 CG CD CE NZ
REMARK 470 GLN A 153 CG CD OE1 NE2
REMARK 470 GLN A 157 CG CD OE1 NE2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 VAL A 160 CG1 CG2
REMARK 470 ASP A 161 CG OD1 OD2
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 164 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 GLU A 202 CG CD OE1 OE2
REMARK 470 PHE A 284 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A 288 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 293 CG CD OE1 OE2
REMARK 470 ASP A 294 CG OD1 OD2
REMARK 470 ARG A 297 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 LYS A 308 CG CD CE NZ
REMARK 470 ARG A 318 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 329 CG CD OE1 NE2
REMARK 470 ASP A 331 CG OD1 OD2
REMARK 470 VAL A 333 CG1 CG2
REMARK 470 LEU A 342 CG CD1 CD2
REMARK 470 LYS A 344 CG CD CE NZ
REMARK 470 LEU A 359 CG CD1 CD2
REMARK 470 GLU A 365 CG CD OE1 OE2
REMARK 470 VAL A 366 CG1 CG2
REMARK 470 ILE A 367 CG1 CG2 CD1
REMARK 470 ASN A 383 CG OD1 ND2
REMARK 470 GLU A 384 CG CD OE1 OE2
REMARK 470 TYR A 385 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 392 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 392 CZ3 CH2
REMARK 470 TYR A 399 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 402 CG CD1 CD2
REMARK 470 LEU A 406 CG CD1 CD2
REMARK 470 PHE A 408 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 411 OG
REMARK 470 THR A 412 OG1 CG2
REMARK 470 ASP A 414 CG OD1 OD2
REMARK 470 GLN A 415 CG CD OE1 NE2
REMARK 470 LEU A 416 CG CD1 CD2
REMARK 470 TYR A 417 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 418 CG CD CE NZ
REMARK 470 GLN A 419 CG CD OE1 NE2
REMARK 470 ILE A 420 CG1 CG2 CD1
REMARK 470 ARG A 422 CG CD NE CZ NH1 NH2
REMARK 470 SER A 424 OG
REMARK 470 LEU A 430 CG CD1 CD2
REMARK 470 LYS A 431 CG CD CE NZ
REMARK 470 ASP A 432 CG OD1 OD2
REMARK 470 PHE A 433 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 434 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 435 CG1 CG2 CD1
REMARK 470 GLU A 437 CG CD OE1 OE2
REMARK 470 GLU A 438 CG CD OE1 OE2
REMARK 470 ARG A 440 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 441 CG OD1 OD2
REMARK 470 PHE A 442 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 443 CG1 CG2 CD1
REMARK 470 ASP A 444 CG OD1 OD2
REMARK 470 LEU A 446 CG CD1 CD2
REMARK 470 ASP A 450 CG OD1 OD2
REMARK 470 ASN A 452 CG OD1 ND2
REMARK 470 ASN A 453 CG OD1 ND2
REMARK 470 THR A 456 OG1 CG2
REMARK 470 LYS A 459 CG CD CE NZ
REMARK 470 LEU A 461 CG CD1 CD2
REMARK 470 ASN A 462 CG OD1 ND2
REMARK 470 HIS A 463 CG ND1 CD2 CE1 NE2
REMARK 470 TRP A 465 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 465 CZ3 CH2
REMARK 470 ILE B 32 CG1 CG2 CD1
REMARK 470 GLN B 42 CG CD OE1 NE2
REMARK 470 ILE B 43 CG1 CG2 CD1
REMARK 470 GLN B 54 CG CD OE1 NE2
REMARK 470 GLU B 58 CG CD OE1 OE2
REMARK 470 LYS B 59 CG CD CE NZ
REMARK 470 GLN B 114 CG CD OE1 NE2
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 LYS B 118 CG CD CE NZ
REMARK 470 ASP B 128 CG OD1 OD2
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 VAL B 134 CG1 CG2
REMARK 470 LYS B 150 CG CD CE NZ
REMARK 470 GLN B 153 CG CD OE1 NE2
REMARK 470 CYS B 154 SG
REMARK 470 LEU B 155 CG CD1 CD2
REMARK 470 GLU B 156 CG CD OE1 OE2
REMARK 470 GLN B 157 CG CD OE1 NE2
REMARK 470 ASN B 189 CG OD1 ND2
REMARK 470 LYS B 190 CG CD CE NZ
REMARK 470 VAL B 204 CG1 CG2
REMARK 470 GLN B 206 CG CD OE1 NE2
REMARK 470 PHE B 209 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 232 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 233 CG CD CE NZ
REMARK 470 MET B 238 CG SD CE
REMARK 470 ARG B 243 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 248 CG CD1 CD2
REMARK 470 LYS B 250 CG CD CE NZ
REMARK 470 GLN B 329 CG CD OE1 NE2
REMARK 470 ASP B 330 CG OD1 OD2
REMARK 470 ASP B 331 CG OD1 OD2
REMARK 470 ASP B 339 CG OD1 OD2
REMARK 470 LEU B 342 CG CD1 CD2
REMARK 470 THR B 354 OG1 CG2
REMARK 470 PHE B 355 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 368 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 383 CG OD1 ND2
REMARK 470 GLU B 384 CG CD OE1 OE2
REMARK 470 LYS B 418 CG CD CE NZ
REMARK 470 LYS B 431 CG CD CE NZ
REMARK 470 ARG B 434 CG CD NE CZ NH1 NH2
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 OD1 ASP B 319 NZ LYS B 321 1.56
REMARK 500 O HIS A 317 OD1 ASP A 390 1.66
REMARK 500 O HIS A 88 O ILE A 104 1.85
REMARK 500 OD2 ASP A 196 OH TYR A 263 2.05
REMARK 500 O GLN A 413 N TYR A 417 2.09
REMARK 500 OD2 ASP B 265 OH TYR B 270 2.13
REMARK 500 O SER A 436 N ARG A 440 2.17
REMARK 500 SG CYS B 38 CD1 LEU B 141 2.17
REMARK 500 OD1 ASN B 252 NH2 ARG B 258 2.18
REMARK 500 OE2 GLU B 117 N ASN B 189 2.18
REMARK 500 O SER A 436 N ALA A 439 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 332 C - N - CD ANGL. DEV. = -16.9 DEGREES
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 LYS A 64 145.79 175.94
REMARK 500 ARG A 70 -128.31 60.76
REMARK 500 ASN A 119 1.13 55.94
REMARK 500 GLU A 202 104.98 -47.50
REMARK 500 THR A 338 -53.40 -121.20
REMARK 500 GLN B 42 -128.16 58.82
REMARK 500 ALA B 50 100.95 -170.54
REMARK 500 PRO B 72 2.33 -68.28
REMARK 500 SER B 105 178.50 -57.10
REMARK 500 VAL B 116 156.70 -49.60
REMARK 500 ASN B 119 -4.36 71.07
REMARK 500 ASN B 148 86.80 -66.88
REMARK 500 VAL B 203 50.81 -105.45
REMARK 500 THR B 220 -27.95 -144.87
REMARK 500 HIS B 253 140.41 -170.98
REMARK 500 ARG B 255 33.38 -83.59
REMARK 500 SER B 268 153.21 177.82
REMARK 500 GLU B 274 113.49 -39.30
REMARK 500 ARG B 318 -6.40 73.76
REMARK 500 ASP B 319 57.83 -152.96
REMARK 500 ASP B 339 62.64 66.26
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 ANP B 501
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 501
DBREF 5XZV A 1 466 UNP P22216 RAD53_YEAST 1 466
DBREF 5XZV B 1 466 UNP P22216 RAD53_YEAST 1 466
SEQADV 5XZV VAL A 467 UNP P22216 EXPRESSION TAG
SEQADV 5XZV ASP A 468 UNP P22216 EXPRESSION TAG
SEQADV 5XZV SER A 469 UNP P22216 EXPRESSION TAG
SEQADV 5XZV SER A 470 UNP P22216 EXPRESSION TAG
SEQADV 5XZV ASN A 471 UNP P22216 EXPRESSION TAG
SEQADV 5XZV VAL B 467 UNP P22216 EXPRESSION TAG
SEQADV 5XZV ASP B 468 UNP P22216 EXPRESSION TAG
SEQADV 5XZV SER B 469 UNP P22216 EXPRESSION TAG
SEQADV 5XZV SER B 470 UNP P22216 EXPRESSION TAG
SEQADV 5XZV ASN B 471 UNP P22216 EXPRESSION TAG
SEQRES 1 A 471 MET GLU ASN ILE THR GLN PRO THR GLN GLN SER THR GLN
SEQRES 2 A 471 ALA THR GLN ARG PHE LEU ILE GLU LYS PHE SER GLN GLU
SEQRES 3 A 471 GLN ILE GLY GLU ASN ILE VAL CYS ARG VAL ILE CYS THR
SEQRES 4 A 471 THR GLY GLN ILE PRO ILE ARG ASP LEU SER ALA ASP ILE
SEQRES 5 A 471 SER GLN VAL LEU LYS GLU LYS ARG SER ILE LYS LYS VAL
SEQRES 6 A 471 TRP THR PHE GLY ARG ASN PRO ALA CYS ASP TYR HIS LEU
SEQRES 7 A 471 GLY ASN ILE SER ARG LEU SER ASN LYS HIS PHE GLN ILE
SEQRES 8 A 471 LEU LEU GLY GLU ASP GLY ASN LEU LEU LEU ASN ASP ILE
SEQRES 9 A 471 SER THR ASN GLY THR TRP LEU ASN GLY GLN LYS VAL GLU
SEQRES 10 A 471 LYS ASN SER ASN GLN LEU LEU SER GLN GLY ASP GLU ILE
SEQRES 11 A 471 THR VAL GLY VAL GLY VAL GLU SER ASP ILE LEU SER LEU
SEQRES 12 A 471 VAL ILE PHE ILE ASN ASP LYS PHE LYS GLN CYS LEU GLU
SEQRES 13 A 471 GLN ASN LYS VAL ASP ARG ILE ARG SER ASN LEU LYS ASN
SEQRES 14 A 471 THR SER LYS ILE ALA SER PRO GLY LEU THR SER SER THR
SEQRES 15 A 471 ALA SER SER MET VAL ALA ASN LYS THR GLY ILE PHE LYS
SEQRES 16 A 471 ASP PHE SER ILE ILE ASP GLU VAL VAL GLY GLN GLY ALA
SEQRES 17 A 471 PHE ALA THR VAL LYS LYS ALA ILE GLU ARG THR THR GLY
SEQRES 18 A 471 LYS THR PHE ALA VAL LYS ILE ILE SER LYS ARG LYS VAL
SEQRES 19 A 471 ILE GLY ASN MET ASP GLY VAL THR ARG GLU LEU GLU VAL
SEQRES 20 A 471 LEU GLN LYS LEU ASN HIS PRO ARG ILE VAL ARG LEU LYS
SEQRES 21 A 471 GLY PHE TYR GLU ASP THR GLU SER TYR TYR MET VAL MET
SEQRES 22 A 471 GLU PHE VAL SER GLY GLY ASP LEU MET ASP PHE VAL ALA
SEQRES 23 A 471 ALA HIS GLY ALA VAL GLY GLU ASP ALA GLY ARG GLU ILE
SEQRES 24 A 471 SER ARG GLN ILE LEU THR ALA ILE LYS TYR ILE HIS SER
SEQRES 25 A 471 MET GLY ILE SER HIS ARG ASP LEU LYS PRO ASP ASN ILE
SEQRES 26 A 471 LEU ILE GLU GLN ASP ASP PRO VAL LEU VAL LYS ILE THR
SEQRES 27 A 471 ASP PHE GLY LEU ALA LYS VAL GLN GLY ASN GLY SER PHE
SEQRES 28 A 471 MET LYS THR PHE CYS GLY THR LEU ALA TYR VAL ALA PRO
SEQRES 29 A 471 GLU VAL ILE ARG GLY LYS ASP THR SER VAL SER PRO ASP
SEQRES 30 A 471 GLU TYR GLU GLU ARG ASN GLU TYR SER SER LEU VAL ASP
SEQRES 31 A 471 MET TRP SER MET GLY CYS LEU VAL TYR VAL ILE LEU THR
SEQRES 32 A 471 GLY HIS LEU PRO PHE SER GLY SER THR GLN ASP GLN LEU
SEQRES 33 A 471 TYR LYS GLN ILE GLY ARG GLY SER TYR HIS GLU GLY PRO
SEQRES 34 A 471 LEU LYS ASP PHE ARG ILE SER GLU GLU ALA ARG ASP PHE
SEQRES 35 A 471 ILE ASP SER LEU LEU GLN VAL ASP PRO ASN ASN ARG SER
SEQRES 36 A 471 THR ALA ALA LYS ALA LEU ASN HIS PRO TRP ILE VAL ASP
SEQRES 37 A 471 SER SER ASN
SEQRES 1 B 471 MET GLU ASN ILE THR GLN PRO THR GLN GLN SER THR GLN
SEQRES 2 B 471 ALA THR GLN ARG PHE LEU ILE GLU LYS PHE SER GLN GLU
SEQRES 3 B 471 GLN ILE GLY GLU ASN ILE VAL CYS ARG VAL ILE CYS THR
SEQRES 4 B 471 THR GLY GLN ILE PRO ILE ARG ASP LEU SER ALA ASP ILE
SEQRES 5 B 471 SER GLN VAL LEU LYS GLU LYS ARG SER ILE LYS LYS VAL
SEQRES 6 B 471 TRP THR PHE GLY ARG ASN PRO ALA CYS ASP TYR HIS LEU
SEQRES 7 B 471 GLY ASN ILE SER ARG LEU SER ASN LYS HIS PHE GLN ILE
SEQRES 8 B 471 LEU LEU GLY GLU ASP GLY ASN LEU LEU LEU ASN ASP ILE
SEQRES 9 B 471 SER THR ASN GLY THR TRP LEU ASN GLY GLN LYS VAL GLU
SEQRES 10 B 471 LYS ASN SER ASN GLN LEU LEU SER GLN GLY ASP GLU ILE
SEQRES 11 B 471 THR VAL GLY VAL GLY VAL GLU SER ASP ILE LEU SER LEU
SEQRES 12 B 471 VAL ILE PHE ILE ASN ASP LYS PHE LYS GLN CYS LEU GLU
SEQRES 13 B 471 GLN ASN LYS VAL ASP ARG ILE ARG SER ASN LEU LYS ASN
SEQRES 14 B 471 THR SER LYS ILE ALA SER PRO GLY LEU THR SER SER THR
SEQRES 15 B 471 ALA SER SER MET VAL ALA ASN LYS THR GLY ILE PHE LYS
SEQRES 16 B 471 ASP PHE SER ILE ILE ASP GLU VAL VAL GLY GLN GLY ALA
SEQRES 17 B 471 PHE ALA THR VAL LYS LYS ALA ILE GLU ARG THR THR GLY
SEQRES 18 B 471 LYS THR PHE ALA VAL LYS ILE ILE SER LYS ARG LYS VAL
SEQRES 19 B 471 ILE GLY ASN MET ASP GLY VAL THR ARG GLU LEU GLU VAL
SEQRES 20 B 471 LEU GLN LYS LEU ASN HIS PRO ARG ILE VAL ARG LEU LYS
SEQRES 21 B 471 GLY PHE TYR GLU ASP THR GLU SER TYR TYR MET VAL MET
SEQRES 22 B 471 GLU PHE VAL SER GLY GLY ASP LEU MET ASP PHE VAL ALA
SEQRES 23 B 471 ALA HIS GLY ALA VAL GLY GLU ASP ALA GLY ARG GLU ILE
SEQRES 24 B 471 SER ARG GLN ILE LEU THR ALA ILE LYS TYR ILE HIS SER
SEQRES 25 B 471 MET GLY ILE SER HIS ARG ASP LEU LYS PRO ASP ASN ILE
SEQRES 26 B 471 LEU ILE GLU GLN ASP ASP PRO VAL LEU VAL LYS ILE THR
SEQRES 27 B 471 ASP PHE GLY LEU ALA LYS VAL GLN GLY ASN GLY SER PHE
SEQRES 28 B 471 MET LYS THR PHE CYS GLY THR LEU ALA TYR VAL ALA PRO
SEQRES 29 B 471 GLU VAL ILE ARG GLY LYS ASP THR SER VAL SER PRO ASP
SEQRES 30 B 471 GLU TYR GLU GLU ARG ASN GLU TYR SER SER LEU VAL ASP
SEQRES 31 B 471 MET TRP SER MET GLY CYS LEU VAL TYR VAL ILE LEU THR
SEQRES 32 B 471 GLY HIS LEU PRO PHE SER GLY SER THR GLN ASP GLN LEU
SEQRES 33 B 471 TYR LYS GLN ILE GLY ARG GLY SER TYR HIS GLU GLY PRO
SEQRES 34 B 471 LEU LYS ASP PHE ARG ILE SER GLU GLU ALA ARG ASP PHE
SEQRES 35 B 471 ILE ASP SER LEU LEU GLN VAL ASP PRO ASN ASN ARG SER
SEQRES 36 B 471 THR ALA ALA LYS ALA LEU ASN HIS PRO TRP ILE VAL ASP
SEQRES 37 B 471 SER SER ASN
HET ANP A 501 31
HET ANP B 501 19
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 3 ANP 2(C10 H17 N6 O12 P3)
HELIX 1 AA1 GLN A 16 PHE A 23 1 8
HELIX 2 AA2 ASP A 51 GLU A 58 1 8
HELIX 3 AA3 GLU A 95 GLY A 97 5 3
HELIX 4 AA4 ASN A 148 ARG A 164 1 17
HELIX 5 AA5 LYS A 231 ILE A 235 1 5
HELIX 6 AA6 ASN A 237 GLN A 249 1 13
HELIX 7 AA7 ASP A 280 GLY A 289 1 10
HELIX 8 AA8 GLY A 292 MET A 313 1 22
HELIX 9 AA9 LYS A 321 ASP A 323 5 3
HELIX 10 AB1 ALA A 363 ILE A 367 5 5
HELIX 11 AB2 GLU A 384 THR A 403 1 20
HELIX 12 AB3 THR A 412 GLY A 423 1 12
HELIX 13 AB4 SER A 436 ASP A 444 1 9
HELIX 14 AB5 ALA A 457 HIS A 463 1 7
HELIX 15 AB6 ASP B 51 LYS B 57 1 7
HELIX 16 AB7 ASN B 148 GLN B 157 1 10
HELIX 17 AB8 THR B 191 LYS B 195 5 5
HELIX 18 AB9 ASP B 239 LEU B 251 1 13
HELIX 19 AC1 ASP B 280 GLY B 289 1 10
HELIX 20 AC2 GLY B 292 MET B 313 1 22
HELIX 21 AC3 LYS B 321 ASP B 323 5 3
HELIX 22 AC4 THR B 358 VAL B 362 5 5
HELIX 23 AC5 ALA B 363 ARG B 368 5 6
HELIX 24 AC6 GLU B 384 GLY B 404 1 21
HELIX 25 AC7 THR B 412 ARG B 422 1 11
HELIX 26 AC8 HIS B 426 PHE B 433 1 8
HELIX 27 AC9 SER B 436 LEU B 447 1 12
HELIX 28 AD1 ASP B 450 ARG B 454 5 5
HELIX 29 AD2 THR B 456 ASN B 462 1 7
SHEET 1 AA1 6 ARG A 46 SER A 49 0
SHEET 2 AA1 6 ILE A 32 CYS A 38 -1 N CYS A 34 O LEU A 48
SHEET 3 AA1 6 ILE A 140 ILE A 147 -1 O PHE A 146 N ARG A 35
SHEET 4 AA1 6 GLU A 129 GLY A 133 -1 N VAL A 132 O LEU A 141
SHEET 5 AA1 6 THR A 109 LEU A 111 -1 N TRP A 110 O THR A 131
SHEET 6 AA1 6 GLN A 114 LYS A 115 -1 O GLN A 114 N LEU A 111
SHEET 1 AA2 4 LYS A 64 PHE A 68 0
SHEET 2 AA2 4 HIS A 88 LEU A 93 -1 O LEU A 93 N LYS A 64
SHEET 3 AA2 4 LEU A 99 ILE A 104 -1 O ASN A 102 N GLN A 90
SHEET 4 AA2 4 GLN A 122 LEU A 124 -1 O GLN A 122 N LEU A 101
SHEET 1 AA3 5 PHE A 197 GLN A 206 0
SHEET 2 AA3 5 ALA A 210 GLU A 217 -1 O ILE A 216 N SER A 198
SHEET 3 AA3 5 THR A 223 SER A 230 -1 O PHE A 224 N ALA A 215
SHEET 4 AA3 5 SER A 268 GLU A 274 -1 O MET A 271 N LYS A 227
SHEET 5 AA3 5 LEU A 259 GLU A 264 -1 N TYR A 263 O TYR A 270
SHEET 1 AA4 2 ILE A 325 GLN A 329 0
SHEET 2 AA4 2 LEU A 334 ILE A 337 -1 O LYS A 336 N LEU A 326
SHEET 1 AA5 6 ARG B 46 LEU B 48 0
SHEET 2 AA5 6 CYS B 34 CYS B 38 -1 N VAL B 36 O ARG B 46
SHEET 3 AA5 6 LEU B 143 ILE B 147 -1 O VAL B 144 N ILE B 37
SHEET 4 AA5 6 GLU B 129 THR B 131 -1 N ILE B 130 O LEU B 143
SHEET 5 AA5 6 TRP B 110 LEU B 111 -1 N TRP B 110 O THR B 131
SHEET 6 AA5 6 GLN B 114 LYS B 115 -1 O GLN B 114 N LEU B 111
SHEET 1 AA6 5 TYR B 76 HIS B 77 0
SHEET 2 AA6 5 LYS B 64 GLY B 69 1 N THR B 67 O TYR B 76
SHEET 3 AA6 5 PHE B 89 LEU B 93 -1 O ILE B 91 N TRP B 66
SHEET 4 AA6 5 LEU B 99 ASP B 103 -1 O ASN B 102 N GLN B 90
SHEET 5 AA6 5 ASN B 121 LEU B 124 -1 O GLN B 122 N LEU B 101
SHEET 1 AA7 5 PHE B 197 ILE B 199 0
SHEET 2 AA7 5 ALA B 210 GLU B 217 -1 O ILE B 216 N SER B 198
SHEET 3 AA7 5 THR B 223 ILE B 229 -1 O PHE B 224 N ALA B 215
SHEET 4 AA7 5 TYR B 269 GLU B 274 -1 O MET B 273 N ALA B 225
SHEET 5 AA7 5 LEU B 259 GLU B 264 -1 N GLY B 261 O VAL B 272
SHEET 1 AA8 2 ILE B 325 GLN B 329 0
SHEET 2 AA8 2 LEU B 334 ILE B 337 -1 O LYS B 336 N LEU B 326
SITE 1 AC1 12 GLY A 205 PHE A 209 ALA A 210 VAL A 212
SITE 2 AC1 12 ALA A 225 LYS A 227 ILE A 229 GLU A 244
SITE 3 AC1 12 GLU A 274 VAL A 276 ASP A 280 ASP A 339
SITE 1 AC2 8 GLY B 205 ALA B 225 GLU B 274 PHE B 275
SITE 2 AC2 8 VAL B 276 ASP B 280 ASP B 323 LEU B 326
CRYST1 116.690 116.690 140.804 90.00 90.00 120.00 P 32 2 1 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 0.008570 0.004948 0.000000 0.00000
SCALE2 0.000000 0.009895 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
