HEADER TRANSFERASE 08-MAY-14 4D28
TITLE CRYSTAL STRUCTURE OF THE KINASE DOMAIN OF CIPK24/SOS2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CBL-INTERACTING SERINE/THREONINE-PROTEIN KINASE 24;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PROTEIN SALT OVERLY SENSITIVE 2, SNF1-RELATED KINASE 3.11,
COMPND 5 SNRK3.11 AT5G35410;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T2
KEYWDS TRANSFERASE, SALT STRESS, SODIUM TRANSPORT, ION HOMEOSTASIS
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.GONZALEZ-RUBIO,A.CHAVES-SANJUAN,M.J.SANCHEZ-BARRENA,A.ALBERT
REVDAT 5 20-DEC-23 4D28 1 REMARK
REVDAT 4 06-DEC-17 4D28 1 TITLE REMARK
REVDAT 3 17-DEC-14 4D28 1 REMARK
REVDAT 2 05-NOV-14 4D28 1 JRNL
REVDAT 1 15-OCT-14 4D28 0
JRNL AUTH A.CHAVES-SANJUAN,M.J.SANCHEZ-BARRENA,J.M.GONZALEZ-RUBIO,
JRNL AUTH 2 M.MORENO,P.RAGEL,M.JIMENEZ,J.M.PARDO,M.MARTINEZ-RIPOLL,
JRNL AUTH 3 F.J.QUINTERO,A.ALBERT
JRNL TITL STRUCTURAL BASIS OF THE REGULATORY MECHANISM OF THE PLANT
JRNL TITL 2 CIPK FAMILY OF PROTEIN KINASES CONTROLLING ION HOMEOSTASIS
JRNL TITL 3 AND ABIOTIC STRESS
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 E4532 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 25288725
JRNL DOI 10.1073/PNAS.1407610111
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 15242
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.271
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 810
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1157
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8821
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.12000
REMARK 3 B22 (A**2) : 1.24000
REMARK 3 B33 (A**2) : 3.78000
REMARK 3 B12 (A**2) : -1.52000
REMARK 3 B13 (A**2) : -2.01000
REMARK 3 B23 (A**2) : -2.30000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.747
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.665
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.659
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.891
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9002 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12160 ; 1.126 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1091 ; 5.629 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 421 ;38.933 ;23.658
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1619 ;20.823 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;18.758 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1349 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6759 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4394 ; 1.105 ; 7.022
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5475 ; 2.046 ;10.518
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4608 ; 0.760 ; 7.070
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES ARE REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4D28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1290060570.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15242
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 70.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.27000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 1.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4CZT
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM TRIS PH 7.0 AND 22% PEG 4K.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 THR A 2
REMARK 465 LYS A 3
REMARK 465 LYS A 4
REMARK 465 MET A 5
REMARK 465 ARG A 6
REMARK 465 ARG A 7
REMARK 465 GLY A 18
REMARK 465 GLU A 19
REMARK 465 GLY A 20
REMARK 465 THR A 21
REMARK 465 PHE A 22
REMARK 465 VAL A 163
REMARK 465 GLU A 164
REMARK 465 LEU A 165
REMARK 465 GLY A 290
REMARK 465 ILE A 291
REMARK 465 GLU A 292
REMARK 465 GLY A 293
REMARK 465 SER A 294
REMARK 465 TYR A 295
REMARK 465 VAL A 296
REMARK 465 ALA A 297
REMARK 465 GLU A 298
REMARK 465 ASN A 299
REMARK 465 VAL A 300
REMARK 465 GLU A 301
REMARK 465 ARG A 302
REMARK 465 ASN A 303
REMARK 465 ASP A 304
REMARK 465 GLU A 305
REMARK 465 GLY A 306
REMARK 465 PRO A 307
REMARK 465 LEU A 308
REMARK 465 MET A 309
REMARK 465 MET A 310
REMARK 465 ASN A 311
REMARK 465 ALA A 312
REMARK 465 PHE A 313
REMARK 465 GLU A 314
REMARK 465 MET A 315
REMARK 465 ILE A 316
REMARK 465 THR A 317
REMARK 465 LEU A 318
REMARK 465 SER A 319
REMARK 465 GLN A 320
REMARK 465 GLY A 321
REMARK 465 LEU A 322
REMARK 465 ASN A 323
REMARK 465 LEU A 324
REMARK 465 SER A 325
REMARK 465 ALA A 326
REMARK 465 LEU A 327
REMARK 465 PHE A 328
REMARK 465 ASP A 329
REMARK 465 ARG A 330
REMARK 465 ARG A 331
REMARK 465 GLN A 332
REMARK 465 ASP A 333
REMARK 465 PHE A 334
REMARK 465 VAL A 335
REMARK 465 LYS A 336
REMARK 465 ARG A 337
REMARK 465 GLN A 338
REMARK 465 THR A 339
REMARK 465 ARG A 340
REMARK 465 PHE A 341
REMARK 465 VAL A 342
REMARK 465 SER A 343
REMARK 465 ARG A 344
REMARK 465 ARG A 345
REMARK 465 GLU A 346
REMARK 465 PRO A 347
REMARK 465 SER A 348
REMARK 465 GLU A 349
REMARK 465 ILE A 350
REMARK 465 ILE A 351
REMARK 465 ALA A 352
REMARK 465 ASN A 353
REMARK 465 ILE A 354
REMARK 465 GLU A 355
REMARK 465 ALA A 356
REMARK 465 VAL A 357
REMARK 465 ALA A 358
REMARK 465 ASN A 359
REMARK 465 SER A 360
REMARK 465 MET A 361
REMARK 465 GLY A 362
REMARK 465 PHE A 363
REMARK 465 LYS A 364
REMARK 465 SER A 365
REMARK 465 HIS A 366
REMARK 465 THR A 367
REMARK 465 ARG A 368
REMARK 465 ASN A 369
REMARK 465 PHE A 370
REMARK 465 LYS A 371
REMARK 465 THR A 372
REMARK 465 ARG A 373
REMARK 465 LEU A 374
REMARK 465 GLU A 375
REMARK 465 GLY A 376
REMARK 465 LEU A 377
REMARK 465 SER A 378
REMARK 465 SER A 379
REMARK 465 ILE A 380
REMARK 465 LYS A 381
REMARK 465 ALA A 382
REMARK 465 GLY A 383
REMARK 465 GLN A 384
REMARK 465 LEU A 385
REMARK 465 ALA A 386
REMARK 465 VAL A 387
REMARK 465 VAL A 388
REMARK 465 ILE A 389
REMARK 465 GLU A 390
REMARK 465 ILE A 391
REMARK 465 TYR A 392
REMARK 465 GLU A 393
REMARK 465 VAL A 394
REMARK 465 ALA A 395
REMARK 465 PRO A 396
REMARK 465 SER A 397
REMARK 465 LEU A 398
REMARK 465 PHE A 399
REMARK 465 MET A 400
REMARK 465 VAL A 401
REMARK 465 ASP A 402
REMARK 465 VAL A 403
REMARK 465 ARG A 404
REMARK 465 LYS A 405
REMARK 465 ALA A 406
REMARK 465 ALA A 407
REMARK 465 GLY A 408
REMARK 465 GLU A 409
REMARK 465 THR A 410
REMARK 465 LEU A 411
REMARK 465 GLU A 412
REMARK 465 TYR A 413
REMARK 465 HIS A 414
REMARK 465 LYS A 415
REMARK 465 PHE A 416
REMARK 465 TYR A 417
REMARK 465 LYS A 418
REMARK 465 LYS A 419
REMARK 465 LEU A 420
REMARK 465 CYS A 421
REMARK 465 SER A 422
REMARK 465 LYS A 423
REMARK 465 LEU A 424
REMARK 465 GLU A 425
REMARK 465 ASN A 426
REMARK 465 ILE A 427
REMARK 465 ILE A 428
REMARK 465 TRP A 429
REMARK 465 ARG A 430
REMARK 465 ALA A 431
REMARK 465 THR A 432
REMARK 465 GLU A 433
REMARK 465 GLY A 434
REMARK 465 ILE A 435
REMARK 465 PRO A 436
REMARK 465 LYS A 437
REMARK 465 SER A 438
REMARK 465 GLU A 439
REMARK 465 ILE A 440
REMARK 465 LEU A 441
REMARK 465 ARG A 442
REMARK 465 THR A 443
REMARK 465 ILE A 444
REMARK 465 THR A 445
REMARK 465 PHE A 446
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 LYS B 3
REMARK 465 LYS B 4
REMARK 465 MET B 5
REMARK 465 ARG B 6
REMARK 465 GLU B 161
REMARK 465 GLY B 162
REMARK 465 VAL B 163
REMARK 465 GLU B 164
REMARK 465 LEU B 165
REMARK 465 LEU B 166
REMARK 465 GLY B 290
REMARK 465 ILE B 291
REMARK 465 GLU B 292
REMARK 465 GLY B 293
REMARK 465 SER B 294
REMARK 465 TYR B 295
REMARK 465 VAL B 296
REMARK 465 ALA B 297
REMARK 465 GLU B 298
REMARK 465 ASN B 299
REMARK 465 VAL B 300
REMARK 465 GLU B 301
REMARK 465 ARG B 302
REMARK 465 ASN B 303
REMARK 465 ASP B 304
REMARK 465 GLU B 305
REMARK 465 GLY B 306
REMARK 465 PRO B 307
REMARK 465 LEU B 308
REMARK 465 MET B 309
REMARK 465 MET B 310
REMARK 465 ASN B 311
REMARK 465 ALA B 312
REMARK 465 PHE B 313
REMARK 465 GLU B 314
REMARK 465 MET B 315
REMARK 465 ILE B 316
REMARK 465 THR B 317
REMARK 465 LEU B 318
REMARK 465 SER B 319
REMARK 465 GLN B 320
REMARK 465 GLY B 321
REMARK 465 LEU B 322
REMARK 465 ASN B 323
REMARK 465 LEU B 324
REMARK 465 SER B 325
REMARK 465 ALA B 326
REMARK 465 LEU B 327
REMARK 465 PHE B 328
REMARK 465 ASP B 329
REMARK 465 ARG B 330
REMARK 465 ARG B 331
REMARK 465 GLN B 332
REMARK 465 ASP B 333
REMARK 465 PHE B 334
REMARK 465 VAL B 335
REMARK 465 LYS B 336
REMARK 465 ARG B 337
REMARK 465 GLN B 338
REMARK 465 THR B 339
REMARK 465 ARG B 340
REMARK 465 PHE B 341
REMARK 465 VAL B 342
REMARK 465 SER B 343
REMARK 465 ARG B 344
REMARK 465 ARG B 345
REMARK 465 GLU B 346
REMARK 465 PRO B 347
REMARK 465 SER B 348
REMARK 465 GLU B 349
REMARK 465 ILE B 350
REMARK 465 ILE B 351
REMARK 465 ALA B 352
REMARK 465 ASN B 353
REMARK 465 ILE B 354
REMARK 465 GLU B 355
REMARK 465 ALA B 356
REMARK 465 VAL B 357
REMARK 465 ALA B 358
REMARK 465 ASN B 359
REMARK 465 SER B 360
REMARK 465 MET B 361
REMARK 465 GLY B 362
REMARK 465 PHE B 363
REMARK 465 LYS B 364
REMARK 465 SER B 365
REMARK 465 HIS B 366
REMARK 465 THR B 367
REMARK 465 ARG B 368
REMARK 465 ASN B 369
REMARK 465 PHE B 370
REMARK 465 LYS B 371
REMARK 465 THR B 372
REMARK 465 ARG B 373
REMARK 465 LEU B 374
REMARK 465 GLU B 375
REMARK 465 GLY B 376
REMARK 465 LEU B 377
REMARK 465 SER B 378
REMARK 465 SER B 379
REMARK 465 ILE B 380
REMARK 465 LYS B 381
REMARK 465 ALA B 382
REMARK 465 GLY B 383
REMARK 465 GLN B 384
REMARK 465 LEU B 385
REMARK 465 ALA B 386
REMARK 465 VAL B 387
REMARK 465 VAL B 388
REMARK 465 ILE B 389
REMARK 465 GLU B 390
REMARK 465 ILE B 391
REMARK 465 TYR B 392
REMARK 465 GLU B 393
REMARK 465 VAL B 394
REMARK 465 ALA B 395
REMARK 465 PRO B 396
REMARK 465 SER B 397
REMARK 465 LEU B 398
REMARK 465 PHE B 399
REMARK 465 MET B 400
REMARK 465 VAL B 401
REMARK 465 ASP B 402
REMARK 465 VAL B 403
REMARK 465 ARG B 404
REMARK 465 LYS B 405
REMARK 465 ALA B 406
REMARK 465 ALA B 407
REMARK 465 GLY B 408
REMARK 465 GLU B 409
REMARK 465 THR B 410
REMARK 465 LEU B 411
REMARK 465 GLU B 412
REMARK 465 TYR B 413
REMARK 465 HIS B 414
REMARK 465 LYS B 415
REMARK 465 PHE B 416
REMARK 465 TYR B 417
REMARK 465 LYS B 418
REMARK 465 LYS B 419
REMARK 465 LEU B 420
REMARK 465 CYS B 421
REMARK 465 SER B 422
REMARK 465 LYS B 423
REMARK 465 LEU B 424
REMARK 465 GLU B 425
REMARK 465 ASN B 426
REMARK 465 ILE B 427
REMARK 465 ILE B 428
REMARK 465 TRP B 429
REMARK 465 ARG B 430
REMARK 465 ALA B 431
REMARK 465 THR B 432
REMARK 465 GLU B 433
REMARK 465 GLY B 434
REMARK 465 ILE B 435
REMARK 465 PRO B 436
REMARK 465 LYS B 437
REMARK 465 SER B 438
REMARK 465 GLU B 439
REMARK 465 ILE B 440
REMARK 465 LEU B 441
REMARK 465 ARG B 442
REMARK 465 THR B 443
REMARK 465 ILE B 444
REMARK 465 THR B 445
REMARK 465 PHE B 446
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 LYS C 3
REMARK 465 LYS C 4
REMARK 465 MET C 5
REMARK 465 ARG C 6
REMARK 465 GLY C 162
REMARK 465 VAL C 163
REMARK 465 GLU C 164
REMARK 465 LEU C 165
REMARK 465 GLY C 290
REMARK 465 ILE C 291
REMARK 465 GLU C 292
REMARK 465 GLY C 293
REMARK 465 SER C 294
REMARK 465 TYR C 295
REMARK 465 VAL C 296
REMARK 465 ALA C 297
REMARK 465 GLU C 298
REMARK 465 ASN C 299
REMARK 465 VAL C 300
REMARK 465 GLU C 301
REMARK 465 ARG C 302
REMARK 465 ASN C 303
REMARK 465 ASP C 304
REMARK 465 GLU C 305
REMARK 465 GLY C 306
REMARK 465 PRO C 307
REMARK 465 LEU C 308
REMARK 465 MET C 309
REMARK 465 MET C 310
REMARK 465 ASN C 311
REMARK 465 ALA C 312
REMARK 465 PHE C 313
REMARK 465 GLU C 314
REMARK 465 MET C 315
REMARK 465 ILE C 316
REMARK 465 THR C 317
REMARK 465 LEU C 318
REMARK 465 SER C 319
REMARK 465 GLN C 320
REMARK 465 GLY C 321
REMARK 465 LEU C 322
REMARK 465 ASN C 323
REMARK 465 LEU C 324
REMARK 465 SER C 325
REMARK 465 ALA C 326
REMARK 465 LEU C 327
REMARK 465 PHE C 328
REMARK 465 ASP C 329
REMARK 465 ARG C 330
REMARK 465 ARG C 331
REMARK 465 GLN C 332
REMARK 465 ASP C 333
REMARK 465 PHE C 334
REMARK 465 VAL C 335
REMARK 465 LYS C 336
REMARK 465 ARG C 337
REMARK 465 GLN C 338
REMARK 465 THR C 339
REMARK 465 ARG C 340
REMARK 465 PHE C 341
REMARK 465 VAL C 342
REMARK 465 SER C 343
REMARK 465 ARG C 344
REMARK 465 ARG C 345
REMARK 465 GLU C 346
REMARK 465 PRO C 347
REMARK 465 SER C 348
REMARK 465 GLU C 349
REMARK 465 ILE C 350
REMARK 465 ILE C 351
REMARK 465 ALA C 352
REMARK 465 ASN C 353
REMARK 465 ILE C 354
REMARK 465 GLU C 355
REMARK 465 ALA C 356
REMARK 465 VAL C 357
REMARK 465 ALA C 358
REMARK 465 ASN C 359
REMARK 465 SER C 360
REMARK 465 MET C 361
REMARK 465 GLY C 362
REMARK 465 PHE C 363
REMARK 465 LYS C 364
REMARK 465 SER C 365
REMARK 465 HIS C 366
REMARK 465 THR C 367
REMARK 465 ARG C 368
REMARK 465 ASN C 369
REMARK 465 PHE C 370
REMARK 465 LYS C 371
REMARK 465 THR C 372
REMARK 465 ARG C 373
REMARK 465 LEU C 374
REMARK 465 GLU C 375
REMARK 465 GLY C 376
REMARK 465 LEU C 377
REMARK 465 SER C 378
REMARK 465 SER C 379
REMARK 465 ILE C 380
REMARK 465 LYS C 381
REMARK 465 ALA C 382
REMARK 465 GLY C 383
REMARK 465 GLN C 384
REMARK 465 LEU C 385
REMARK 465 ALA C 386
REMARK 465 VAL C 387
REMARK 465 VAL C 388
REMARK 465 ILE C 389
REMARK 465 GLU C 390
REMARK 465 ILE C 391
REMARK 465 TYR C 392
REMARK 465 GLU C 393
REMARK 465 VAL C 394
REMARK 465 ALA C 395
REMARK 465 PRO C 396
REMARK 465 SER C 397
REMARK 465 LEU C 398
REMARK 465 PHE C 399
REMARK 465 MET C 400
REMARK 465 VAL C 401
REMARK 465 ASP C 402
REMARK 465 VAL C 403
REMARK 465 ARG C 404
REMARK 465 LYS C 405
REMARK 465 ALA C 406
REMARK 465 ALA C 407
REMARK 465 GLY C 408
REMARK 465 GLU C 409
REMARK 465 THR C 410
REMARK 465 LEU C 411
REMARK 465 GLU C 412
REMARK 465 TYR C 413
REMARK 465 HIS C 414
REMARK 465 LYS C 415
REMARK 465 PHE C 416
REMARK 465 TYR C 417
REMARK 465 LYS C 418
REMARK 465 LYS C 419
REMARK 465 LEU C 420
REMARK 465 CYS C 421
REMARK 465 SER C 422
REMARK 465 LYS C 423
REMARK 465 LEU C 424
REMARK 465 GLU C 425
REMARK 465 ASN C 426
REMARK 465 ILE C 427
REMARK 465 ILE C 428
REMARK 465 TRP C 429
REMARK 465 ARG C 430
REMARK 465 ALA C 431
REMARK 465 THR C 432
REMARK 465 GLU C 433
REMARK 465 GLY C 434
REMARK 465 ILE C 435
REMARK 465 PRO C 436
REMARK 465 LYS C 437
REMARK 465 SER C 438
REMARK 465 GLU C 439
REMARK 465 ILE C 440
REMARK 465 LEU C 441
REMARK 465 ARG C 442
REMARK 465 THR C 443
REMARK 465 ILE C 444
REMARK 465 THR C 445
REMARK 465 PHE C 446
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 LYS D 3
REMARK 465 LYS D 4
REMARK 465 MET D 5
REMARK 465 ARG D 6
REMARK 465 ARG D 7
REMARK 465 VAL D 8
REMARK 465 GLY D 9
REMARK 465 ILE D 17
REMARK 465 GLY D 18
REMARK 465 GLU D 19
REMARK 465 GLY D 20
REMARK 465 GLU D 161
REMARK 465 GLY D 162
REMARK 465 VAL D 163
REMARK 465 GLU D 164
REMARK 465 LEU D 165
REMARK 465 GLY D 290
REMARK 465 ILE D 291
REMARK 465 GLU D 292
REMARK 465 GLY D 293
REMARK 465 SER D 294
REMARK 465 TYR D 295
REMARK 465 VAL D 296
REMARK 465 ALA D 297
REMARK 465 GLU D 298
REMARK 465 ASN D 299
REMARK 465 VAL D 300
REMARK 465 GLU D 301
REMARK 465 ARG D 302
REMARK 465 ASN D 303
REMARK 465 ASP D 304
REMARK 465 GLU D 305
REMARK 465 GLY D 306
REMARK 465 PRO D 307
REMARK 465 LEU D 308
REMARK 465 MET D 309
REMARK 465 MET D 310
REMARK 465 ASN D 311
REMARK 465 ALA D 312
REMARK 465 PHE D 313
REMARK 465 GLU D 314
REMARK 465 MET D 315
REMARK 465 ILE D 316
REMARK 465 THR D 317
REMARK 465 LEU D 318
REMARK 465 SER D 319
REMARK 465 GLN D 320
REMARK 465 GLY D 321
REMARK 465 LEU D 322
REMARK 465 ASN D 323
REMARK 465 LEU D 324
REMARK 465 SER D 325
REMARK 465 ALA D 326
REMARK 465 LEU D 327
REMARK 465 PHE D 328
REMARK 465 ASP D 329
REMARK 465 ARG D 330
REMARK 465 ARG D 331
REMARK 465 GLN D 332
REMARK 465 ASP D 333
REMARK 465 PHE D 334
REMARK 465 VAL D 335
REMARK 465 LYS D 336
REMARK 465 ARG D 337
REMARK 465 GLN D 338
REMARK 465 THR D 339
REMARK 465 ARG D 340
REMARK 465 PHE D 341
REMARK 465 VAL D 342
REMARK 465 SER D 343
REMARK 465 ARG D 344
REMARK 465 ARG D 345
REMARK 465 GLU D 346
REMARK 465 PRO D 347
REMARK 465 SER D 348
REMARK 465 GLU D 349
REMARK 465 ILE D 350
REMARK 465 ILE D 351
REMARK 465 ALA D 352
REMARK 465 ASN D 353
REMARK 465 ILE D 354
REMARK 465 GLU D 355
REMARK 465 ALA D 356
REMARK 465 VAL D 357
REMARK 465 ALA D 358
REMARK 465 ASN D 359
REMARK 465 SER D 360
REMARK 465 MET D 361
REMARK 465 GLY D 362
REMARK 465 PHE D 363
REMARK 465 LYS D 364
REMARK 465 SER D 365
REMARK 465 HIS D 366
REMARK 465 THR D 367
REMARK 465 ARG D 368
REMARK 465 ASN D 369
REMARK 465 PHE D 370
REMARK 465 LYS D 371
REMARK 465 THR D 372
REMARK 465 ARG D 373
REMARK 465 LEU D 374
REMARK 465 GLU D 375
REMARK 465 GLY D 376
REMARK 465 LEU D 377
REMARK 465 SER D 378
REMARK 465 SER D 379
REMARK 465 ILE D 380
REMARK 465 LYS D 381
REMARK 465 ALA D 382
REMARK 465 GLY D 383
REMARK 465 GLN D 384
REMARK 465 LEU D 385
REMARK 465 ALA D 386
REMARK 465 VAL D 387
REMARK 465 VAL D 388
REMARK 465 ILE D 389
REMARK 465 GLU D 390
REMARK 465 ILE D 391
REMARK 465 TYR D 392
REMARK 465 GLU D 393
REMARK 465 VAL D 394
REMARK 465 ALA D 395
REMARK 465 PRO D 396
REMARK 465 SER D 397
REMARK 465 LEU D 398
REMARK 465 PHE D 399
REMARK 465 MET D 400
REMARK 465 VAL D 401
REMARK 465 ASP D 402
REMARK 465 VAL D 403
REMARK 465 ARG D 404
REMARK 465 LYS D 405
REMARK 465 ALA D 406
REMARK 465 ALA D 407
REMARK 465 GLY D 408
REMARK 465 GLU D 409
REMARK 465 THR D 410
REMARK 465 LEU D 411
REMARK 465 GLU D 412
REMARK 465 TYR D 413
REMARK 465 HIS D 414
REMARK 465 LYS D 415
REMARK 465 PHE D 416
REMARK 465 TYR D 417
REMARK 465 LYS D 418
REMARK 465 LYS D 419
REMARK 465 LEU D 420
REMARK 465 CYS D 421
REMARK 465 SER D 422
REMARK 465 LYS D 423
REMARK 465 LEU D 424
REMARK 465 GLU D 425
REMARK 465 ASN D 426
REMARK 465 ILE D 427
REMARK 465 ILE D 428
REMARK 465 TRP D 429
REMARK 465 ARG D 430
REMARK 465 ALA D 431
REMARK 465 THR D 432
REMARK 465 GLU D 433
REMARK 465 GLY D 434
REMARK 465 ILE D 435
REMARK 465 PRO D 436
REMARK 465 LYS D 437
REMARK 465 SER D 438
REMARK 465 GLU D 439
REMARK 465 ILE D 440
REMARK 465 LEU D 441
REMARK 465 ARG D 442
REMARK 465 THR D 443
REMARK 465 ILE D 444
REMARK 465 THR D 445
REMARK 465 PHE D 446
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 CD1 ILE B 41 CD1 TYR B 85 1.42
REMARK 500 OD1 ASN C 174 OE2 GLU C 212 1.60
REMARK 500 O TYR D 175 NE1 TRP D 194 1.83
REMARK 500 OE2 GLU A 179 NH2 ARG A 252 1.86
REMARK 500 NH2 ARG B 99 OE1 GLU B 110 1.90
REMARK 500 OD1 ASP C 143 N ASN C 147 1.92
REMARK 500 CD1 ILE B 41 CE1 TYR B 85 1.95
REMARK 500 O LEU C 281 N ILE C 284 1.96
REMARK 500 O LEU B 281 N ILE B 284 1.96
REMARK 500 OE2 GLU C 179 NH1 ARG C 252 1.96
REMARK 500 O LEU D 281 N ILE D 284 1.96
REMARK 500 NH2 ARG B 99 OE2 GLU B 110 1.96
REMARK 500 O LEU A 281 N ILE A 284 1.98
REMARK 500 NH2 ARG B 99 CD GLU B 110 2.04
REMARK 500 N VAL A 8 O TYR A 11 2.07
REMARK 500 NH2 ARG C 99 OE2 GLU C 110 2.08
REMARK 500 NH1 ARG A 99 OH TYR A 114 2.10
REMARK 500 NH1 ARG B 7 O TYR B 11 2.11
REMARK 500 NZ LYS B 40 OD1 ASP B 152 2.12
REMARK 500 CD ARG B 7 OE2 GLU B 12 2.12
REMARK 500 OG SER C 80 N LYS C 83 2.13
REMARK 500 O ASP C 246 NE ARG C 252 2.14
REMARK 500 O GLU C 212 CD2 LEU C 215 2.17
REMARK 500 OD2 ASP C 246 OG1 THR C 251 2.17
REMARK 500 OD2 ASP D 246 OG1 THR D 251 2.18
REMARK 500 OD1 ASP D 143 N ASN D 147 2.18
REMARK 500 N ASN D 30 O ASP D 35 2.18
REMARK 500 OD2 ASP B 246 OG1 THR B 251 2.19
REMARK 500 OD2 ASP B 134 NZ LYS B 136 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 262 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO B 249 C - N - CA ANGL. DEV. = -11.7 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 10 -7.08 84.56
REMARK 500 ARG A 15 146.29 -170.88
REMARK 500 LYS A 49 60.12 -105.46
REMARK 500 ARG A 133 -14.69 77.91
REMARK 500 ASP A 134 62.87 -151.30
REMARK 500 GLN A 184 -115.30 -114.07
REMARK 500 ASN A 267 11.92 58.27
REMARK 500 GLU A 278 115.29 -35.37
REMARK 500 ASN A 280 119.75 -30.64
REMARK 500 ARG B 15 140.86 -173.68
REMARK 500 THR B 21 -127.07 52.91
REMARK 500 ALA B 23 97.95 -49.91
REMARK 500 LYS B 44 -72.19 -66.40
REMARK 500 LYS B 49 61.32 -117.66
REMARK 500 LEU B 135 120.93 -31.20
REMARK 500 GLN B 184 -112.60 -104.01
REMARK 500 LEU B 245 50.79 -96.43
REMARK 500 GLU B 278 117.63 -38.51
REMARK 500 ASN B 280 120.55 -30.27
REMARK 500 ARG C 15 143.59 -171.01
REMARK 500 LYS C 49 58.31 -102.34
REMARK 500 ASP C 134 22.12 -145.06
REMARK 500 ASP C 152 30.80 70.65
REMARK 500 ASN C 167 -65.16 -122.61
REMARK 500 GLN C 184 -121.13 -91.81
REMARK 500 LEU C 245 46.52 -92.01
REMARK 500 PRO C 270 97.94 -56.87
REMARK 500 ASN C 280 122.48 -30.02
REMARK 500 ARG D 15 143.51 -172.16
REMARK 500 ASN D 50 137.88 179.03
REMARK 500 ARG D 133 -5.09 81.50
REMARK 500 ASP D 134 45.70 -145.68
REMARK 500 VAL D 176 111.50 -37.10
REMARK 500 GLN D 184 -133.07 -112.50
REMARK 500 ASN D 267 28.43 39.74
REMARK 500 GLU D 278 117.79 -39.11
REMARK 500 ASN D 280 120.58 -30.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CZT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE KINASE DOMAIN OF SNRK3.23 AT1G30270
REMARK 900 RELATED ID: 4CZU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE KINASE DOMAIN OF SNRK3.23 AT1G30270 T190D
REMARK 900 MUTANT
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STRUCTURE CONTAINS SOME POINT MUTATIONS.
DBREF 4D28 A 1 446 UNP Q9LDI3 CIPKO_ARATH 1 446
DBREF 4D28 B 1 446 UNP Q9LDI3 CIPKO_ARATH 1 446
DBREF 4D28 C 1 446 UNP Q9LDI3 CIPKO_ARATH 1 446
DBREF 4D28 D 1 446 UNP Q9LDI3 CIPKO_ARATH 1 446
SEQADV 4D28 LYS A 81 UNP Q9LDI3 PRO 81 ENGINEERED MUTATION
SEQADV 4D28 LYS A 107 UNP Q9LDI3 GLU 107 ENGINEERED MUTATION
SEQADV 4D28 ASP A 109 UNP Q9LDI3 SER 109 ENGINEERED MUTATION
SEQADV 4D28 SER A 127 UNP Q9LDI3 CYS 127 ENGINEERED MUTATION
SEQADV 4D28 ASN A 167 UNP Q9LDI3 ARG 167 CONFLICT
SEQADV 4D28 ASP A 168 UNP Q9LDI3 THR 168 ENGINEERED MUTATION
SEQADV 4D28 ASP A 228 UNP Q9LDI3 SER 228 ENGINEERED MUTATION
SEQADV 4D28 LYS A 266 UNP Q9LDI3 LEU 266 ENGINEERED MUTATION
SEQADV 4D28 LYS B 81 UNP Q9LDI3 PRO 81 ENGINEERED MUTATION
SEQADV 4D28 LYS B 107 UNP Q9LDI3 GLU 107 ENGINEERED MUTATION
SEQADV 4D28 ASP B 109 UNP Q9LDI3 SER 109 ENGINEERED MUTATION
SEQADV 4D28 SER B 127 UNP Q9LDI3 CYS 127 ENGINEERED MUTATION
SEQADV 4D28 ASN B 167 UNP Q9LDI3 ARG 167 CONFLICT
SEQADV 4D28 ASP B 168 UNP Q9LDI3 THR 168 ENGINEERED MUTATION
SEQADV 4D28 ASP B 228 UNP Q9LDI3 SER 228 ENGINEERED MUTATION
SEQADV 4D28 LYS B 266 UNP Q9LDI3 LEU 266 ENGINEERED MUTATION
SEQADV 4D28 LYS C 81 UNP Q9LDI3 PRO 81 ENGINEERED MUTATION
SEQADV 4D28 LYS C 107 UNP Q9LDI3 GLU 107 ENGINEERED MUTATION
SEQADV 4D28 ASP C 109 UNP Q9LDI3 SER 109 ENGINEERED MUTATION
SEQADV 4D28 SER C 127 UNP Q9LDI3 CYS 127 ENGINEERED MUTATION
SEQADV 4D28 ASN C 167 UNP Q9LDI3 ARG 167 CONFLICT
SEQADV 4D28 ASP C 168 UNP Q9LDI3 THR 168 ENGINEERED MUTATION
SEQADV 4D28 ASP C 228 UNP Q9LDI3 SER 228 ENGINEERED MUTATION
SEQADV 4D28 LYS C 266 UNP Q9LDI3 LEU 266 ENGINEERED MUTATION
SEQADV 4D28 LYS D 81 UNP Q9LDI3 PRO 81 ENGINEERED MUTATION
SEQADV 4D28 LYS D 107 UNP Q9LDI3 GLU 107 ENGINEERED MUTATION
SEQADV 4D28 ASP D 109 UNP Q9LDI3 SER 109 ENGINEERED MUTATION
SEQADV 4D28 SER D 127 UNP Q9LDI3 CYS 127 ENGINEERED MUTATION
SEQADV 4D28 ASN D 167 UNP Q9LDI3 ARG 167 CONFLICT
SEQADV 4D28 ASP D 168 UNP Q9LDI3 THR 168 ENGINEERED MUTATION
SEQADV 4D28 ASP D 228 UNP Q9LDI3 SER 228 ENGINEERED MUTATION
SEQADV 4D28 LYS D 266 UNP Q9LDI3 LEU 266 ENGINEERED MUTATION
SEQRES 1 A 446 MET THR LYS LYS MET ARG ARG VAL GLY LYS TYR GLU VAL
SEQRES 2 A 446 GLY ARG THR ILE GLY GLU GLY THR PHE ALA LYS VAL LYS
SEQRES 3 A 446 PHE ALA ARG ASN THR ASP THR GLY ASP ASN VAL ALA ILE
SEQRES 4 A 446 LYS ILE MET ALA LYS SER THR ILE LEU LYS ASN ARG MET
SEQRES 5 A 446 VAL ASP GLN ILE LYS ARG GLU ILE SER ILE MET LYS ILE
SEQRES 6 A 446 VAL ARG HIS PRO ASN ILE VAL ARG LEU TYR GLU VAL LEU
SEQRES 7 A 446 ALA SER LYS SER LYS ILE TYR ILE VAL LEU GLU PHE VAL
SEQRES 8 A 446 THR GLY GLY GLU LEU PHE ASP ARG ILE VAL HIS LYS GLY
SEQRES 9 A 446 ARG LEU LYS GLU ASP GLU SER ARG LYS TYR PHE GLN GLN
SEQRES 10 A 446 LEU VAL ASP ALA VAL ALA HIS CYS HIS SER LYS GLY VAL
SEQRES 11 A 446 TYR HIS ARG ASP LEU LYS PRO GLU ASN LEU LEU LEU ASP
SEQRES 12 A 446 THR ASN GLY ASN LEU LYS VAL SER ASP PHE GLY LEU SER
SEQRES 13 A 446 ALA LEU PRO GLN GLU GLY VAL GLU LEU LEU ASN ASP THR
SEQRES 14 A 446 CYS GLY THR PRO ASN TYR VAL ALA PRO GLU VAL LEU SER
SEQRES 15 A 446 GLY GLN GLY TYR ASP GLY SER ALA ALA ASP ILE TRP SER
SEQRES 16 A 446 CYS GLY VAL ILE LEU PHE VAL ILE LEU ALA GLY TYR LEU
SEQRES 17 A 446 PRO PHE SER GLU THR ASP LEU PRO GLY LEU TYR ARG LYS
SEQRES 18 A 446 ILE ASN ALA ALA GLU PHE ASP CYS PRO PRO TRP PHE SER
SEQRES 19 A 446 ALA GLU VAL LYS PHE LEU ILE HIS ARG ILE LEU ASP PRO
SEQRES 20 A 446 ASN PRO LYS THR ARG ILE GLN ILE GLN GLY ILE LYS LYS
SEQRES 21 A 446 ASP PRO TRP PHE ARG LYS ASN TYR VAL PRO ILE ARG ALA
SEQRES 22 A 446 ARG GLU GLU GLU GLU VAL ASN LEU ASP ASP ILE ARG ALA
SEQRES 23 A 446 VAL PHE ASP GLY ILE GLU GLY SER TYR VAL ALA GLU ASN
SEQRES 24 A 446 VAL GLU ARG ASN ASP GLU GLY PRO LEU MET MET ASN ALA
SEQRES 25 A 446 PHE GLU MET ILE THR LEU SER GLN GLY LEU ASN LEU SER
SEQRES 26 A 446 ALA LEU PHE ASP ARG ARG GLN ASP PHE VAL LYS ARG GLN
SEQRES 27 A 446 THR ARG PHE VAL SER ARG ARG GLU PRO SER GLU ILE ILE
SEQRES 28 A 446 ALA ASN ILE GLU ALA VAL ALA ASN SER MET GLY PHE LYS
SEQRES 29 A 446 SER HIS THR ARG ASN PHE LYS THR ARG LEU GLU GLY LEU
SEQRES 30 A 446 SER SER ILE LYS ALA GLY GLN LEU ALA VAL VAL ILE GLU
SEQRES 31 A 446 ILE TYR GLU VAL ALA PRO SER LEU PHE MET VAL ASP VAL
SEQRES 32 A 446 ARG LYS ALA ALA GLY GLU THR LEU GLU TYR HIS LYS PHE
SEQRES 33 A 446 TYR LYS LYS LEU CYS SER LYS LEU GLU ASN ILE ILE TRP
SEQRES 34 A 446 ARG ALA THR GLU GLY ILE PRO LYS SER GLU ILE LEU ARG
SEQRES 35 A 446 THR ILE THR PHE
SEQRES 1 B 446 MET THR LYS LYS MET ARG ARG VAL GLY LYS TYR GLU VAL
SEQRES 2 B 446 GLY ARG THR ILE GLY GLU GLY THR PHE ALA LYS VAL LYS
SEQRES 3 B 446 PHE ALA ARG ASN THR ASP THR GLY ASP ASN VAL ALA ILE
SEQRES 4 B 446 LYS ILE MET ALA LYS SER THR ILE LEU LYS ASN ARG MET
SEQRES 5 B 446 VAL ASP GLN ILE LYS ARG GLU ILE SER ILE MET LYS ILE
SEQRES 6 B 446 VAL ARG HIS PRO ASN ILE VAL ARG LEU TYR GLU VAL LEU
SEQRES 7 B 446 ALA SER LYS SER LYS ILE TYR ILE VAL LEU GLU PHE VAL
SEQRES 8 B 446 THR GLY GLY GLU LEU PHE ASP ARG ILE VAL HIS LYS GLY
SEQRES 9 B 446 ARG LEU LYS GLU ASP GLU SER ARG LYS TYR PHE GLN GLN
SEQRES 10 B 446 LEU VAL ASP ALA VAL ALA HIS CYS HIS SER LYS GLY VAL
SEQRES 11 B 446 TYR HIS ARG ASP LEU LYS PRO GLU ASN LEU LEU LEU ASP
SEQRES 12 B 446 THR ASN GLY ASN LEU LYS VAL SER ASP PHE GLY LEU SER
SEQRES 13 B 446 ALA LEU PRO GLN GLU GLY VAL GLU LEU LEU ASN ASP THR
SEQRES 14 B 446 CYS GLY THR PRO ASN TYR VAL ALA PRO GLU VAL LEU SER
SEQRES 15 B 446 GLY GLN GLY TYR ASP GLY SER ALA ALA ASP ILE TRP SER
SEQRES 16 B 446 CYS GLY VAL ILE LEU PHE VAL ILE LEU ALA GLY TYR LEU
SEQRES 17 B 446 PRO PHE SER GLU THR ASP LEU PRO GLY LEU TYR ARG LYS
SEQRES 18 B 446 ILE ASN ALA ALA GLU PHE ASP CYS PRO PRO TRP PHE SER
SEQRES 19 B 446 ALA GLU VAL LYS PHE LEU ILE HIS ARG ILE LEU ASP PRO
SEQRES 20 B 446 ASN PRO LYS THR ARG ILE GLN ILE GLN GLY ILE LYS LYS
SEQRES 21 B 446 ASP PRO TRP PHE ARG LYS ASN TYR VAL PRO ILE ARG ALA
SEQRES 22 B 446 ARG GLU GLU GLU GLU VAL ASN LEU ASP ASP ILE ARG ALA
SEQRES 23 B 446 VAL PHE ASP GLY ILE GLU GLY SER TYR VAL ALA GLU ASN
SEQRES 24 B 446 VAL GLU ARG ASN ASP GLU GLY PRO LEU MET MET ASN ALA
SEQRES 25 B 446 PHE GLU MET ILE THR LEU SER GLN GLY LEU ASN LEU SER
SEQRES 26 B 446 ALA LEU PHE ASP ARG ARG GLN ASP PHE VAL LYS ARG GLN
SEQRES 27 B 446 THR ARG PHE VAL SER ARG ARG GLU PRO SER GLU ILE ILE
SEQRES 28 B 446 ALA ASN ILE GLU ALA VAL ALA ASN SER MET GLY PHE LYS
SEQRES 29 B 446 SER HIS THR ARG ASN PHE LYS THR ARG LEU GLU GLY LEU
SEQRES 30 B 446 SER SER ILE LYS ALA GLY GLN LEU ALA VAL VAL ILE GLU
SEQRES 31 B 446 ILE TYR GLU VAL ALA PRO SER LEU PHE MET VAL ASP VAL
SEQRES 32 B 446 ARG LYS ALA ALA GLY GLU THR LEU GLU TYR HIS LYS PHE
SEQRES 33 B 446 TYR LYS LYS LEU CYS SER LYS LEU GLU ASN ILE ILE TRP
SEQRES 34 B 446 ARG ALA THR GLU GLY ILE PRO LYS SER GLU ILE LEU ARG
SEQRES 35 B 446 THR ILE THR PHE
SEQRES 1 C 446 MET THR LYS LYS MET ARG ARG VAL GLY LYS TYR GLU VAL
SEQRES 2 C 446 GLY ARG THR ILE GLY GLU GLY THR PHE ALA LYS VAL LYS
SEQRES 3 C 446 PHE ALA ARG ASN THR ASP THR GLY ASP ASN VAL ALA ILE
SEQRES 4 C 446 LYS ILE MET ALA LYS SER THR ILE LEU LYS ASN ARG MET
SEQRES 5 C 446 VAL ASP GLN ILE LYS ARG GLU ILE SER ILE MET LYS ILE
SEQRES 6 C 446 VAL ARG HIS PRO ASN ILE VAL ARG LEU TYR GLU VAL LEU
SEQRES 7 C 446 ALA SER LYS SER LYS ILE TYR ILE VAL LEU GLU PHE VAL
SEQRES 8 C 446 THR GLY GLY GLU LEU PHE ASP ARG ILE VAL HIS LYS GLY
SEQRES 9 C 446 ARG LEU LYS GLU ASP GLU SER ARG LYS TYR PHE GLN GLN
SEQRES 10 C 446 LEU VAL ASP ALA VAL ALA HIS CYS HIS SER LYS GLY VAL
SEQRES 11 C 446 TYR HIS ARG ASP LEU LYS PRO GLU ASN LEU LEU LEU ASP
SEQRES 12 C 446 THR ASN GLY ASN LEU LYS VAL SER ASP PHE GLY LEU SER
SEQRES 13 C 446 ALA LEU PRO GLN GLU GLY VAL GLU LEU LEU ASN ASP THR
SEQRES 14 C 446 CYS GLY THR PRO ASN TYR VAL ALA PRO GLU VAL LEU SER
SEQRES 15 C 446 GLY GLN GLY TYR ASP GLY SER ALA ALA ASP ILE TRP SER
SEQRES 16 C 446 CYS GLY VAL ILE LEU PHE VAL ILE LEU ALA GLY TYR LEU
SEQRES 17 C 446 PRO PHE SER GLU THR ASP LEU PRO GLY LEU TYR ARG LYS
SEQRES 18 C 446 ILE ASN ALA ALA GLU PHE ASP CYS PRO PRO TRP PHE SER
SEQRES 19 C 446 ALA GLU VAL LYS PHE LEU ILE HIS ARG ILE LEU ASP PRO
SEQRES 20 C 446 ASN PRO LYS THR ARG ILE GLN ILE GLN GLY ILE LYS LYS
SEQRES 21 C 446 ASP PRO TRP PHE ARG LYS ASN TYR VAL PRO ILE ARG ALA
SEQRES 22 C 446 ARG GLU GLU GLU GLU VAL ASN LEU ASP ASP ILE ARG ALA
SEQRES 23 C 446 VAL PHE ASP GLY ILE GLU GLY SER TYR VAL ALA GLU ASN
SEQRES 24 C 446 VAL GLU ARG ASN ASP GLU GLY PRO LEU MET MET ASN ALA
SEQRES 25 C 446 PHE GLU MET ILE THR LEU SER GLN GLY LEU ASN LEU SER
SEQRES 26 C 446 ALA LEU PHE ASP ARG ARG GLN ASP PHE VAL LYS ARG GLN
SEQRES 27 C 446 THR ARG PHE VAL SER ARG ARG GLU PRO SER GLU ILE ILE
SEQRES 28 C 446 ALA ASN ILE GLU ALA VAL ALA ASN SER MET GLY PHE LYS
SEQRES 29 C 446 SER HIS THR ARG ASN PHE LYS THR ARG LEU GLU GLY LEU
SEQRES 30 C 446 SER SER ILE LYS ALA GLY GLN LEU ALA VAL VAL ILE GLU
SEQRES 31 C 446 ILE TYR GLU VAL ALA PRO SER LEU PHE MET VAL ASP VAL
SEQRES 32 C 446 ARG LYS ALA ALA GLY GLU THR LEU GLU TYR HIS LYS PHE
SEQRES 33 C 446 TYR LYS LYS LEU CYS SER LYS LEU GLU ASN ILE ILE TRP
SEQRES 34 C 446 ARG ALA THR GLU GLY ILE PRO LYS SER GLU ILE LEU ARG
SEQRES 35 C 446 THR ILE THR PHE
SEQRES 1 D 446 MET THR LYS LYS MET ARG ARG VAL GLY LYS TYR GLU VAL
SEQRES 2 D 446 GLY ARG THR ILE GLY GLU GLY THR PHE ALA LYS VAL LYS
SEQRES 3 D 446 PHE ALA ARG ASN THR ASP THR GLY ASP ASN VAL ALA ILE
SEQRES 4 D 446 LYS ILE MET ALA LYS SER THR ILE LEU LYS ASN ARG MET
SEQRES 5 D 446 VAL ASP GLN ILE LYS ARG GLU ILE SER ILE MET LYS ILE
SEQRES 6 D 446 VAL ARG HIS PRO ASN ILE VAL ARG LEU TYR GLU VAL LEU
SEQRES 7 D 446 ALA SER LYS SER LYS ILE TYR ILE VAL LEU GLU PHE VAL
SEQRES 8 D 446 THR GLY GLY GLU LEU PHE ASP ARG ILE VAL HIS LYS GLY
SEQRES 9 D 446 ARG LEU LYS GLU ASP GLU SER ARG LYS TYR PHE GLN GLN
SEQRES 10 D 446 LEU VAL ASP ALA VAL ALA HIS CYS HIS SER LYS GLY VAL
SEQRES 11 D 446 TYR HIS ARG ASP LEU LYS PRO GLU ASN LEU LEU LEU ASP
SEQRES 12 D 446 THR ASN GLY ASN LEU LYS VAL SER ASP PHE GLY LEU SER
SEQRES 13 D 446 ALA LEU PRO GLN GLU GLY VAL GLU LEU LEU ASN ASP THR
SEQRES 14 D 446 CYS GLY THR PRO ASN TYR VAL ALA PRO GLU VAL LEU SER
SEQRES 15 D 446 GLY GLN GLY TYR ASP GLY SER ALA ALA ASP ILE TRP SER
SEQRES 16 D 446 CYS GLY VAL ILE LEU PHE VAL ILE LEU ALA GLY TYR LEU
SEQRES 17 D 446 PRO PHE SER GLU THR ASP LEU PRO GLY LEU TYR ARG LYS
SEQRES 18 D 446 ILE ASN ALA ALA GLU PHE ASP CYS PRO PRO TRP PHE SER
SEQRES 19 D 446 ALA GLU VAL LYS PHE LEU ILE HIS ARG ILE LEU ASP PRO
SEQRES 20 D 446 ASN PRO LYS THR ARG ILE GLN ILE GLN GLY ILE LYS LYS
SEQRES 21 D 446 ASP PRO TRP PHE ARG LYS ASN TYR VAL PRO ILE ARG ALA
SEQRES 22 D 446 ARG GLU GLU GLU GLU VAL ASN LEU ASP ASP ILE ARG ALA
SEQRES 23 D 446 VAL PHE ASP GLY ILE GLU GLY SER TYR VAL ALA GLU ASN
SEQRES 24 D 446 VAL GLU ARG ASN ASP GLU GLY PRO LEU MET MET ASN ALA
SEQRES 25 D 446 PHE GLU MET ILE THR LEU SER GLN GLY LEU ASN LEU SER
SEQRES 26 D 446 ALA LEU PHE ASP ARG ARG GLN ASP PHE VAL LYS ARG GLN
SEQRES 27 D 446 THR ARG PHE VAL SER ARG ARG GLU PRO SER GLU ILE ILE
SEQRES 28 D 446 ALA ASN ILE GLU ALA VAL ALA ASN SER MET GLY PHE LYS
SEQRES 29 D 446 SER HIS THR ARG ASN PHE LYS THR ARG LEU GLU GLY LEU
SEQRES 30 D 446 SER SER ILE LYS ALA GLY GLN LEU ALA VAL VAL ILE GLU
SEQRES 31 D 446 ILE TYR GLU VAL ALA PRO SER LEU PHE MET VAL ASP VAL
SEQRES 32 D 446 ARG LYS ALA ALA GLY GLU THR LEU GLU TYR HIS LYS PHE
SEQRES 33 D 446 TYR LYS LYS LEU CYS SER LYS LEU GLU ASN ILE ILE TRP
SEQRES 34 D 446 ARG ALA THR GLU GLY ILE PRO LYS SER GLU ILE LEU ARG
SEQRES 35 D 446 THR ILE THR PHE
HELIX 1 1 LYS A 44 LYS A 49 1 6
HELIX 2 2 MET A 52 VAL A 66 1 15
HELIX 3 3 LEU A 96 GLY A 104 1 9
HELIX 4 4 LYS A 107 LYS A 128 1 22
HELIX 5 5 ALA A 177 GLY A 183 1 7
HELIX 6 6 ASP A 187 GLY A 206 1 20
HELIX 7 7 ASP A 214 ALA A 225 1 12
HELIX 8 8 SER A 234 LEU A 245 1 12
HELIX 9 9 GLN A 254 ASP A 261 1 8
HELIX 10 10 ASP A 261 LYS A 266 1 6
HELIX 11 11 ASN A 280 VAL A 287 1 8
HELIX 12 12 LYS B 44 LYS B 49 1 6
HELIX 13 13 MET B 52 VAL B 66 1 15
HELIX 14 14 LEU B 96 GLY B 104 1 9
HELIX 15 15 LYS B 107 GLY B 129 1 23
HELIX 16 16 LYS B 136 GLU B 138 5 3
HELIX 17 17 ALA B 177 SER B 182 1 6
HELIX 18 18 ASP B 187 GLY B 206 1 20
HELIX 19 19 ASP B 214 ALA B 225 1 12
HELIX 20 20 SER B 234 LEU B 245 1 12
HELIX 21 21 GLN B 254 LYS B 260 1 7
HELIX 22 22 ASP B 261 LYS B 266 1 6
HELIX 23 23 ASN B 280 VAL B 287 1 8
HELIX 24 24 LYS C 44 LYS C 49 1 6
HELIX 25 25 MET C 52 VAL C 66 1 15
HELIX 26 26 GLU C 95 GLY C 104 1 10
HELIX 27 27 LYS C 107 LYS C 128 1 22
HELIX 28 28 LYS C 136 GLU C 138 5 3
HELIX 29 29 ALA C 177 GLY C 183 1 7
HELIX 30 30 ASP C 187 GLY C 206 1 20
HELIX 31 31 ASP C 214 ALA C 225 1 12
HELIX 32 32 SER C 234 LEU C 245 1 12
HELIX 33 33 GLN C 254 LYS C 260 1 7
HELIX 34 34 ASP C 261 LYS C 266 1 6
HELIX 35 35 ASN C 280 VAL C 287 1 8
HELIX 36 36 THR D 31 GLY D 34 5 4
HELIX 37 37 LYS D 44 LYS D 49 1 6
HELIX 38 38 MET D 52 ILE D 65 1 14
HELIX 39 39 GLU D 95 GLY D 104 1 10
HELIX 40 40 LYS D 107 LYS D 128 1 22
HELIX 41 41 ALA D 177 GLY D 183 1 7
HELIX 42 42 ASP D 187 GLY D 206 1 20
HELIX 43 43 ASP D 214 ALA D 225 1 12
HELIX 44 44 SER D 234 LEU D 245 1 12
HELIX 45 45 GLN D 254 LYS D 260 1 7
HELIX 46 46 ASP D 261 LYS D 266 1 6
HELIX 47 47 ASN D 280 VAL D 287 1 8
SHEET 1 AA 5 TYR A 11 VAL A 13 0
SHEET 2 AA 5 LYS A 24 ASN A 30 -1 O ARG A 29 N GLU A 12
SHEET 3 AA 5 ASP A 35 ALA A 43 -1 O ASP A 35 N ASN A 30
SHEET 4 AA 5 LYS A 83 LEU A 88 -1 O ILE A 84 N MET A 42
SHEET 5 AA 5 VAL A 77 ALA A 79 -1 O LEU A 78 N TYR A 85
SHEET 1 AB 3 GLY A 94 GLU A 95 0
SHEET 2 AB 3 LEU A 140 LEU A 142 -1 O LEU A 142 N GLY A 94
SHEET 3 AB 3 LEU A 148 VAL A 150 -1 O LYS A 149 N LEU A 141
SHEET 1 BA 5 TYR B 11 VAL B 13 0
SHEET 2 BA 5 LYS B 24 ASN B 30 -1 O ARG B 29 N GLU B 12
SHEET 3 BA 5 ASN B 36 ALA B 43 -1 O VAL B 37 N ALA B 28
SHEET 4 BA 5 LYS B 83 GLU B 89 -1 O ILE B 84 N MET B 42
SHEET 5 BA 5 LEU B 74 ALA B 79 -1 O GLU B 76 N VAL B 87
SHEET 1 BB 2 LEU B 140 LEU B 142 0
SHEET 2 BB 2 LEU B 148 VAL B 150 -1 O LYS B 149 N LEU B 141
SHEET 1 CA 5 GLU C 12 VAL C 13 0
SHEET 2 CA 5 LYS C 24 ARG C 29 -1 O ARG C 29 N GLU C 12
SHEET 3 CA 5 ASN C 36 ALA C 43 -1 O VAL C 37 N ALA C 28
SHEET 4 CA 5 LYS C 83 GLU C 89 -1 O ILE C 84 N MET C 42
SHEET 5 CA 5 LEU C 74 ALA C 79 -1 N TYR C 75 O VAL C 87
SHEET 1 CB 2 LEU C 140 LEU C 142 0
SHEET 2 CB 2 LEU C 148 VAL C 150 -1 O LYS C 149 N LEU C 141
SHEET 1 DA 2 GLU D 12 VAL D 13 0
SHEET 2 DA 2 ALA D 28 ARG D 29 -1 O ARG D 29 N GLU D 12
SHEET 1 DB 4 LYS D 24 LYS D 26 0
SHEET 2 DB 4 ILE D 39 ALA D 43 -1 O ILE D 39 N LYS D 26
SHEET 3 DB 4 LYS D 83 LEU D 88 -1 O ILE D 84 N MET D 42
SHEET 4 DB 4 LEU D 74 ALA D 79 -1 N TYR D 75 O VAL D 87
SHEET 1 DC 2 LEU D 140 LEU D 142 0
SHEET 2 DC 2 LEU D 148 VAL D 150 -1 O LYS D 149 N LEU D 141
CISPEP 1 ARG A 15 THR A 16 0 -24.34
CISPEP 2 GLU A 161 GLY A 162 0 -6.94
CISPEP 3 ARG B 15 THR B 16 0 -20.32
CISPEP 4 ARG C 15 THR C 16 0 -21.58
CISPEP 5 ARG D 15 THR D 16 0 -11.87
CISPEP 6 GLY D 171 THR D 172 0 3.46
CRYST1 69.111 71.353 77.834 104.85 100.32 118.96 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014469 0.008007 0.006352 0.00000
SCALE2 0.000000 0.016018 0.006960 0.00000
SCALE3 0.000000 0.000000 0.014239 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
