HEADER TRANSFERASE/TRANSFERASE INHIBITOR 31-JUL-17 5WNF
TITLE X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A
TITLE 2 HIGHLY SELECTIVE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 6-415;
COMPND 5 SYNONYM: RENAL CARCINOMA ANTIGEN NY-REN-35,RHO-ASSOCIATED,COILED-
COMPND 6 COIL-CONTAINING PROTEIN KINASE 1,COILED-COIL-CONTAINING PROTEIN
COMPND 7 KINASE I,ROCK-I,P160 ROCK-1,P160ROCK;
COMPND 8 EC: 2.7.11.1;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: N-TERMINAL AND KINASE DOMAIN, RESIDUES 6-415
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ROCK1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS RHO KINASE, KINASE INHIBITOR, PHOSPHORYLATION, TRANSFERASE-INHIBITOR
KEYWDS 2 COMPLEX, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LI
REVDAT 2 13-MAR-24 5WNF 1 REMARK
REVDAT 1 01-AUG-18 5WNF 0
JRNL AUTH X.LI,D.MARSHALL,R.SIBLEY,T.BOSANAC,J.GINN,S.KUGLER,
JRNL AUTH 2 E.GAUTSCHI,T.MOLINARO,L.SOLEYMANZADEH,C.K.SHIH,E.R.R.YOUNG
JRNL TITL NOVEL MECHANISM OF RHO KINASE SELECTIVITY: BEYOND THE ATP
JRNL TITL 2 POCKET
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 74094
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 3639
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.38
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5364
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2530
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5088
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.15
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 276
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12522
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 152
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 84.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.68690
REMARK 3 B22 (A**2) : 2.96540
REMARK 3 B33 (A**2) : -4.65230
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.42950
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.410
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.407
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.244
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.435
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.252
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 13005 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17574 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4556 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 348 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1854 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 13005 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1580 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 14305 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.41
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.14
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1490 -1.2744 40.4498
REMARK 3 T TENSOR
REMARK 3 T11: -0.3227 T22: -0.1520
REMARK 3 T33: -0.1098 T12: -0.0791
REMARK 3 T13: -0.0231 T23: 0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 0.9063 L22: 1.8014
REMARK 3 L33: 2.3233 L12: 0.0425
REMARK 3 L13: 0.5007 L23: 0.4142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: 0.0800 S13: 0.2091
REMARK 3 S21: -0.2013 S22: 0.0715 S23: -0.2325
REMARK 3 S31: -0.2086 S32: 0.3906 S33: -0.0238
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3479 -15.2644 -12.2588
REMARK 3 T TENSOR
REMARK 3 T11: 0.1260 T22: -0.4423
REMARK 3 T33: -0.4941 T12: 0.3409
REMARK 3 T13: -0.0977 T23: -0.0625
REMARK 3 L TENSOR
REMARK 3 L11: 1.5354 L22: 3.1489
REMARK 3 L33: 5.8900 L12: -0.7301
REMARK 3 L13: -0.3474 L23: -0.6118
REMARK 3 S TENSOR
REMARK 3 S11: 0.3848 S12: 0.4040 S13: -0.2604
REMARK 3 S21: -1.3218 S22: -0.7072 S23: 0.3275
REMARK 3 S31: 0.2004 S32: -0.3021 S33: 0.3224
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -62.0369 -18.7441 28.3160
REMARK 3 T TENSOR
REMARK 3 T11: -0.2450 T22: -0.1841
REMARK 3 T33: -0.2928 T12: -0.1658
REMARK 3 T13: -0.0373 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 1.5658 L22: 1.8350
REMARK 3 L33: 3.2494 L12: 0.7114
REMARK 3 L13: -0.2171 L23: 0.2297
REMARK 3 S TENSOR
REMARK 3 S11: -0.2949 S12: 0.5385 S13: -0.0455
REMARK 3 S21: -0.7317 S22: 0.2954 S23: 0.1767
REMARK 3 S31: 0.1418 S32: -0.2956 S33: -0.0004
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -61.3994 -27.7629 82.2790
REMARK 3 T TENSOR
REMARK 3 T11: -0.2534 T22: -0.1591
REMARK 3 T33: -0.0874 T12: -0.0144
REMARK 3 T13: -0.0388 T23: -0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 0.8053 L22: 1.6455
REMARK 3 L33: 1.8513 L12: 0.1932
REMARK 3 L13: 0.2333 L23: -0.3704
REMARK 3 S TENSOR
REMARK 3 S11: 0.0784 S12: 0.0245 S13: -0.2575
REMARK 3 S21: 0.1667 S22: 0.0959 S23: -0.1756
REMARK 3 S31: 0.3026 S32: -0.0492 S33: -0.1743
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5WNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74142
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 39.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.780
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.71
REMARK 200 R MERGE FOR SHELL (I) : 0.63700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8.5% PEG3350, 0.1M MES, 50 MM CACL2,
REMARK 280 PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 81.45250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.14600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.45250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.14600
REMARK 290 SMTRY3 4 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: 4620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 HIS A 4
REMARK 465 MET A 5
REMARK 465 SER A 6
REMARK 465 ASN A 402
REMARK 465 ARG A 403
REMARK 465 ARG A 404
REMARK 465 TYR A 405
REMARK 465 LEU A 406
REMARK 465 SER A 407
REMARK 465 SER A 408
REMARK 465 ALA A 409
REMARK 465 ASN A 410
REMARK 465 PRO A 411
REMARK 465 ASN A 412
REMARK 465 ASP A 413
REMARK 465 ASN A 414
REMARK 465 ARG A 415
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 LEU B 3
REMARK 465 HIS B 4
REMARK 465 ARG B 230
REMARK 465 CYS B 231
REMARK 465 ASP B 232
REMARK 465 THR B 233
REMARK 465 ALA B 234
REMARK 465 VAL B 235
REMARK 465 GLY B 236
REMARK 465 SER B 248
REMARK 465 GLN B 249
REMARK 465 GLY B 250
REMARK 465 GLY B 251
REMARK 465 ASP B 252
REMARK 465 GLY B 253
REMARK 465 PHE B 299
REMARK 465 PRO B 300
REMARK 465 ASP B 301
REMARK 465 ASP B 302
REMARK 465 ASN B 303
REMARK 465 ASP B 304
REMARK 465 THR B 318
REMARK 465 ASP B 319
REMARK 465 ARG B 320
REMARK 465 GLU B 321
REMARK 465 VAL B 322
REMARK 465 ARG B 323
REMARK 465 LEU B 324
REMARK 465 GLY B 325
REMARK 465 ARG B 326
REMARK 465 ASN B 327
REMARK 465 GLY B 328
REMARK 465 LEU B 371
REMARK 465 GLU B 372
REMARK 465 GLU B 373
REMARK 465 ASP B 374
REMARK 465 LYS B 375
REMARK 465 GLY B 376
REMARK 465 GLU B 377
REMARK 465 GLU B 378
REMARK 465 GLU B 379
REMARK 465 THR B 380
REMARK 465 ARG B 403
REMARK 465 ARG B 404
REMARK 465 TYR B 405
REMARK 465 LEU B 406
REMARK 465 SER B 407
REMARK 465 SER B 408
REMARK 465 ALA B 409
REMARK 465 ASN B 410
REMARK 465 PRO B 411
REMARK 465 ASN B 412
REMARK 465 ASP B 413
REMARK 465 ASN B 414
REMARK 465 ARG B 415
REMARK 465 GLY C 1
REMARK 465 SER C 2
REMARK 465 LEU C 3
REMARK 465 LYS C 247
REMARK 465 SER C 248
REMARK 465 GLN C 249
REMARK 465 GLY C 250
REMARK 465 GLY C 251
REMARK 465 ASP C 301
REMARK 465 ASP C 302
REMARK 465 ASN C 303
REMARK 465 ASP C 304
REMARK 465 GLU C 373
REMARK 465 ASP C 374
REMARK 465 LYS C 375
REMARK 465 GLY C 376
REMARK 465 ARG C 403
REMARK 465 ARG C 404
REMARK 465 TYR C 405
REMARK 465 LEU C 406
REMARK 465 SER C 407
REMARK 465 SER C 408
REMARK 465 ALA C 409
REMARK 465 ASN C 410
REMARK 465 PRO C 411
REMARK 465 ASN C 412
REMARK 465 ASP C 413
REMARK 465 ASN C 414
REMARK 465 ARG C 415
REMARK 465 GLY D 1
REMARK 465 SER D 2
REMARK 465 LEU D 3
REMARK 465 HIS D 4
REMARK 465 MET D 5
REMARK 465 SER D 6
REMARK 465 ARG D 403
REMARK 465 ARG D 404
REMARK 465 TYR D 405
REMARK 465 LEU D 406
REMARK 465 SER D 407
REMARK 465 SER D 408
REMARK 465 ALA D 409
REMARK 465 ASN D 410
REMARK 465 PRO D 411
REMARK 465 ASN D 412
REMARK 465 ASP D 413
REMARK 465 ASN D 414
REMARK 465 ARG D 415
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 ARG A 10 -36.33 -130.96
REMARK 500 ASP A 198 51.88 -150.52
REMARK 500 GLU A 378 -133.91 -84.66
REMARK 500 TYR A 400 -78.31 -127.68
REMARK 500 PHE B 7 120.49 -39.08
REMARK 500 ASP B 198 47.25 -150.53
REMARK 500 MET B 223 81.27 -61.13
REMARK 500 ASN B 224 -120.54 9.21
REMARK 500 TYR B 240 -7.90 -58.39
REMARK 500 ASP C 198 45.59 -151.29
REMARK 500 ASP D 198 46.91 -151.80
REMARK 500 GLN D 249 96.78 -55.45
REMARK 500 LEU D 317 56.83 -95.31
REMARK 500 GLU D 372 96.22 -60.26
REMARK 500 GLU D 373 87.68 -55.49
REMARK 500 GLU D 378 -129.48 -122.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B4V A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B4V B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B4V C 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B4V D 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5WNE RELATED DB: PDB
REMARK 900 RELATED ID: 5WNG RELATED DB: PDB
REMARK 900 RELATED ID: 5WNH RELATED DB: PDB
DBREF 5WNF A 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 5WNF B 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 5WNF C 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 5WNF D 6 415 UNP Q13464 ROCK1_HUMAN 6 415
SEQADV 5WNF GLY A 1 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF SER A 2 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF LEU A 3 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF HIS A 4 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF MET A 5 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF GLY B 1 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF SER B 2 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF LEU B 3 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF HIS B 4 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF MET B 5 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF GLY C 1 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF SER C 2 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF LEU C 3 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF HIS C 4 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF MET C 5 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF GLY D 1 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF SER D 2 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF LEU D 3 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF HIS D 4 UNP Q13464 EXPRESSION TAG
SEQADV 5WNF MET D 5 UNP Q13464 EXPRESSION TAG
SEQRES 1 A 415 GLY SER LEU HIS MET SER PHE GLU THR ARG PHE GLU LYS
SEQRES 2 A 415 MET ASP ASN LEU LEU ARG ASP PRO LYS SER GLU VAL ASN
SEQRES 3 A 415 SER ASP CYS LEU LEU ASP GLY LEU ASP ALA LEU VAL TYR
SEQRES 4 A 415 ASP LEU ASP PHE PRO ALA LEU ARG LYS ASN LYS ASN ILE
SEQRES 5 A 415 ASP ASN PHE LEU SER ARG TYR LYS ASP THR ILE ASN LYS
SEQRES 6 A 415 ILE ARG ASP LEU ARG MET LYS ALA GLU ASP TYR GLU VAL
SEQRES 7 A 415 VAL LYS VAL ILE GLY ARG GLY ALA PHE GLY GLU VAL GLN
SEQRES 8 A 415 LEU VAL ARG HIS LYS SER THR ARG LYS VAL TYR ALA MET
SEQRES 9 A 415 LYS LEU LEU SER LYS PHE GLU MET ILE LYS ARG SER ASP
SEQRES 10 A 415 SER ALA PHE PHE TRP GLU GLU ARG ASP ILE MET ALA PHE
SEQRES 11 A 415 ALA ASN SER PRO TRP VAL VAL GLN LEU PHE TYR ALA PHE
SEQRES 12 A 415 GLN ASP ASP ARG TYR LEU TYR MET VAL MET GLU TYR MET
SEQRES 13 A 415 PRO GLY GLY ASP LEU VAL ASN LEU MET SER ASN TYR ASP
SEQRES 14 A 415 VAL PRO GLU LYS TRP ALA ARG PHE TYR THR ALA GLU VAL
SEQRES 15 A 415 VAL LEU ALA LEU ASP ALA ILE HIS SER MET GLY PHE ILE
SEQRES 16 A 415 HIS ARG ASP VAL LYS PRO ASP ASN MET LEU LEU ASP LYS
SEQRES 17 A 415 SER GLY HIS LEU LYS LEU ALA ASP PHE GLY THR CYS MET
SEQRES 18 A 415 LYS MET ASN LYS GLU GLY MET VAL ARG CYS ASP THR ALA
SEQRES 19 A 415 VAL GLY THR PRO ASP TYR ILE SER PRO GLU VAL LEU LYS
SEQRES 20 A 415 SER GLN GLY GLY ASP GLY TYR TYR GLY ARG GLU CYS ASP
SEQRES 21 A 415 TRP TRP SER VAL GLY VAL PHE LEU TYR GLU MET LEU VAL
SEQRES 22 A 415 GLY ASP THR PRO PHE TYR ALA ASP SER LEU VAL GLY THR
SEQRES 23 A 415 TYR SER LYS ILE MET ASN HIS LYS ASN SER LEU THR PHE
SEQRES 24 A 415 PRO ASP ASP ASN ASP ILE SER LYS GLU ALA LYS ASN LEU
SEQRES 25 A 415 ILE CYS ALA PHE LEU THR ASP ARG GLU VAL ARG LEU GLY
SEQRES 26 A 415 ARG ASN GLY VAL GLU GLU ILE LYS ARG HIS LEU PHE PHE
SEQRES 27 A 415 LYS ASN ASP GLN TRP ALA TRP GLU THR LEU ARG ASP THR
SEQRES 28 A 415 VAL ALA PRO VAL VAL PRO ASP LEU SER SER ASP ILE ASP
SEQRES 29 A 415 THR SER ASN PHE ASP ASP LEU GLU GLU ASP LYS GLY GLU
SEQRES 30 A 415 GLU GLU THR PHE PRO ILE PRO LYS ALA PHE VAL GLY ASN
SEQRES 31 A 415 GLN LEU PRO PHE VAL GLY PHE THR TYR TYR SER ASN ARG
SEQRES 32 A 415 ARG TYR LEU SER SER ALA ASN PRO ASN ASP ASN ARG
SEQRES 1 B 415 GLY SER LEU HIS MET SER PHE GLU THR ARG PHE GLU LYS
SEQRES 2 B 415 MET ASP ASN LEU LEU ARG ASP PRO LYS SER GLU VAL ASN
SEQRES 3 B 415 SER ASP CYS LEU LEU ASP GLY LEU ASP ALA LEU VAL TYR
SEQRES 4 B 415 ASP LEU ASP PHE PRO ALA LEU ARG LYS ASN LYS ASN ILE
SEQRES 5 B 415 ASP ASN PHE LEU SER ARG TYR LYS ASP THR ILE ASN LYS
SEQRES 6 B 415 ILE ARG ASP LEU ARG MET LYS ALA GLU ASP TYR GLU VAL
SEQRES 7 B 415 VAL LYS VAL ILE GLY ARG GLY ALA PHE GLY GLU VAL GLN
SEQRES 8 B 415 LEU VAL ARG HIS LYS SER THR ARG LYS VAL TYR ALA MET
SEQRES 9 B 415 LYS LEU LEU SER LYS PHE GLU MET ILE LYS ARG SER ASP
SEQRES 10 B 415 SER ALA PHE PHE TRP GLU GLU ARG ASP ILE MET ALA PHE
SEQRES 11 B 415 ALA ASN SER PRO TRP VAL VAL GLN LEU PHE TYR ALA PHE
SEQRES 12 B 415 GLN ASP ASP ARG TYR LEU TYR MET VAL MET GLU TYR MET
SEQRES 13 B 415 PRO GLY GLY ASP LEU VAL ASN LEU MET SER ASN TYR ASP
SEQRES 14 B 415 VAL PRO GLU LYS TRP ALA ARG PHE TYR THR ALA GLU VAL
SEQRES 15 B 415 VAL LEU ALA LEU ASP ALA ILE HIS SER MET GLY PHE ILE
SEQRES 16 B 415 HIS ARG ASP VAL LYS PRO ASP ASN MET LEU LEU ASP LYS
SEQRES 17 B 415 SER GLY HIS LEU LYS LEU ALA ASP PHE GLY THR CYS MET
SEQRES 18 B 415 LYS MET ASN LYS GLU GLY MET VAL ARG CYS ASP THR ALA
SEQRES 19 B 415 VAL GLY THR PRO ASP TYR ILE SER PRO GLU VAL LEU LYS
SEQRES 20 B 415 SER GLN GLY GLY ASP GLY TYR TYR GLY ARG GLU CYS ASP
SEQRES 21 B 415 TRP TRP SER VAL GLY VAL PHE LEU TYR GLU MET LEU VAL
SEQRES 22 B 415 GLY ASP THR PRO PHE TYR ALA ASP SER LEU VAL GLY THR
SEQRES 23 B 415 TYR SER LYS ILE MET ASN HIS LYS ASN SER LEU THR PHE
SEQRES 24 B 415 PRO ASP ASP ASN ASP ILE SER LYS GLU ALA LYS ASN LEU
SEQRES 25 B 415 ILE CYS ALA PHE LEU THR ASP ARG GLU VAL ARG LEU GLY
SEQRES 26 B 415 ARG ASN GLY VAL GLU GLU ILE LYS ARG HIS LEU PHE PHE
SEQRES 27 B 415 LYS ASN ASP GLN TRP ALA TRP GLU THR LEU ARG ASP THR
SEQRES 28 B 415 VAL ALA PRO VAL VAL PRO ASP LEU SER SER ASP ILE ASP
SEQRES 29 B 415 THR SER ASN PHE ASP ASP LEU GLU GLU ASP LYS GLY GLU
SEQRES 30 B 415 GLU GLU THR PHE PRO ILE PRO LYS ALA PHE VAL GLY ASN
SEQRES 31 B 415 GLN LEU PRO PHE VAL GLY PHE THR TYR TYR SER ASN ARG
SEQRES 32 B 415 ARG TYR LEU SER SER ALA ASN PRO ASN ASP ASN ARG
SEQRES 1 C 415 GLY SER LEU HIS MET SER PHE GLU THR ARG PHE GLU LYS
SEQRES 2 C 415 MET ASP ASN LEU LEU ARG ASP PRO LYS SER GLU VAL ASN
SEQRES 3 C 415 SER ASP CYS LEU LEU ASP GLY LEU ASP ALA LEU VAL TYR
SEQRES 4 C 415 ASP LEU ASP PHE PRO ALA LEU ARG LYS ASN LYS ASN ILE
SEQRES 5 C 415 ASP ASN PHE LEU SER ARG TYR LYS ASP THR ILE ASN LYS
SEQRES 6 C 415 ILE ARG ASP LEU ARG MET LYS ALA GLU ASP TYR GLU VAL
SEQRES 7 C 415 VAL LYS VAL ILE GLY ARG GLY ALA PHE GLY GLU VAL GLN
SEQRES 8 C 415 LEU VAL ARG HIS LYS SER THR ARG LYS VAL TYR ALA MET
SEQRES 9 C 415 LYS LEU LEU SER LYS PHE GLU MET ILE LYS ARG SER ASP
SEQRES 10 C 415 SER ALA PHE PHE TRP GLU GLU ARG ASP ILE MET ALA PHE
SEQRES 11 C 415 ALA ASN SER PRO TRP VAL VAL GLN LEU PHE TYR ALA PHE
SEQRES 12 C 415 GLN ASP ASP ARG TYR LEU TYR MET VAL MET GLU TYR MET
SEQRES 13 C 415 PRO GLY GLY ASP LEU VAL ASN LEU MET SER ASN TYR ASP
SEQRES 14 C 415 VAL PRO GLU LYS TRP ALA ARG PHE TYR THR ALA GLU VAL
SEQRES 15 C 415 VAL LEU ALA LEU ASP ALA ILE HIS SER MET GLY PHE ILE
SEQRES 16 C 415 HIS ARG ASP VAL LYS PRO ASP ASN MET LEU LEU ASP LYS
SEQRES 17 C 415 SER GLY HIS LEU LYS LEU ALA ASP PHE GLY THR CYS MET
SEQRES 18 C 415 LYS MET ASN LYS GLU GLY MET VAL ARG CYS ASP THR ALA
SEQRES 19 C 415 VAL GLY THR PRO ASP TYR ILE SER PRO GLU VAL LEU LYS
SEQRES 20 C 415 SER GLN GLY GLY ASP GLY TYR TYR GLY ARG GLU CYS ASP
SEQRES 21 C 415 TRP TRP SER VAL GLY VAL PHE LEU TYR GLU MET LEU VAL
SEQRES 22 C 415 GLY ASP THR PRO PHE TYR ALA ASP SER LEU VAL GLY THR
SEQRES 23 C 415 TYR SER LYS ILE MET ASN HIS LYS ASN SER LEU THR PHE
SEQRES 24 C 415 PRO ASP ASP ASN ASP ILE SER LYS GLU ALA LYS ASN LEU
SEQRES 25 C 415 ILE CYS ALA PHE LEU THR ASP ARG GLU VAL ARG LEU GLY
SEQRES 26 C 415 ARG ASN GLY VAL GLU GLU ILE LYS ARG HIS LEU PHE PHE
SEQRES 27 C 415 LYS ASN ASP GLN TRP ALA TRP GLU THR LEU ARG ASP THR
SEQRES 28 C 415 VAL ALA PRO VAL VAL PRO ASP LEU SER SER ASP ILE ASP
SEQRES 29 C 415 THR SER ASN PHE ASP ASP LEU GLU GLU ASP LYS GLY GLU
SEQRES 30 C 415 GLU GLU THR PHE PRO ILE PRO LYS ALA PHE VAL GLY ASN
SEQRES 31 C 415 GLN LEU PRO PHE VAL GLY PHE THR TYR TYR SER ASN ARG
SEQRES 32 C 415 ARG TYR LEU SER SER ALA ASN PRO ASN ASP ASN ARG
SEQRES 1 D 415 GLY SER LEU HIS MET SER PHE GLU THR ARG PHE GLU LYS
SEQRES 2 D 415 MET ASP ASN LEU LEU ARG ASP PRO LYS SER GLU VAL ASN
SEQRES 3 D 415 SER ASP CYS LEU LEU ASP GLY LEU ASP ALA LEU VAL TYR
SEQRES 4 D 415 ASP LEU ASP PHE PRO ALA LEU ARG LYS ASN LYS ASN ILE
SEQRES 5 D 415 ASP ASN PHE LEU SER ARG TYR LYS ASP THR ILE ASN LYS
SEQRES 6 D 415 ILE ARG ASP LEU ARG MET LYS ALA GLU ASP TYR GLU VAL
SEQRES 7 D 415 VAL LYS VAL ILE GLY ARG GLY ALA PHE GLY GLU VAL GLN
SEQRES 8 D 415 LEU VAL ARG HIS LYS SER THR ARG LYS VAL TYR ALA MET
SEQRES 9 D 415 LYS LEU LEU SER LYS PHE GLU MET ILE LYS ARG SER ASP
SEQRES 10 D 415 SER ALA PHE PHE TRP GLU GLU ARG ASP ILE MET ALA PHE
SEQRES 11 D 415 ALA ASN SER PRO TRP VAL VAL GLN LEU PHE TYR ALA PHE
SEQRES 12 D 415 GLN ASP ASP ARG TYR LEU TYR MET VAL MET GLU TYR MET
SEQRES 13 D 415 PRO GLY GLY ASP LEU VAL ASN LEU MET SER ASN TYR ASP
SEQRES 14 D 415 VAL PRO GLU LYS TRP ALA ARG PHE TYR THR ALA GLU VAL
SEQRES 15 D 415 VAL LEU ALA LEU ASP ALA ILE HIS SER MET GLY PHE ILE
SEQRES 16 D 415 HIS ARG ASP VAL LYS PRO ASP ASN MET LEU LEU ASP LYS
SEQRES 17 D 415 SER GLY HIS LEU LYS LEU ALA ASP PHE GLY THR CYS MET
SEQRES 18 D 415 LYS MET ASN LYS GLU GLY MET VAL ARG CYS ASP THR ALA
SEQRES 19 D 415 VAL GLY THR PRO ASP TYR ILE SER PRO GLU VAL LEU LYS
SEQRES 20 D 415 SER GLN GLY GLY ASP GLY TYR TYR GLY ARG GLU CYS ASP
SEQRES 21 D 415 TRP TRP SER VAL GLY VAL PHE LEU TYR GLU MET LEU VAL
SEQRES 22 D 415 GLY ASP THR PRO PHE TYR ALA ASP SER LEU VAL GLY THR
SEQRES 23 D 415 TYR SER LYS ILE MET ASN HIS LYS ASN SER LEU THR PHE
SEQRES 24 D 415 PRO ASP ASP ASN ASP ILE SER LYS GLU ALA LYS ASN LEU
SEQRES 25 D 415 ILE CYS ALA PHE LEU THR ASP ARG GLU VAL ARG LEU GLY
SEQRES 26 D 415 ARG ASN GLY VAL GLU GLU ILE LYS ARG HIS LEU PHE PHE
SEQRES 27 D 415 LYS ASN ASP GLN TRP ALA TRP GLU THR LEU ARG ASP THR
SEQRES 28 D 415 VAL ALA PRO VAL VAL PRO ASP LEU SER SER ASP ILE ASP
SEQRES 29 D 415 THR SER ASN PHE ASP ASP LEU GLU GLU ASP LYS GLY GLU
SEQRES 30 D 415 GLU GLU THR PHE PRO ILE PRO LYS ALA PHE VAL GLY ASN
SEQRES 31 D 415 GLN LEU PRO PHE VAL GLY PHE THR TYR TYR SER ASN ARG
SEQRES 32 D 415 ARG TYR LEU SER SER ALA ASN PRO ASN ASP ASN ARG
HET B4V A 501 35
HET GOL A 502 6
HET GOL A 503 6
HET B4V B 900 35
HET B4V C 900 35
HET B4V D 900 35
HETNAM B4V 1-(4-AMINO-1,2,5-OXADIAZOL-3-YL)-5-METHYL-N-({3-[(5-
HETNAM 2 B4V METHYL-4,5,6,7-TETRAHYDRO[1,3]THIAZOLO[5,4-C]PYRIDIN-
HETNAM 3 B4V 2-YL)CARBAMOYL]PHENYL}METHYL)-1H-1,2,3-TRIAZOLE-4-
HETNAM 4 B4V CARBOXAMIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 B4V 4(C21 H22 N10 O3 S)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 11 HOH *162(H2 O)
HELIX 1 AA1 PHE A 7 ASP A 20 1 14
HELIX 2 AA2 ASN A 26 ASP A 42 1 17
HELIX 3 AA3 ALA A 45 LYS A 48 5 4
HELIX 4 AA4 ASN A 49 ARG A 70 1 22
HELIX 5 AA5 LYS A 72 GLU A 74 5 3
HELIX 6 AA6 LYS A 109 ARG A 115 1 7
HELIX 7 AA7 PHE A 120 ALA A 131 1 12
HELIX 8 AA8 LEU A 161 TYR A 168 1 8
HELIX 9 AA9 PRO A 171 MET A 192 1 22
HELIX 10 AB1 SER A 242 LYS A 247 1 6
HELIX 11 AB2 ARG A 257 GLY A 274 1 18
HELIX 12 AB3 SER A 282 ASN A 292 1 11
HELIX 13 AB4 ASN A 292 LEU A 297 1 6
HELIX 14 AB5 SER A 306 LEU A 317 1 12
HELIX 15 AB6 ASP A 319 ARG A 323 5 5
HELIX 16 AB7 VAL A 329 ARG A 334 1 6
HELIX 17 AB8 HIS A 335 LYS A 339 5 5
HELIX 18 AB9 THR A 347 THR A 351 5 5
HELIX 19 AC1 GLN A 391 VAL A 395 5 5
HELIX 20 AC2 GLU B 8 ASP B 20 1 13
HELIX 21 AC3 ASN B 26 ASP B 42 1 17
HELIX 22 AC4 ALA B 45 LYS B 48 5 4
HELIX 23 AC5 ASN B 49 ARG B 70 1 22
HELIX 24 AC6 LYS B 72 GLU B 74 5 3
HELIX 25 AC7 LYS B 109 ARG B 115 1 7
HELIX 26 AC8 PHE B 120 ALA B 131 1 12
HELIX 27 AC9 LEU B 161 TYR B 168 1 8
HELIX 28 AD1 PRO B 171 MET B 192 1 22
HELIX 29 AD2 LYS B 200 ASP B 202 5 3
HELIX 30 AD3 ARG B 257 GLY B 274 1 18
HELIX 31 AD4 SER B 282 ASN B 292 1 11
HELIX 32 AD5 ASN B 292 LEU B 297 1 6
HELIX 33 AD6 SER B 306 LEU B 317 1 12
HELIX 34 AD7 GLU B 330 ARG B 334 1 5
HELIX 35 AD8 HIS B 335 LYS B 339 5 5
HELIX 36 AD9 THR B 347 THR B 351 5 5
HELIX 37 AE1 GLN B 391 VAL B 395 5 5
HELIX 38 AE2 SER C 6 ASP C 20 1 15
HELIX 39 AE3 ASN C 26 ASP C 42 1 17
HELIX 40 AE4 ALA C 45 LYS C 48 5 4
HELIX 41 AE5 ASN C 49 ARG C 70 1 22
HELIX 42 AE6 LYS C 72 GLU C 74 5 3
HELIX 43 AE7 LYS C 109 ARG C 115 1 7
HELIX 44 AE8 PHE C 120 ALA C 131 1 12
HELIX 45 AE9 LEU C 161 TYR C 168 1 8
HELIX 46 AF1 PRO C 171 MET C 192 1 22
HELIX 47 AF2 LYS C 200 ASP C 202 5 3
HELIX 48 AF3 ARG C 257 GLY C 274 1 18
HELIX 49 AF4 SER C 282 ASN C 292 1 11
HELIX 50 AF5 ASN C 292 LEU C 297 1 6
HELIX 51 AF6 SER C 306 LEU C 317 1 12
HELIX 52 AF7 VAL C 329 ARG C 334 1 6
HELIX 53 AF8 HIS C 335 LYS C 339 5 5
HELIX 54 AF9 THR C 347 THR C 351 5 5
HELIX 55 AG1 GLN C 391 VAL C 395 5 5
HELIX 56 AG2 GLU D 8 ASP D 20 1 13
HELIX 57 AG3 ASN D 26 ASP D 42 1 17
HELIX 58 AG4 ALA D 45 LYS D 48 5 4
HELIX 59 AG5 ASN D 49 ARG D 70 1 22
HELIX 60 AG6 LYS D 72 GLU D 74 5 3
HELIX 61 AG7 LYS D 109 ARG D 115 1 7
HELIX 62 AG8 PHE D 121 ALA D 131 1 11
HELIX 63 AG9 LEU D 161 TYR D 168 1 8
HELIX 64 AH1 PRO D 171 MET D 192 1 22
HELIX 65 AH2 LYS D 200 ASP D 202 5 3
HELIX 66 AH3 SER D 242 GLN D 249 1 8
HELIX 67 AH4 ARG D 257 GLY D 274 1 18
HELIX 68 AH5 SER D 282 ASN D 292 1 11
HELIX 69 AH6 ASN D 292 LEU D 297 1 6
HELIX 70 AH7 SER D 306 LEU D 317 1 12
HELIX 71 AH8 VAL D 329 ARG D 334 1 6
HELIX 72 AH9 HIS D 335 LYS D 339 5 5
HELIX 73 AI1 THR D 347 THR D 351 5 5
HELIX 74 AI2 GLN D 391 VAL D 395 5 5
SHEET 1 AA1 5 TYR A 76 GLY A 85 0
SHEET 2 AA1 5 GLY A 88 HIS A 95 -1 O LEU A 92 N LYS A 80
SHEET 3 AA1 5 VAL A 101 SER A 108 -1 O MET A 104 N GLN A 91
SHEET 4 AA1 5 TYR A 148 MET A 153 -1 O MET A 153 N ALA A 103
SHEET 5 AA1 5 LEU A 139 GLN A 144 -1 N PHE A 143 O TYR A 150
SHEET 1 AA2 3 GLY A 159 ASP A 160 0
SHEET 2 AA2 3 MET A 204 LEU A 206 -1 O LEU A 206 N GLY A 159
SHEET 3 AA2 3 LEU A 212 LEU A 214 -1 O LYS A 213 N LEU A 205
SHEET 1 AA3 2 PHE A 194 ILE A 195 0
SHEET 2 AA3 2 MET A 221 LYS A 222 -1 O MET A 221 N ILE A 195
SHEET 1 AA4 2 MET A 228 ARG A 230 0
SHEET 2 AA4 2 TYR A 254 GLY A 256 -1 O TYR A 255 N VAL A 229
SHEET 1 AA5 6 TYR B 76 ARG B 84 0
SHEET 2 AA5 6 GLY B 88 HIS B 95 -1 O LEU B 92 N LYS B 80
SHEET 3 AA5 6 VAL B 101 SER B 108 -1 O MET B 104 N GLN B 91
SHEET 4 AA5 6 TYR B 148 MET B 153 -1 O MET B 153 N ALA B 103
SHEET 5 AA5 6 LEU B 139 GLN B 144 -1 N PHE B 143 O TYR B 150
SHEET 6 AA5 6 TYR B 399 TYR B 400 -1 O TYR B 399 N ALA B 142
SHEET 1 AA6 3 GLY B 159 ASP B 160 0
SHEET 2 AA6 3 MET B 204 LEU B 206 -1 O LEU B 206 N GLY B 159
SHEET 3 AA6 3 LEU B 212 LEU B 214 -1 O LYS B 213 N LEU B 205
SHEET 1 AA7 2 PHE B 194 ILE B 195 0
SHEET 2 AA7 2 MET B 221 LYS B 222 -1 O MET B 221 N ILE B 195
SHEET 1 AA8 6 TYR C 76 GLY C 85 0
SHEET 2 AA8 6 GLY C 88 HIS C 95 -1 O LEU C 92 N LYS C 80
SHEET 3 AA8 6 VAL C 101 SER C 108 -1 O MET C 104 N GLN C 91
SHEET 4 AA8 6 TYR C 148 MET C 153 -1 O MET C 153 N ALA C 103
SHEET 5 AA8 6 LEU C 139 GLN C 144 -1 N PHE C 143 O TYR C 150
SHEET 6 AA8 6 TYR C 399 TYR C 400 -1 O TYR C 399 N ALA C 142
SHEET 1 AA9 3 GLY C 159 ASP C 160 0
SHEET 2 AA9 3 MET C 204 LEU C 206 -1 O LEU C 206 N GLY C 159
SHEET 3 AA9 3 LEU C 212 LEU C 214 -1 O LYS C 213 N LEU C 205
SHEET 1 AB1 2 PHE C 194 ILE C 195 0
SHEET 2 AB1 2 MET C 221 LYS C 222 -1 O MET C 221 N ILE C 195
SHEET 1 AB2 2 VAL C 229 ARG C 230 0
SHEET 2 AB2 2 TYR C 254 TYR C 255 -1 O TYR C 255 N VAL C 229
SHEET 1 AB3 6 TYR D 76 ARG D 84 0
SHEET 2 AB3 6 GLY D 88 HIS D 95 -1 O LEU D 92 N LYS D 80
SHEET 3 AB3 6 VAL D 101 SER D 108 -1 O MET D 104 N GLN D 91
SHEET 4 AB3 6 TYR D 148 MET D 153 -1 O MET D 153 N ALA D 103
SHEET 5 AB3 6 LEU D 139 GLN D 144 -1 N PHE D 143 O TYR D 150
SHEET 6 AB3 6 TYR D 399 TYR D 400 -1 O TYR D 399 N ALA D 142
SHEET 1 AB4 3 GLY D 159 ASP D 160 0
SHEET 2 AB4 3 MET D 204 LEU D 206 -1 O LEU D 206 N GLY D 159
SHEET 3 AB4 3 LEU D 212 LEU D 214 -1 O LYS D 213 N LEU D 205
SHEET 1 AB5 2 PHE D 194 ILE D 195 0
SHEET 2 AB5 2 MET D 221 LYS D 222 -1 O MET D 221 N ILE D 195
SHEET 1 AB6 2 VAL D 229 ARG D 230 0
SHEET 2 AB6 2 TYR D 254 TYR D 255 -1 O TYR D 255 N VAL D 229
CISPEP 1 MET B 5 SER B 6 0 0.42
CISPEP 2 PHE B 7 GLU B 8 0 3.78
CISPEP 3 PRO B 238 ASP B 239 0 3.15
SITE 1 AC1 18 ILE A 82 GLY A 85 ALA A 86 PHE A 87
SITE 2 AC1 18 GLY A 88 GLU A 89 VAL A 90 ALA A 103
SITE 3 AC1 18 LEU A 107 ASP A 117 PHE A 120 VAL A 137
SITE 4 AC1 18 GLU A 154 TYR A 155 MET A 156 LEU A 205
SITE 5 AC1 18 GLY A 218 PHE A 368
SITE 1 AC2 5 ASP A 169 VAL A 170 MET A 271 LEU A 272
SITE 2 AC2 5 ASP A 304
SITE 1 AC3 5 ASN A 163 SER A 166 ASN A 167 ASP A 369
SITE 2 AC3 5 GLU C 12
SITE 1 AC4 17 GLY B 85 ALA B 86 PHE B 87 GLY B 88
SITE 2 AC4 17 GLU B 89 VAL B 90 ALA B 103 LEU B 107
SITE 3 AC4 17 ASP B 117 PHE B 120 VAL B 137 MET B 153
SITE 4 AC4 17 GLU B 154 TYR B 155 MET B 156 LEU B 205
SITE 5 AC4 17 GLY B 218
SITE 1 AC5 19 ILE C 82 GLY C 85 ALA C 86 PHE C 87
SITE 2 AC5 19 GLY C 88 VAL C 90 ALA C 103 LEU C 107
SITE 3 AC5 19 ASP C 117 PHE C 120 VAL C 137 MET C 153
SITE 4 AC5 19 GLU C 154 TYR C 155 MET C 156 LEU C 205
SITE 5 AC5 19 ASP C 216 PHE C 368 HOH C1009
SITE 1 AC6 18 ASP A 281 ILE D 82 GLY D 85 ALA D 86
SITE 2 AC6 18 PHE D 87 VAL D 90 ALA D 103 ASP D 117
SITE 3 AC6 18 PHE D 120 VAL D 137 GLU D 154 TYR D 155
SITE 4 AC6 18 MET D 156 LEU D 205 PHE D 368 HOH D1011
SITE 5 AC6 18 HOH D1021 HOH D1028
CRYST1 162.905 82.292 169.739 90.00 115.87 90.00 C 1 2 1 16
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 0.006139 0.000000 0.002977 0.00000
SCALE2 0.000000 0.012152 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006548 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
