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HEADER BIOSYNTHETIC PROTEIN 19-NOV-24 9KNK
TITLE CRYSTAL STRUCTURE OF FULL-LENGTH PHA SYNTHASE (PHAC) FROM AEROMONAS
TITLE 2 CAVIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHA SYNTHASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROMONAS CAVIAE;
SOURCE 3 ORGANISM_TAXID: 648;
SOURCE 4 GENE: PHAC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHA SYNTHASE, FULL-LENGTH PHAC, DIMER, TUNNEL, CATALYTIC TRIAD,
KEYWDS 2 POLYHYDROXYALKANOATES, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.CHEK,S.Y.KIM,T.MORI,T.HAKOSHIMA
REVDAT 1 21-MAY-25 9KNK 0
JRNL AUTH M.F.CHEK,S.Y.KIM,T.MORI,K.MATSUMOTO,S.SATO,T.HAKOSHIMA
JRNL TITL STRUCTURES OF POLYHYDROXYALKANOATE SYNTHASE PHAC FROM
JRNL TITL 2 AEROMONAS CAVIAE, PRODUCING BIODEGRADABLE PLASTICS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 04626 2025
JRNL REFN ESSN 1521-3773
JRNL PMID 40276819
JRNL DOI 10.1002/ANIE.202504626
REMARK 2
REMARK 2 RESOLUTION. 3.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 31877
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1592
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 47.6600 - 7.3200 0.97 2814 149 0.1621 0.1828
REMARK 3 2 7.3100 - 5.8100 0.98 2765 145 0.2169 0.2204
REMARK 3 3 5.8100 - 5.0800 0.99 2760 146 0.1952 0.2780
REMARK 3 4 5.0800 - 4.6100 0.98 2736 144 0.1727 0.2134
REMARK 3 5 4.6100 - 4.2800 0.99 2792 147 0.1761 0.2238
REMARK 3 6 4.2800 - 4.0300 0.99 2734 142 0.1945 0.2758
REMARK 3 7 4.0300 - 3.8300 0.99 2767 146 0.2080 0.2697
REMARK 3 8 3.8300 - 3.6600 0.99 2758 144 0.2243 0.2615
REMARK 3 9 3.6600 - 3.5200 0.99 2763 146 0.2458 0.3165
REMARK 3 10 3.5200 - 3.4000 1.00 2761 144 0.2429 0.2982
REMARK 3 11 3.4000 - 3.2900 0.94 2635 139 0.2739 0.3143
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) : 0.393
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.036
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 111.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 116.0
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 : 0.003 12574
REMARK 3 ANGLE : 0.585 17165
REMARK 3 CHIRALITY : 0.040 1948
REMARK 3 PLANARITY : 0.004 2218
REMARK 3 DIHEDRAL : 4.013 1700
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 : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 6 through 18 or
REMARK 3 (resid 19 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 20
REMARK 3 through 22 or (resid 23 through 27 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 28 through 29 or
REMARK 3 (resid 30 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 31
REMARK 3 through 41 or resid 54 through 75 or
REMARK 3 (resid 76 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 77
REMARK 3 through 78 or resid 105 through 111 or
REMARK 3 (resid 112 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 113
REMARK 3 through 129 or (resid 130 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 131 through 133 or (resid 134
REMARK 3 through 135 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 136 or (resid 137 through 140 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 141 through 144 or (resid 145
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 146 through 161
REMARK 3 or (resid 162 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 163 through 167 or resid 172 through 176
REMARK 3 or (resid 177 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 178 through 186 or (resid 187 through 188
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 189 through 190
REMARK 3 or (resid 191 through 192 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 193 through 194 or resid 202
REMARK 3 through 203 or (resid 204 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 205 through 206 or (resid 207
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 208 through 220
REMARK 3 or (resid 221 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 222 through 236 or (resid 237 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 238 through 248 or (resid 249
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 250 through 283
REMARK 3 or (resid 284 through 285 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 286 through 304 or (resid 305
REMARK 3 through 307 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 308 through 310 or (resid 311 through 312
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 313 through 328
REMARK 3 or (resid 329 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 330 through 334 or (resid 335 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 336 through 341 or (resid 342
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 343 through 358
REMARK 3 or resid 361 through 370 or (resid 371
REMARK 3 through 374 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 375 through 395 or resid 397 through 406
REMARK 3 or (resid 407 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 408 or (resid 409 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 410 through 451 or (resid 452 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 453 or (resid 454 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 455 through 456 or
REMARK 3 resid 458 or (resid 459 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 460 through 461 or (resid 462
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 463 or (resid
REMARK 3 464 and (name N or name CA or name C or
REMARK 3 name O or name CB )) or resid 465 through
REMARK 3 487 or (resid 488 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 489 through 494 or (resid 495 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 496 through 499 or
REMARK 3 (resid 500 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 501
REMARK 3 through 514 or (resid 515 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 516 through 521 or resid 525
REMARK 3 through 544 or (resid 545 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 546 through 552 or (resid 553
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 558 through 583))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 6 through 69 or
REMARK 3 (resid 70 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 71
REMARK 3 through 119 or (resid 120 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 121 through 126 or (resid 127
REMARK 3 through 128 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 129 or (resid 130 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 131 through 144 or (resid 145 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 146 through 161 or
REMARK 3 (resid 162 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 163
REMARK 3 through 167 or resid 172 through 183 or
REMARK 3 (resid 184 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 185
REMARK 3 through 186 or (resid 187 through 188 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 189 through 190 or
REMARK 3 (resid 191 through 192 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 193 through 194 or resid 202
REMARK 3 through 203 or (resid 204 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 205 through 206 or (resid 207
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 208 through 220
REMARK 3 or (resid 221 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 222 through 248 or (resid 249 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 250 through 257 or (resid 258
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 259 through 283
REMARK 3 or (resid 284 through 285 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 286 through 304 or (resid 305
REMARK 3 through 307 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 308 through 311 or (resid 312 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 313 through 328 or (resid 329
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 330 through 334
REMARK 3 or (resid 335 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 336 through 337 or (resid 338 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 339 through 341 or (resid 342
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 343 through 358
REMARK 3 or resid 361 through 370 or (resid 371
REMARK 3 through 374 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 375 or (resid 376 through 378 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 379 through 395 or resid 397
REMARK 3 through 430 or (resid 431 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 432 through 453 or (resid 454
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 455 through 456
REMARK 3 or resid 458 through 499 or (resid 500
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 501 through 521
REMARK 3 or resid 525 through 552 or (resid 553
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or (resid 558 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 559 through 565 or (resid 566
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 567 through 583))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and (resid 6 through 22 or
REMARK 3 (resid 23 through 27 and (name N or name
REMARK 3 CA or name C or name O or name CB )) or
REMARK 3 resid 28 through 29 or (resid 30 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 31 through 41 or
REMARK 3 resid 54 through 75 or (resid 76 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 77 through 78 or
REMARK 3 resid 105 through 119 or (resid 120 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 121 through 126 or
REMARK 3 (resid 127 through 128 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 129 through 139 or (resid 140
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 141 through 194
REMARK 3 or resid 202 through 257 or (resid 258
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 259 through 310
REMARK 3 or (resid 311 through 312 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 313 through 337 or (resid 338
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 339 through 375
REMARK 3 or (resid 376 through 378 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 379 through 406 or (resid 407
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 408 or (resid
REMARK 3 409 and (name N or name CA or name C or
REMARK 3 name O or name CB )) or resid 410 through
REMARK 3 430 or (resid 431 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 432 through 458 or (resid 459 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 460 through 461 or
REMARK 3 (resid 462 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 463 or
REMARK 3 (resid 464 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 465
REMARK 3 through 487 or (resid 488 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 489 through 514 or (resid 515
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 516 through 544
REMARK 3 or (resid 545 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 546 through 553 or (resid 558 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 559 through 565 or (resid 566
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 567 through 583))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9KNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1300053603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999994
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31906
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.290
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.41
REMARK 200 R MERGE FOR SHELL (I) : 0.50800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, GLYCEROL, PEG6000,
REMARK 280 OCTYL BETA-D-GLUCOPYRANOSIDE, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 78.31600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.31600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.15000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 PRO A 4
REMARK 465 LEU A 43
REMARK 465 GLY A 44
REMARK 465 GLN A 45
REMARK 465 VAL A 46
REMARK 465 LEU A 47
REMARK 465 GLU A 48
REMARK 465 GLN A 49
REMARK 465 GLY A 50
REMARK 465 ALA A 80
REMARK 465 GLY A 81
REMARK 465 GLN A 82
REMARK 465 PRO A 83
REMARK 465 SER A 84
REMARK 465 GLU A 85
REMARK 465 PRO A 86
REMARK 465 VAL A 87
REMARK 465 ILE A 88
REMARK 465 THR A 89
REMARK 465 PRO A 90
REMARK 465 GLU A 91
REMARK 465 ARG A 92
REMARK 465 SER A 93
REMARK 465 ASP A 94
REMARK 465 ARG A 95
REMARK 465 ARG A 96
REMARK 465 PHE A 97
REMARK 465 LYS A 98
REMARK 465 ALA A 99
REMARK 465 GLU A 100
REMARK 465 ALA A 101
REMARK 465 TRP A 102
REMARK 465 SER A 103
REMARK 465 SER A 170
REMARK 465 ASP A 171
REMARK 465 THR A 198
REMARK 465 ASP A 199
REMARK 465 GLU A 200
REMARK 465 SER A 201
REMARK 465 GLU A 555
REMARK 465 GLY A 556
REMARK 465 ALA A 586
REMARK 465 CYS A 587
REMARK 465 PRO A 588
REMARK 465 THR A 589
REMARK 465 GLU A 590
REMARK 465 GLU A 591
REMARK 465 ASP A 592
REMARK 465 ALA A 593
REMARK 465 ALA A 594
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 PRO B 4
REMARK 465 SER B 5
REMARK 465 ASP B 42
REMARK 465 LEU B 43
REMARK 465 GLY B 44
REMARK 465 GLN B 45
REMARK 465 VAL B 46
REMARK 465 LEU B 47
REMARK 465 GLU B 48
REMARK 465 GLN B 49
REMARK 465 GLY B 50
REMARK 465 SER B 51
REMARK 465 GLN B 52
REMARK 465 GLN B 53
REMARK 465 SER B 79
REMARK 465 ALA B 80
REMARK 465 GLY B 81
REMARK 465 GLN B 82
REMARK 465 PRO B 83
REMARK 465 SER B 84
REMARK 465 GLU B 85
REMARK 465 PRO B 86
REMARK 465 VAL B 87
REMARK 465 ILE B 88
REMARK 465 THR B 89
REMARK 465 PRO B 90
REMARK 465 GLU B 91
REMARK 465 ARG B 92
REMARK 465 SER B 93
REMARK 465 ASP B 94
REMARK 465 ARG B 95
REMARK 465 ARG B 96
REMARK 465 PHE B 97
REMARK 465 LYS B 98
REMARK 465 ALA B 99
REMARK 465 GLU B 100
REMARK 465 ALA B 101
REMARK 465 TRP B 102
REMARK 465 SER B 103
REMARK 465 GLU B 104
REMARK 465 GLU B 169
REMARK 465 SER B 170
REMARK 465 ILE B 195
REMARK 465 ARG B 196
REMARK 465 LEU B 197
REMARK 465 THR B 198
REMARK 465 ASP B 554
REMARK 465 GLU B 555
REMARK 465 GLY B 556
REMARK 465 ALA B 586
REMARK 465 CYS B 587
REMARK 465 PRO B 588
REMARK 465 THR B 589
REMARK 465 GLU B 590
REMARK 465 GLU B 591
REMARK 465 ASP B 592
REMARK 465 ALA B 593
REMARK 465 ALA B 594
REMARK 465 GLY C -1
REMARK 465 PRO C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 3
REMARK 465 PRO C 4
REMARK 465 GLY C 44
REMARK 465 GLN C 45
REMARK 465 VAL C 46
REMARK 465 LEU C 47
REMARK 465 GLU C 48
REMARK 465 GLN C 49
REMARK 465 GLY C 50
REMARK 465 SER C 51
REMARK 465 ALA C 80
REMARK 465 GLY C 81
REMARK 465 GLN C 82
REMARK 465 PRO C 83
REMARK 465 SER C 84
REMARK 465 GLU C 85
REMARK 465 PRO C 86
REMARK 465 VAL C 87
REMARK 465 ILE C 88
REMARK 465 THR C 89
REMARK 465 PRO C 90
REMARK 465 GLU C 91
REMARK 465 ARG C 92
REMARK 465 SER C 93
REMARK 465 ASP C 94
REMARK 465 ARG C 95
REMARK 465 ARG C 96
REMARK 465 PHE C 97
REMARK 465 LYS C 98
REMARK 465 ALA C 99
REMARK 465 GLU C 100
REMARK 465 ALA C 101
REMARK 465 TRP C 102
REMARK 465 SER C 103
REMARK 465 LEU C 168
REMARK 465 GLU C 169
REMARK 465 SER C 170
REMARK 465 ASP C 171
REMARK 465 LEU C 197
REMARK 465 THR C 198
REMARK 465 ASP C 199
REMARK 465 GLU C 200
REMARK 465 LEU C 359
REMARK 465 GLY C 360
REMARK 465 ASN C 396
REMARK 465 ARG C 457
REMARK 465 GLY C 522
REMARK 465 ALA C 523
REMARK 465 GLU C 524
REMARK 465 GLU C 555
REMARK 465 GLY C 556
REMARK 465 SER C 557
REMARK 465 VAL C 584
REMARK 465 PHE C 585
REMARK 465 ALA C 586
REMARK 465 CYS C 587
REMARK 465 PRO C 588
REMARK 465 THR C 589
REMARK 465 GLU C 590
REMARK 465 GLU C 591
REMARK 465 ASP C 592
REMARK 465 ALA C 593
REMARK 465 ALA C 594
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 LYS A 70 CG CD CE NZ
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 ARG A 120 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 127 CG OD1 OD2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 GLN A 258 CG CD OE1 NE2
REMARK 470 GLU A 312 CG CD OE1 OE2
REMARK 470 LYS A 338 CG CD CE NZ
REMARK 470 GLU A 376 CG CD OE1 OE2
REMARK 470 LYS A 378 CG CD CE NZ
REMARK 470 LYS A 431 CG CD CE NZ
REMARK 470 GLU A 524 CG CD OE1 OE2
REMARK 470 GLU A 558 CG CD OE1 OE2
REMARK 470 GLU A 566 CG CD OE1 OE2
REMARK 470 LYS B 19 CG CD CE NZ
REMARK 470 MET B 23 CG SD CE
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 GLN B 27 CG CD OE1 NE2
REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 76 CG CD1 CD2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 LYS B 112 CG CD CE NZ
REMARK 470 GLN B 134 CG CD OE1 NE2
REMARK 470 LYS B 135 CG CD CE NZ
REMARK 470 ARG B 137 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 470 ARG B 139 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 140 CG CD1 CD2
REMARK 470 LYS B 165 CG CD CE NZ
REMARK 470 ARG B 177 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 188 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 237 CG CD CE NZ
REMARK 470 ARG B 311 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 378 CG CD CE NZ
REMARK 470 TYR B 407 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 409 CG CD CE NZ
REMARK 470 LYS B 452 CG CD CE NZ
REMARK 470 ARG B 457 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 459 CG OD1 OD2
REMARK 470 LYS B 462 CG CD CE NZ
REMARK 470 LYS B 464 CG CD CE NZ
REMARK 470 LYS B 488 CG CD CE NZ
REMARK 470 ARG B 495 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 515 CG CD CE NZ
REMARK 470 GLU B 524 CG CD OE1 OE2
REMARK 470 GLU B 545 CG CD OE1 OE2
REMARK 470 LYS C 19 CG CD CE NZ
REMARK 470 LYS C 25 CG CD CE NZ
REMARK 470 LYS C 70 CG CD CE NZ
REMARK 470 LYS C 78 CG CD CE NZ
REMARK 470 GLU C 104 CG CD OE1 OE2
REMARK 470 LYS C 112 CG CD CE NZ
REMARK 470 GLU C 130 CG CD OE1 OE2
REMARK 470 GLN C 134 CG CD OE1 NE2
REMARK 470 LYS C 135 CG CD CE NZ
REMARK 470 ARG C 137 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 138 CG CD OE1 OE2
REMARK 470 ARG C 139 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 145 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 162 CG CD OE1 OE2
REMARK 470 LYS C 165 CG CD CE NZ
REMARK 470 ARG C 177 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 184 CG CD OE1 OE2
REMARK 470 GLU C 187 CG CD OE1 OE2
REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 191 CG OD1 OD2
REMARK 470 GLN C 192 CG CD OE1 NE2
REMARK 470 ARG C 196 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 204 CG CD OE1 OE2
REMARK 470 ARG C 207 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 221 CG CD OE1 OE2
REMARK 470 LYS C 237 CG CD CE NZ
REMARK 470 LYS C 249 CG CD CE NZ
REMARK 470 GLN C 284 CG CD OE1 NE2
REMARK 470 GLU C 305 CG CD OE1 OE2
REMARK 470 GLU C 312 CG CD OE1 OE2
REMARK 470 MET C 329 CG SD CE
REMARK 470 ARG C 335 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 342 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 371 CG CD1 CD2
REMARK 470 GLU C 372 CG CD OE1 OE2
REMARK 470 GLN C 374 CG CD OE1 NE2
REMARK 470 LYS C 378 CG CD CE NZ
REMARK 470 LYS C 452 CG CD CE NZ
REMARK 470 ARG C 454 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 495 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 500 CG CD OE1 OE2
REMARK 470 ARG C 553 CG CD NE CZ NH1 NH2
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 GLN A 37 46.44 -93.52
REMARK 500 LEU A 40 -51.87 63.94
REMARK 500 LEU A 129 31.59 -87.91
REMARK 500 MET A 255 -68.00 -96.32
REMARK 500 GLN A 284 33.54 -90.95
REMARK 500 TYR A 318 -146.35 -107.93
REMARK 500 GLU A 500 49.07 -93.57
REMARK 500 SER A 501 -158.87 -166.78
REMARK 500 TYR A 516 -156.33 -128.87
REMARK 500 GLU B 200 48.11 -88.29
REMARK 500 TYR B 251 8.25 -69.73
REMARK 500 MET B 255 -67.47 -96.61
REMARK 500 TYR B 318 -145.14 -109.29
REMARK 500 GLU B 500 48.64 -93.32
REMARK 500 SER B 501 -160.09 -166.21
REMARK 500 TYR B 516 -158.61 -128.58
REMARK 500 GLN C 37 59.43 -98.82
REMARK 500 LEU C 40 48.77 -93.87
REMARK 500 ASP C 41 14.49 -156.67
REMARK 500 LEU C 129 31.09 -86.99
REMARK 500 ALA C 202 -139.57 -145.15
REMARK 500 MET C 255 -65.92 -96.72
REMARK 500 TYR C 318 -150.72 -106.33
REMARK 500 GLU C 500 48.96 -91.93
REMARK 500 SER C 501 -160.78 -165.77
REMARK 500 TYR C 516 -160.01 -128.61
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9KNK A 1 594 UNP O32471 O32471_AERCA 1 594
DBREF 9KNK B 1 594 UNP O32471 O32471_AERCA 1 594
DBREF 9KNK C 1 594 UNP O32471 O32471_AERCA 1 594
SEQADV 9KNK GLY A -1 UNP O32471 EXPRESSION TAG
SEQADV 9KNK PRO A 0 UNP O32471 EXPRESSION TAG
SEQADV 9KNK GLY B -1 UNP O32471 EXPRESSION TAG
SEQADV 9KNK PRO B 0 UNP O32471 EXPRESSION TAG
SEQADV 9KNK GLY C -1 UNP O32471 EXPRESSION TAG
SEQADV 9KNK PRO C 0 UNP O32471 EXPRESSION TAG
SEQRES 1 A 596 GLY PRO MET SER GLN PRO SER TYR GLY PRO LEU PHE GLU
SEQRES 2 A 596 ALA LEU ALA HIS TYR ASN ASP LYS LEU LEU ALA MET ALA
SEQRES 3 A 596 LYS ALA GLN THR GLU ARG THR ALA GLN ALA LEU LEU GLN
SEQRES 4 A 596 THR ASN LEU ASP ASP LEU GLY GLN VAL LEU GLU GLN GLY
SEQRES 5 A 596 SER GLN GLN PRO TRP GLN LEU ILE GLN ALA GLN MET ASN
SEQRES 6 A 596 TRP TRP GLN ASP GLN LEU LYS LEU MET GLN HIS THR LEU
SEQRES 7 A 596 LEU LYS SER ALA GLY GLN PRO SER GLU PRO VAL ILE THR
SEQRES 8 A 596 PRO GLU ARG SER ASP ARG ARG PHE LYS ALA GLU ALA TRP
SEQRES 9 A 596 SER GLU GLN PRO ILE TYR ASP TYR LEU LYS GLN SER TYR
SEQRES 10 A 596 LEU LEU THR ALA ARG HIS LEU LEU ALA SER VAL ASP ALA
SEQRES 11 A 596 LEU GLU GLY VAL PRO GLN LYS SER ARG GLU ARG LEU ARG
SEQRES 12 A 596 PHE PHE THR ARG GLN TYR VAL ASN ALA MET ALA PRO SER
SEQRES 13 A 596 ASN PHE LEU ALA THR ASN PRO GLU LEU LEU LYS LEU THR
SEQRES 14 A 596 LEU GLU SER ASP GLY GLN ASN LEU VAL ARG GLY LEU ALA
SEQRES 15 A 596 LEU LEU ALA GLU ASP LEU GLU ARG SER ALA ASP GLN LEU
SEQRES 16 A 596 ASN ILE ARG LEU THR ASP GLU SER ALA PHE GLU LEU GLY
SEQRES 17 A 596 ARG ASP LEU ALA LEU THR PRO GLY ARG VAL VAL GLN ARG
SEQRES 18 A 596 THR GLU LEU TYR GLU LEU ILE GLN TYR SER PRO THR THR
SEQRES 19 A 596 GLU THR VAL GLY LYS THR PRO VAL LEU ILE VAL PRO PRO
SEQRES 20 A 596 PHE ILE ASN LYS TYR TYR ILE MET ASP MET ARG PRO GLN
SEQRES 21 A 596 ASN SER LEU VAL ALA TRP LEU VAL ALA GLN GLY GLN THR
SEQRES 22 A 596 VAL PHE MET ILE SER TRP ARG ASN PRO GLY VAL ALA GLN
SEQRES 23 A 596 ALA GLN ILE ASP LEU ASP ASP TYR VAL VAL ASP GLY VAL
SEQRES 24 A 596 ILE ALA ALA LEU ASP GLY VAL GLU ALA ALA THR GLY GLU
SEQRES 25 A 596 ARG GLU VAL HIS GLY ILE GLY TYR CYS ILE GLY GLY THR
SEQRES 26 A 596 ALA LEU SER LEU ALA MET GLY TRP LEU ALA ALA ARG ARG
SEQRES 27 A 596 GLN LYS GLN ARG VAL ARG THR ALA THR LEU PHE THR THR
SEQRES 28 A 596 LEU LEU ASP PHE SER GLN PRO GLY GLU LEU GLY ILE PHE
SEQRES 29 A 596 ILE HIS GLU PRO ILE ILE ALA ALA LEU GLU ALA GLN ASN
SEQRES 30 A 596 GLU ALA LYS GLY ILE MET ASP GLY ARG GLN LEU ALA VAL
SEQRES 31 A 596 SER PHE SER LEU LEU ARG GLU ASN SER LEU TYR TRP ASN
SEQRES 32 A 596 TYR TYR ILE ASP SER TYR LEU LYS GLY GLN SER PRO VAL
SEQRES 33 A 596 ALA PHE ASP LEU LEU HIS TRP ASN SER ASP SER THR ASN
SEQRES 34 A 596 VAL ALA GLY LYS THR HIS ASN SER LEU LEU ARG ARG LEU
SEQRES 35 A 596 TYR LEU GLU ASN GLN LEU VAL LYS GLY GLU LEU LYS ILE
SEQRES 36 A 596 ARG ASN THR ARG ILE ASP LEU GLY LYS VAL LYS THR PRO
SEQRES 37 A 596 VAL LEU LEU VAL SER ALA VAL ASP ASP HIS ILE ALA LEU
SEQRES 38 A 596 TRP GLN GLY THR TRP GLN GLY MET LYS LEU PHE GLY GLY
SEQRES 39 A 596 GLU GLN ARG PHE LEU LEU ALA GLU SER GLY HIS ILE ALA
SEQRES 40 A 596 GLY ILE ILE ASN PRO PRO ALA ALA ASN LYS TYR GLY PHE
SEQRES 41 A 596 TRP HIS ASN GLY ALA GLU ALA GLU SER PRO GLU SER TRP
SEQRES 42 A 596 LEU ALA GLY ALA THR HIS GLN GLY GLY SER TRP TRP PRO
SEQRES 43 A 596 GLU MET MET GLY PHE ILE GLN ASN ARG ASP GLU GLY SER
SEQRES 44 A 596 GLU PRO VAL PRO ALA ARG VAL PRO GLU GLU GLY LEU ALA
SEQRES 45 A 596 PRO ALA PRO GLY HIS TYR VAL LYS VAL ARG LEU ASN PRO
SEQRES 46 A 596 VAL PHE ALA CYS PRO THR GLU GLU ASP ALA ALA
SEQRES 1 B 596 GLY PRO MET SER GLN PRO SER TYR GLY PRO LEU PHE GLU
SEQRES 2 B 596 ALA LEU ALA HIS TYR ASN ASP LYS LEU LEU ALA MET ALA
SEQRES 3 B 596 LYS ALA GLN THR GLU ARG THR ALA GLN ALA LEU LEU GLN
SEQRES 4 B 596 THR ASN LEU ASP ASP LEU GLY GLN VAL LEU GLU GLN GLY
SEQRES 5 B 596 SER GLN GLN PRO TRP GLN LEU ILE GLN ALA GLN MET ASN
SEQRES 6 B 596 TRP TRP GLN ASP GLN LEU LYS LEU MET GLN HIS THR LEU
SEQRES 7 B 596 LEU LYS SER ALA GLY GLN PRO SER GLU PRO VAL ILE THR
SEQRES 8 B 596 PRO GLU ARG SER ASP ARG ARG PHE LYS ALA GLU ALA TRP
SEQRES 9 B 596 SER GLU GLN PRO ILE TYR ASP TYR LEU LYS GLN SER TYR
SEQRES 10 B 596 LEU LEU THR ALA ARG HIS LEU LEU ALA SER VAL ASP ALA
SEQRES 11 B 596 LEU GLU GLY VAL PRO GLN LYS SER ARG GLU ARG LEU ARG
SEQRES 12 B 596 PHE PHE THR ARG GLN TYR VAL ASN ALA MET ALA PRO SER
SEQRES 13 B 596 ASN PHE LEU ALA THR ASN PRO GLU LEU LEU LYS LEU THR
SEQRES 14 B 596 LEU GLU SER ASP GLY GLN ASN LEU VAL ARG GLY LEU ALA
SEQRES 15 B 596 LEU LEU ALA GLU ASP LEU GLU ARG SER ALA ASP GLN LEU
SEQRES 16 B 596 ASN ILE ARG LEU THR ASP GLU SER ALA PHE GLU LEU GLY
SEQRES 17 B 596 ARG ASP LEU ALA LEU THR PRO GLY ARG VAL VAL GLN ARG
SEQRES 18 B 596 THR GLU LEU TYR GLU LEU ILE GLN TYR SER PRO THR THR
SEQRES 19 B 596 GLU THR VAL GLY LYS THR PRO VAL LEU ILE VAL PRO PRO
SEQRES 20 B 596 PHE ILE ASN LYS TYR TYR ILE MET ASP MET ARG PRO GLN
SEQRES 21 B 596 ASN SER LEU VAL ALA TRP LEU VAL ALA GLN GLY GLN THR
SEQRES 22 B 596 VAL PHE MET ILE SER TRP ARG ASN PRO GLY VAL ALA GLN
SEQRES 23 B 596 ALA GLN ILE ASP LEU ASP ASP TYR VAL VAL ASP GLY VAL
SEQRES 24 B 596 ILE ALA ALA LEU ASP GLY VAL GLU ALA ALA THR GLY GLU
SEQRES 25 B 596 ARG GLU VAL HIS GLY ILE GLY TYR CYS ILE GLY GLY THR
SEQRES 26 B 596 ALA LEU SER LEU ALA MET GLY TRP LEU ALA ALA ARG ARG
SEQRES 27 B 596 GLN LYS GLN ARG VAL ARG THR ALA THR LEU PHE THR THR
SEQRES 28 B 596 LEU LEU ASP PHE SER GLN PRO GLY GLU LEU GLY ILE PHE
SEQRES 29 B 596 ILE HIS GLU PRO ILE ILE ALA ALA LEU GLU ALA GLN ASN
SEQRES 30 B 596 GLU ALA LYS GLY ILE MET ASP GLY ARG GLN LEU ALA VAL
SEQRES 31 B 596 SER PHE SER LEU LEU ARG GLU ASN SER LEU TYR TRP ASN
SEQRES 32 B 596 TYR TYR ILE ASP SER TYR LEU LYS GLY GLN SER PRO VAL
SEQRES 33 B 596 ALA PHE ASP LEU LEU HIS TRP ASN SER ASP SER THR ASN
SEQRES 34 B 596 VAL ALA GLY LYS THR HIS ASN SER LEU LEU ARG ARG LEU
SEQRES 35 B 596 TYR LEU GLU ASN GLN LEU VAL LYS GLY GLU LEU LYS ILE
SEQRES 36 B 596 ARG ASN THR ARG ILE ASP LEU GLY LYS VAL LYS THR PRO
SEQRES 37 B 596 VAL LEU LEU VAL SER ALA VAL ASP ASP HIS ILE ALA LEU
SEQRES 38 B 596 TRP GLN GLY THR TRP GLN GLY MET LYS LEU PHE GLY GLY
SEQRES 39 B 596 GLU GLN ARG PHE LEU LEU ALA GLU SER GLY HIS ILE ALA
SEQRES 40 B 596 GLY ILE ILE ASN PRO PRO ALA ALA ASN LYS TYR GLY PHE
SEQRES 41 B 596 TRP HIS ASN GLY ALA GLU ALA GLU SER PRO GLU SER TRP
SEQRES 42 B 596 LEU ALA GLY ALA THR HIS GLN GLY GLY SER TRP TRP PRO
SEQRES 43 B 596 GLU MET MET GLY PHE ILE GLN ASN ARG ASP GLU GLY SER
SEQRES 44 B 596 GLU PRO VAL PRO ALA ARG VAL PRO GLU GLU GLY LEU ALA
SEQRES 45 B 596 PRO ALA PRO GLY HIS TYR VAL LYS VAL ARG LEU ASN PRO
SEQRES 46 B 596 VAL PHE ALA CYS PRO THR GLU GLU ASP ALA ALA
SEQRES 1 C 596 GLY PRO MET SER GLN PRO SER TYR GLY PRO LEU PHE GLU
SEQRES 2 C 596 ALA LEU ALA HIS TYR ASN ASP LYS LEU LEU ALA MET ALA
SEQRES 3 C 596 LYS ALA GLN THR GLU ARG THR ALA GLN ALA LEU LEU GLN
SEQRES 4 C 596 THR ASN LEU ASP ASP LEU GLY GLN VAL LEU GLU GLN GLY
SEQRES 5 C 596 SER GLN GLN PRO TRP GLN LEU ILE GLN ALA GLN MET ASN
SEQRES 6 C 596 TRP TRP GLN ASP GLN LEU LYS LEU MET GLN HIS THR LEU
SEQRES 7 C 596 LEU LYS SER ALA GLY GLN PRO SER GLU PRO VAL ILE THR
SEQRES 8 C 596 PRO GLU ARG SER ASP ARG ARG PHE LYS ALA GLU ALA TRP
SEQRES 9 C 596 SER GLU GLN PRO ILE TYR ASP TYR LEU LYS GLN SER TYR
SEQRES 10 C 596 LEU LEU THR ALA ARG HIS LEU LEU ALA SER VAL ASP ALA
SEQRES 11 C 596 LEU GLU GLY VAL PRO GLN LYS SER ARG GLU ARG LEU ARG
SEQRES 12 C 596 PHE PHE THR ARG GLN TYR VAL ASN ALA MET ALA PRO SER
SEQRES 13 C 596 ASN PHE LEU ALA THR ASN PRO GLU LEU LEU LYS LEU THR
SEQRES 14 C 596 LEU GLU SER ASP GLY GLN ASN LEU VAL ARG GLY LEU ALA
SEQRES 15 C 596 LEU LEU ALA GLU ASP LEU GLU ARG SER ALA ASP GLN LEU
SEQRES 16 C 596 ASN ILE ARG LEU THR ASP GLU SER ALA PHE GLU LEU GLY
SEQRES 17 C 596 ARG ASP LEU ALA LEU THR PRO GLY ARG VAL VAL GLN ARG
SEQRES 18 C 596 THR GLU LEU TYR GLU LEU ILE GLN TYR SER PRO THR THR
SEQRES 19 C 596 GLU THR VAL GLY LYS THR PRO VAL LEU ILE VAL PRO PRO
SEQRES 20 C 596 PHE ILE ASN LYS TYR TYR ILE MET ASP MET ARG PRO GLN
SEQRES 21 C 596 ASN SER LEU VAL ALA TRP LEU VAL ALA GLN GLY GLN THR
SEQRES 22 C 596 VAL PHE MET ILE SER TRP ARG ASN PRO GLY VAL ALA GLN
SEQRES 23 C 596 ALA GLN ILE ASP LEU ASP ASP TYR VAL VAL ASP GLY VAL
SEQRES 24 C 596 ILE ALA ALA LEU ASP GLY VAL GLU ALA ALA THR GLY GLU
SEQRES 25 C 596 ARG GLU VAL HIS GLY ILE GLY TYR CYS ILE GLY GLY THR
SEQRES 26 C 596 ALA LEU SER LEU ALA MET GLY TRP LEU ALA ALA ARG ARG
SEQRES 27 C 596 GLN LYS GLN ARG VAL ARG THR ALA THR LEU PHE THR THR
SEQRES 28 C 596 LEU LEU ASP PHE SER GLN PRO GLY GLU LEU GLY ILE PHE
SEQRES 29 C 596 ILE HIS GLU PRO ILE ILE ALA ALA LEU GLU ALA GLN ASN
SEQRES 30 C 596 GLU ALA LYS GLY ILE MET ASP GLY ARG GLN LEU ALA VAL
SEQRES 31 C 596 SER PHE SER LEU LEU ARG GLU ASN SER LEU TYR TRP ASN
SEQRES 32 C 596 TYR TYR ILE ASP SER TYR LEU LYS GLY GLN SER PRO VAL
SEQRES 33 C 596 ALA PHE ASP LEU LEU HIS TRP ASN SER ASP SER THR ASN
SEQRES 34 C 596 VAL ALA GLY LYS THR HIS ASN SER LEU LEU ARG ARG LEU
SEQRES 35 C 596 TYR LEU GLU ASN GLN LEU VAL LYS GLY GLU LEU LYS ILE
SEQRES 36 C 596 ARG ASN THR ARG ILE ASP LEU GLY LYS VAL LYS THR PRO
SEQRES 37 C 596 VAL LEU LEU VAL SER ALA VAL ASP ASP HIS ILE ALA LEU
SEQRES 38 C 596 TRP GLN GLY THR TRP GLN GLY MET LYS LEU PHE GLY GLY
SEQRES 39 C 596 GLU GLN ARG PHE LEU LEU ALA GLU SER GLY HIS ILE ALA
SEQRES 40 C 596 GLY ILE ILE ASN PRO PRO ALA ALA ASN LYS TYR GLY PHE
SEQRES 41 C 596 TRP HIS ASN GLY ALA GLU ALA GLU SER PRO GLU SER TRP
SEQRES 42 C 596 LEU ALA GLY ALA THR HIS GLN GLY GLY SER TRP TRP PRO
SEQRES 43 C 596 GLU MET MET GLY PHE ILE GLN ASN ARG ASP GLU GLY SER
SEQRES 44 C 596 GLU PRO VAL PRO ALA ARG VAL PRO GLU GLU GLY LEU ALA
SEQRES 45 C 596 PRO ALA PRO GLY HIS TYR VAL LYS VAL ARG LEU ASN PRO
SEQRES 46 C 596 VAL PHE ALA CYS PRO THR GLU GLU ASP ALA ALA
FORMUL 4 HOH *7(H2 O)
HELIX 1 AA1 TYR A 6 GLN A 37 1 32
HELIX 2 AA2 PRO A 54 SER A 79 1 26
HELIX 3 AA3 GLN A 105 LEU A 129 1 25
HELIX 4 AA4 PRO A 133 ALA A 152 1 20
HELIX 5 AA5 PRO A 153 PHE A 156 5 4
HELIX 6 AA6 ASN A 160 LEU A 168 1 9
HELIX 7 AA7 GLN A 173 LEU A 197 1 25
HELIX 8 AA8 LYS A 249 ASP A 254 5 6
HELIX 9 AA9 ARG A 256 ASN A 259 5 4
HELIX 10 AB1 SER A 260 GLN A 268 1 9
HELIX 11 AB2 ASP A 288 ASP A 295 1 8
HELIX 12 AB3 GLY A 296 GLY A 309 1 14
HELIX 13 AB4 ILE A 320 ARG A 335 1 16
HELIX 14 AB5 PRO A 356 ILE A 363 5 8
HELIX 15 AB6 HIS A 364 GLY A 379 1 16
HELIX 16 AB7 ASP A 382 VAL A 388 1 7
HELIX 17 AB8 SER A 397 TYR A 403 1 7
HELIX 18 AB9 TYR A 403 LYS A 409 1 7
HELIX 19 AC1 PRO A 413 SER A 423 1 11
HELIX 20 AC2 GLY A 430 ARG A 439 1 10
HELIX 21 AC3 ASP A 459 VAL A 463 5 5
HELIX 22 AC4 LEU A 479 LYS A 488 1 10
HELIX 23 AC5 SER A 527 GLY A 534 1 8
HELIX 24 AC6 TRP A 542 ASP A 554 1 13
HELIX 25 AC7 GLY B 7 GLN B 37 1 31
HELIX 26 AC8 TRP B 55 LYS B 78 1 24
HELIX 27 AC9 PRO B 106 LEU B 129 1 24
HELIX 28 AD1 PRO B 133 MET B 151 1 19
HELIX 29 AD2 ALA B 152 PHE B 156 5 5
HELIX 30 AD3 ASN B 160 LEU B 168 1 9
HELIX 31 AD4 GLY B 172 ASN B 194 1 23
HELIX 32 AD5 LYS B 249 ASP B 254 5 6
HELIX 33 AD6 SER B 260 GLN B 268 1 9
HELIX 34 AD7 GLY B 281 ALA B 285 5 5
HELIX 35 AD8 ASP B 288 ASP B 295 1 8
HELIX 36 AD9 GLY B 296 GLY B 309 1 14
HELIX 37 AE1 ILE B 320 ARG B 335 1 16
HELIX 38 AE2 PRO B 356 ILE B 363 5 8
HELIX 39 AE3 HIS B 364 GLY B 379 1 16
HELIX 40 AE4 ASP B 382 VAL B 388 1 7
HELIX 41 AE5 SER B 397 TYR B 403 1 7
HELIX 42 AE6 TYR B 403 LYS B 409 1 7
HELIX 43 AE7 PRO B 413 SER B 423 1 11
HELIX 44 AE8 GLY B 430 ARG B 439 1 10
HELIX 45 AE9 ASP B 459 VAL B 463 5 5
HELIX 46 AF1 LEU B 479 LYS B 488 1 10
HELIX 47 AF2 PRO B 510 ASN B 514 5 5
HELIX 48 AF3 SER B 527 GLY B 534 1 8
HELIX 49 AF4 TRP B 542 ARG B 553 1 12
HELIX 50 AF5 TYR C 6 LEU C 35 1 30
HELIX 51 AF6 PRO C 54 SER C 79 1 26
HELIX 52 AF7 GLN C 105 LEU C 129 1 25
HELIX 53 AF8 PRO C 133 ALA C 152 1 20
HELIX 54 AF9 PRO C 153 THR C 159 5 7
HELIX 55 AG1 ASN C 160 THR C 167 1 8
HELIX 56 AG2 GLN C 173 ARG C 196 1 24
HELIX 57 AG3 LYS C 249 ASP C 254 5 6
HELIX 58 AG4 ARG C 256 ASN C 259 5 4
HELIX 59 AG5 SER C 260 GLN C 268 1 9
HELIX 60 AG6 VAL C 282 ILE C 287 5 6
HELIX 61 AG7 ASP C 288 ASP C 295 1 8
HELIX 62 AG8 GLY C 296 GLY C 309 1 14
HELIX 63 AG9 ILE C 320 ARG C 335 1 16
HELIX 64 AH1 HIS C 364 GLY C 379 1 16
HELIX 65 AH2 ASP C 382 VAL C 388 1 7
HELIX 66 AH3 LEU C 398 TYR C 403 1 6
HELIX 67 AH4 TYR C 403 LYS C 409 1 7
HELIX 68 AH5 PRO C 413 SER C 423 1 11
HELIX 69 AH6 GLY C 430 ARG C 439 1 10
HELIX 70 AH7 ASP C 459 VAL C 463 5 5
HELIX 71 AH8 LEU C 479 LYS C 488 1 10
HELIX 72 AH9 SER C 527 ALA C 535 1 9
HELIX 73 AI1 TRP C 542 ARG C 553 1 12
SHEET 1 AA111 THR A 536 GLY A 539 0
SHEET 2 AA111 GLY A 517 HIS A 520 -1 N HIS A 520 O THR A 536
SHEET 3 AA111 GLN A 494 ALA A 499 -1 N LEU A 498 O TRP A 519
SHEET 4 AA111 VAL A 467 ALA A 472 1 N SER A 471 O ALA A 499
SHEET 5 AA111 VAL A 341 PHE A 347 1 N LEU A 346 O VAL A 470
SHEET 6 AA111 VAL A 313 GLY A 317 1 N GLY A 317 O PHE A 347
SHEET 7 AA111 VAL A 240 VAL A 243 1 N VAL A 243 O ILE A 316
SHEET 8 AA111 VAL A 272 TRP A 277 1 O PHE A 273 N VAL A 240
SHEET 9 AA111 TYR A 223 TYR A 228 -1 N ILE A 226 O MET A 274
SHEET 10 AA111 GLY A 214 ARG A 219 -1 N ARG A 215 O GLN A 227
SHEET 11 AA111 ALA A 570 PRO A 571 -1 O ALA A 570 N VAL A 216
SHEET 1 AA2 2 THR A 234 VAL A 235 0
SHEET 2 AA2 2 VAL A 560 PRO A 561 -1 O VAL A 560 N VAL A 235
SHEET 1 AA3 2 ILE A 380 MET A 381 0
SHEET 2 AA3 2 VAL A 428 ALA A 429 -1 O VAL A 428 N MET A 381
SHEET 1 AA410 GLY B 214 ARG B 219 0
SHEET 2 AA410 TYR B 223 TYR B 228 -1 O GLN B 227 N ARG B 215
SHEET 3 AA410 VAL B 272 TRP B 277 -1 O MET B 274 N ILE B 226
SHEET 4 AA410 VAL B 240 VAL B 243 1 N VAL B 240 O PHE B 273
SHEET 5 AA410 VAL B 313 GLY B 317 1 O ILE B 316 N VAL B 243
SHEET 6 AA410 VAL B 341 PHE B 347 1 O PHE B 347 N GLY B 317
SHEET 7 AA410 VAL B 467 ALA B 472 1 O VAL B 470 N LEU B 346
SHEET 8 AA410 GLN B 494 ALA B 499 1 O ALA B 499 N SER B 471
SHEET 9 AA410 GLY B 517 HIS B 520 -1 O TRP B 519 N LEU B 498
SHEET 10 AA410 THR B 536 GLY B 539 -1 O THR B 536 N HIS B 520
SHEET 1 AA5 2 THR B 234 VAL B 235 0
SHEET 2 AA5 2 VAL B 560 PRO B 561 -1 O VAL B 560 N VAL B 235
SHEET 1 AA6 2 ILE B 380 MET B 381 0
SHEET 2 AA6 2 VAL B 428 ALA B 429 -1 O VAL B 428 N MET B 381
SHEET 1 AA711 THR C 536 GLY C 539 0
SHEET 2 AA711 GLY C 517 HIS C 520 -1 N PHE C 518 O GLN C 538
SHEET 3 AA711 GLN C 494 ALA C 499 -1 N LEU C 498 O TRP C 519
SHEET 4 AA711 VAL C 467 ALA C 472 1 N SER C 471 O ALA C 499
SHEET 5 AA711 VAL C 341 PHE C 347 1 N LEU C 346 O VAL C 470
SHEET 6 AA711 VAL C 313 GLY C 317 1 N GLY C 317 O THR C 345
SHEET 7 AA711 VAL C 240 VAL C 243 1 N VAL C 243 O ILE C 316
SHEET 8 AA711 VAL C 272 TRP C 277 1 O PHE C 273 N VAL C 240
SHEET 9 AA711 TYR C 223 TYR C 228 -1 N ILE C 226 O MET C 274
SHEET 10 AA711 GLY C 214 ARG C 219 -1 N ARG C 215 O GLN C 227
SHEET 11 AA711 ALA C 570 PRO C 571 -1 O ALA C 570 N VAL C 216
SHEET 1 AA8 2 THR C 234 VAL C 235 0
SHEET 2 AA8 2 VAL C 560 PRO C 561 -1 O VAL C 560 N VAL C 235
SHEET 1 AA9 2 ILE C 380 MET C 381 0
SHEET 2 AA9 2 VAL C 428 ALA C 429 -1 O VAL C 428 N MET C 381
CRYST1 156.632 96.300 142.999 90.00 90.46 90.00 C 1 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 0.006384 0.000000 0.000051 0.00000
SCALE2 0.000000 0.010384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006993 0.00000
MTRIX1 1 0.455322 -0.890060 -0.021791 91.16835 1
MTRIX2 1 -0.888201 -0.452408 -0.080169 63.27870 1
MTRIX3 1 0.061496 0.055857 -0.996543 93.25586 1
MTRIX1 2 -0.445573 -0.893455 0.056594 84.18570 1
MTRIX2 2 0.894495 -0.441721 0.069002 52.92851 1
MTRIX3 2 -0.036652 0.081368 0.996010 -49.96777 1
TER 4210 PHE A 585
TER 8286 PHE B 585
TER 12292 PRO C 583
MASTER 770 0 0 73 44 0 0 1212296 3 0 138
END |