HEADER TRANSFERASE/TRANSFERASE INHIBITOR 21-SEP-11 3TWJ
TITLE RHO-ASSOCIATED PROTEIN KINASE 1 (ROCK 1) IN COMPLEX WITH RKI1447
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL KINASE DOMAIN, RESIDUE 6-415;
COMPND 5 SYNONYM: RENAL CARCINOMA ANTIGEN NY-REN-35, RHO-ASSOCIATED, COILED-
COMPND 6 COIL-CONTAINING PROTEIN KINASE 1, RHO-ASSOCIATED, COILED-COIL-
COMPND 7 CONTAINING PROTEIN KINASE I, ROCK-I, P160 ROCK-1, P160ROCK;
COMPND 8 EC: 2.7.11.1;
COMPND 9 ENGINEERED: YES
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_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFB-DUAL-PBL
KEYWDS KINASE, DIMER, DIMERIZATION, MYOSIN, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.MARTIN,J.-Y.ZHU,E.SCHONBRUNN
REVDAT 3 13-SEP-23 3TWJ 1 REMARK
REVDAT 2 17-OCT-12 3TWJ 1 JRNL
REVDAT 1 22-AUG-12 3TWJ 0
JRNL AUTH R.A.PATEL,K.D.FORINASH,R.PIREDDU,Y.SUN,N.SUN,M.P.MARTIN,
JRNL AUTH 2 E.SCHONBRUNN,N.J.LAWRENCE,S.M.SEBTI
JRNL TITL RKI-1447 IS A POTENT INHIBITOR OF THE RHO-ASSOCIATED ROCK
JRNL TITL 2 KINASES WITH ANTI-INVASIVE AND ANTITUMOR ACTIVITIES IN
JRNL TITL 3 BREAST CANCER.
JRNL REF CANCER RES. V. 72 5025 2012
JRNL REFN ISSN 0008-5472
JRNL PMID 22846914
JRNL DOI 10.1158/0008-5472.CAN-12-0954
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 49896
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1048
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 19.7375 - 5.5128 0.99 7173 154 0.2094 0.2401
REMARK 3 2 5.5128 - 4.3915 1.00 7041 151 0.2043 0.2666
REMARK 3 3 4.3915 - 3.8410 1.00 6979 150 0.2118 0.2618
REMARK 3 4 3.8410 - 3.4919 1.00 6926 149 0.2300 0.3432
REMARK 3 5 3.4919 - 3.2428 1.00 6959 149 0.2453 0.3189
REMARK 3 6 3.2428 - 3.0524 0.99 6901 148 0.2546 0.3893
REMARK 3 7 3.0524 - 2.9000 0.99 6869 147 0.2624 0.3461
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 44.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.29
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.24230
REMARK 3 B22 (A**2) : -1.09250
REMARK 3 B33 (A**2) : 0.85020
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 13219
REMARK 3 ANGLE : 1.494 17856
REMARK 3 CHIRALITY : 0.099 1878
REMARK 3 PLANARITY : 0.006 2320
REMARK 3 DIHEDRAL : 20.156 4913
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TWJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49897
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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: MONOMER FROM CHAIN A OF 3TV7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML ROCK1, 75 MM HEPES PH 7.4,
REMARK 280 2.5 % TACSIMATE PH 7.4, 5 % PEG 5000 MME, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 102.54500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.54500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 72.83500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.46000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 72.83500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.46000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 102.54500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 72.83500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.46000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 102.54500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 72.83500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.46000
REMARK 290 SMTRY3 8 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: 3900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: 3430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 SER A 6
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 SER B 6
REMARK 465 PHE B 7
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 SER C 6
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 SER D 6
REMARK 465 PHE D 7
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 MET D 221
REMARK 475 LYS D 222
REMARK 475 MET D 223
REMARK 475 ASN D 224
REMARK 475 LYS D 225
REMARK 475 GLU D 226
REMARK 475 GLY D 227
REMARK 475 MET D 228
REMARK 475 VAL D 229
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 B 157 C - N - CA ANGL. DEV. = 11.2 DEGREES
REMARK 500 PRO C 238 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 GLY C 253 N - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 CYS D 220 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 PRO D 384 C - N - CA ANGL. DEV. = 9.3 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 60 -72.86 -45.44
REMARK 500 VAL A 79 -72.03 -108.52
REMARK 500 ALA A 86 -12.16 68.05
REMARK 500 SER A 116 -121.14 61.81
REMARK 500 ARG A 197 82.09 61.09
REMARK 500 ASP A 198 72.25 67.78
REMARK 500 ASP A 216 70.92 43.72
REMARK 500 ASN A 224 -72.27 -132.70
REMARK 500 LYS A 225 -65.45 -126.71
REMARK 500 THR A 237 72.82 59.85
REMARK 500 ASP A 252 -70.21 -54.41
REMARK 500 ASP A 302 -9.74 -59.35
REMARK 500 ASN A 340 158.36 177.32
REMARK 500 GLU A 372 -73.25 -121.77
REMARK 500 LYS A 385 -71.94 -71.57
REMARK 500 VAL A 388 -59.77 -121.30
REMARK 500 ARG B 10 -10.56 88.10
REMARK 500 ASP B 20 131.49 177.53
REMARK 500 PHE B 43 136.61 -175.64
REMARK 500 VAL B 79 -62.78 -96.37
REMARK 500 ARG B 115 -14.60 56.77
REMARK 500 ASP B 117 -124.40 47.81
REMARK 500 SER B 118 18.37 56.63
REMARK 500 ALA B 119 37.45 31.04
REMARK 500 ILE B 127 -71.84 -50.04
REMARK 500 ARG B 197 -14.54 80.45
REMARK 500 ASP B 207 -166.83 -74.53
REMARK 500 CYS B 220 -144.24 61.23
REMARK 500 MET B 221 -69.37 -131.02
REMARK 500 ASN B 224 -2.16 66.72
REMARK 500 CYS B 231 -136.77 43.38
REMARK 500 ASP B 232 -121.28 49.27
REMARK 500 THR B 233 -118.30 65.15
REMARK 500 ALA B 234 -76.05 -122.18
REMARK 500 ASP B 252 -74.60 -57.66
REMARK 500 PRO B 300 -168.26 -71.61
REMARK 500 ASP B 302 2.35 93.45
REMARK 500 ASP B 304 -75.60 -79.52
REMARK 500 ILE B 305 80.89 36.81
REMARK 500 GLN B 342 -73.24 -57.27
REMARK 500 THR B 347 -59.25 -125.01
REMARK 500 LEU B 348 -102.91 47.34
REMARK 500 LEU B 359 -72.94 -52.26
REMARK 500 SER B 360 -137.35 53.51
REMARK 500 LYS B 375 -140.22 60.98
REMARK 500 GLU B 377 71.99 51.74
REMARK 500 PHE B 381 77.77 40.05
REMARK 500 ALA C 45 -71.85 -48.79
REMARK 500 LYS C 60 -71.11 -45.02
REMARK 500 THR C 62 -71.39 -55.28
REMARK 500
REMARK 500 THIS ENTRY HAS 106 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 7 GLU A 8 146.69
REMARK 500 THR B 9 ARG B 10 137.03
REMARK 500 LYS B 114 ARG B 115 137.86
REMARK 500 ARG B 115 SER B 116 146.16
REMARK 500 SER B 118 ALA B 119 131.72
REMARK 500 TYR B 148 LEU B 149 149.97
REMARK 500 GLY B 218 THR B 219 -143.64
REMARK 500 CYS B 220 MET B 221 -149.45
REMARK 500 GLY B 227 MET B 228 -138.65
REMARK 500 GLY B 250 GLY B 251 -42.77
REMARK 500 ASP B 302 ASN B 303 140.82
REMARK 500 ILE B 363 ASP B 364 -147.06
REMARK 500 LYS B 375 GLY B 376 -135.25
REMARK 500 PHE C 217 GLY C 218 -138.49
REMARK 500 THR C 219 CYS C 220 -142.90
REMARK 500 GLY C 236 THR C 237 -134.06
REMARK 500 ASP C 252 GLY C 253 -139.35
REMARK 500 ASN C 303 ASP C 304 -138.45
REMARK 500 SER C 360 SER C 361 -134.43
REMARK 500 SER C 361 ASP C 362 142.75
REMARK 500 THR D 9 ARG D 10 146.92
REMARK 500 ARG D 19 ASP D 20 149.91
REMARK 500 PRO D 21 LYS D 22 142.01
REMARK 500 SER D 116 ASP D 117 -148.19
REMARK 500 CYS D 220 MET D 221 -34.08
REMARK 500 VAL D 229 ARG D 230 136.30
REMARK 500 ASP D 232 THR D 233 142.87
REMARK 500 THR D 233 ALA D 234 146.94
REMARK 500 ILE D 363 ASP D 364 -145.28
REMARK 500 ASP D 369 ASP D 370 -134.13
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 07R A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 07R C 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1
DBREF 3TWJ A 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 3TWJ B 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 3TWJ C 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 3TWJ D 6 415 UNP Q13464 ROCK1_HUMAN 6 415
SEQRES 1 A 410 SER PHE GLU THR ARG PHE GLU LYS MET ASP ASN LEU LEU
SEQRES 2 A 410 ARG ASP PRO LYS SER GLU VAL ASN SER ASP CYS LEU LEU
SEQRES 3 A 410 ASP GLY LEU ASP ALA LEU VAL TYR ASP LEU ASP PHE PRO
SEQRES 4 A 410 ALA LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU SER
SEQRES 5 A 410 ARG TYR LYS ASP THR ILE ASN LYS ILE ARG ASP LEU ARG
SEQRES 6 A 410 MET LYS ALA GLU ASP TYR GLU VAL VAL LYS VAL ILE GLY
SEQRES 7 A 410 ARG GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS
SEQRES 8 A 410 SER THR ARG LYS VAL TYR ALA MET LYS LEU LEU SER LYS
SEQRES 9 A 410 PHE GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP
SEQRES 10 A 410 GLU GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP
SEQRES 11 A 410 VAL VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR
SEQRES 12 A 410 LEU TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU
SEQRES 13 A 410 VAL ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP
SEQRES 14 A 410 ALA ARG PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP
SEQRES 15 A 410 ALA ILE HIS SER MET GLY PHE ILE HIS ARG ASP VAL LYS
SEQRES 16 A 410 PRO ASP ASN MET LEU LEU ASP LYS SER GLY HIS LEU LYS
SEQRES 17 A 410 LEU ALA ASP PHE GLY THR CYS MET LYS MET ASN LYS GLU
SEQRES 18 A 410 GLY MET VAL ARG CYS ASP THR ALA VAL GLY THR PRO ASP
SEQRES 19 A 410 TYR ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP
SEQRES 20 A 410 GLY TYR TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY
SEQRES 21 A 410 VAL PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE
SEQRES 22 A 410 TYR ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET
SEQRES 23 A 410 ASN HIS LYS ASN SER LEU THR PHE PRO ASP ASP ASN ASP
SEQRES 24 A 410 ILE SER LYS GLU ALA LYS ASN LEU ILE CYS ALA PHE LEU
SEQRES 25 A 410 THR ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU
SEQRES 26 A 410 GLU ILE LYS ARG HIS LEU PHE PHE LYS ASN ASP GLN TRP
SEQRES 27 A 410 ALA TRP GLU THR LEU ARG ASP THR VAL ALA PRO VAL VAL
SEQRES 28 A 410 PRO ASP LEU SER SER ASP ILE ASP THR SER ASN PHE ASP
SEQRES 29 A 410 ASP LEU GLU GLU ASP LYS GLY GLU GLU GLU THR PHE PRO
SEQRES 30 A 410 ILE PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE VAL
SEQRES 31 A 410 GLY PHE THR TYR TYR SER ASN ARG ARG TYR LEU SER SER
SEQRES 32 A 410 ALA ASN PRO ASN ASP ASN ARG
SEQRES 1 B 410 SER PHE GLU THR ARG PHE GLU LYS MET ASP ASN LEU LEU
SEQRES 2 B 410 ARG ASP PRO LYS SER GLU VAL ASN SER ASP CYS LEU LEU
SEQRES 3 B 410 ASP GLY LEU ASP ALA LEU VAL TYR ASP LEU ASP PHE PRO
SEQRES 4 B 410 ALA LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU SER
SEQRES 5 B 410 ARG TYR LYS ASP THR ILE ASN LYS ILE ARG ASP LEU ARG
SEQRES 6 B 410 MET LYS ALA GLU ASP TYR GLU VAL VAL LYS VAL ILE GLY
SEQRES 7 B 410 ARG GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS
SEQRES 8 B 410 SER THR ARG LYS VAL TYR ALA MET LYS LEU LEU SER LYS
SEQRES 9 B 410 PHE GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP
SEQRES 10 B 410 GLU GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP
SEQRES 11 B 410 VAL VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR
SEQRES 12 B 410 LEU TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU
SEQRES 13 B 410 VAL ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP
SEQRES 14 B 410 ALA ARG PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP
SEQRES 15 B 410 ALA ILE HIS SER MET GLY PHE ILE HIS ARG ASP VAL LYS
SEQRES 16 B 410 PRO ASP ASN MET LEU LEU ASP LYS SER GLY HIS LEU LYS
SEQRES 17 B 410 LEU ALA ASP PHE GLY THR CYS MET LYS MET ASN LYS GLU
SEQRES 18 B 410 GLY MET VAL ARG CYS ASP THR ALA VAL GLY THR PRO ASP
SEQRES 19 B 410 TYR ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP
SEQRES 20 B 410 GLY TYR TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY
SEQRES 21 B 410 VAL PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE
SEQRES 22 B 410 TYR ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET
SEQRES 23 B 410 ASN HIS LYS ASN SER LEU THR PHE PRO ASP ASP ASN ASP
SEQRES 24 B 410 ILE SER LYS GLU ALA LYS ASN LEU ILE CYS ALA PHE LEU
SEQRES 25 B 410 THR ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU
SEQRES 26 B 410 GLU ILE LYS ARG HIS LEU PHE PHE LYS ASN ASP GLN TRP
SEQRES 27 B 410 ALA TRP GLU THR LEU ARG ASP THR VAL ALA PRO VAL VAL
SEQRES 28 B 410 PRO ASP LEU SER SER ASP ILE ASP THR SER ASN PHE ASP
SEQRES 29 B 410 ASP LEU GLU GLU ASP LYS GLY GLU GLU GLU THR PHE PRO
SEQRES 30 B 410 ILE PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE VAL
SEQRES 31 B 410 GLY PHE THR TYR TYR SER ASN ARG ARG TYR LEU SER SER
SEQRES 32 B 410 ALA ASN PRO ASN ASP ASN ARG
SEQRES 1 C 410 SER PHE GLU THR ARG PHE GLU LYS MET ASP ASN LEU LEU
SEQRES 2 C 410 ARG ASP PRO LYS SER GLU VAL ASN SER ASP CYS LEU LEU
SEQRES 3 C 410 ASP GLY LEU ASP ALA LEU VAL TYR ASP LEU ASP PHE PRO
SEQRES 4 C 410 ALA LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU SER
SEQRES 5 C 410 ARG TYR LYS ASP THR ILE ASN LYS ILE ARG ASP LEU ARG
SEQRES 6 C 410 MET LYS ALA GLU ASP TYR GLU VAL VAL LYS VAL ILE GLY
SEQRES 7 C 410 ARG GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS
SEQRES 8 C 410 SER THR ARG LYS VAL TYR ALA MET LYS LEU LEU SER LYS
SEQRES 9 C 410 PHE GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP
SEQRES 10 C 410 GLU GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP
SEQRES 11 C 410 VAL VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR
SEQRES 12 C 410 LEU TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU
SEQRES 13 C 410 VAL ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP
SEQRES 14 C 410 ALA ARG PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP
SEQRES 15 C 410 ALA ILE HIS SER MET GLY PHE ILE HIS ARG ASP VAL LYS
SEQRES 16 C 410 PRO ASP ASN MET LEU LEU ASP LYS SER GLY HIS LEU LYS
SEQRES 17 C 410 LEU ALA ASP PHE GLY THR CYS MET LYS MET ASN LYS GLU
SEQRES 18 C 410 GLY MET VAL ARG CYS ASP THR ALA VAL GLY THR PRO ASP
SEQRES 19 C 410 TYR ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP
SEQRES 20 C 410 GLY TYR TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY
SEQRES 21 C 410 VAL PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE
SEQRES 22 C 410 TYR ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET
SEQRES 23 C 410 ASN HIS LYS ASN SER LEU THR PHE PRO ASP ASP ASN ASP
SEQRES 24 C 410 ILE SER LYS GLU ALA LYS ASN LEU ILE CYS ALA PHE LEU
SEQRES 25 C 410 THR ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU
SEQRES 26 C 410 GLU ILE LYS ARG HIS LEU PHE PHE LYS ASN ASP GLN TRP
SEQRES 27 C 410 ALA TRP GLU THR LEU ARG ASP THR VAL ALA PRO VAL VAL
SEQRES 28 C 410 PRO ASP LEU SER SER ASP ILE ASP THR SER ASN PHE ASP
SEQRES 29 C 410 ASP LEU GLU GLU ASP LYS GLY GLU GLU GLU THR PHE PRO
SEQRES 30 C 410 ILE PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE VAL
SEQRES 31 C 410 GLY PHE THR TYR TYR SER ASN ARG ARG TYR LEU SER SER
SEQRES 32 C 410 ALA ASN PRO ASN ASP ASN ARG
SEQRES 1 D 410 SER PHE GLU THR ARG PHE GLU LYS MET ASP ASN LEU LEU
SEQRES 2 D 410 ARG ASP PRO LYS SER GLU VAL ASN SER ASP CYS LEU LEU
SEQRES 3 D 410 ASP GLY LEU ASP ALA LEU VAL TYR ASP LEU ASP PHE PRO
SEQRES 4 D 410 ALA LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU SER
SEQRES 5 D 410 ARG TYR LYS ASP THR ILE ASN LYS ILE ARG ASP LEU ARG
SEQRES 6 D 410 MET LYS ALA GLU ASP TYR GLU VAL VAL LYS VAL ILE GLY
SEQRES 7 D 410 ARG GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS
SEQRES 8 D 410 SER THR ARG LYS VAL TYR ALA MET LYS LEU LEU SER LYS
SEQRES 9 D 410 PHE GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP
SEQRES 10 D 410 GLU GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP
SEQRES 11 D 410 VAL VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR
SEQRES 12 D 410 LEU TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU
SEQRES 13 D 410 VAL ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP
SEQRES 14 D 410 ALA ARG PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP
SEQRES 15 D 410 ALA ILE HIS SER MET GLY PHE ILE HIS ARG ASP VAL LYS
SEQRES 16 D 410 PRO ASP ASN MET LEU LEU ASP LYS SER GLY HIS LEU LYS
SEQRES 17 D 410 LEU ALA ASP PHE GLY THR CYS MET LYS MET ASN LYS GLU
SEQRES 18 D 410 GLY MET VAL ARG CYS ASP THR ALA VAL GLY THR PRO ASP
SEQRES 19 D 410 TYR ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP
SEQRES 20 D 410 GLY TYR TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY
SEQRES 21 D 410 VAL PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE
SEQRES 22 D 410 TYR ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET
SEQRES 23 D 410 ASN HIS LYS ASN SER LEU THR PHE PRO ASP ASP ASN ASP
SEQRES 24 D 410 ILE SER LYS GLU ALA LYS ASN LEU ILE CYS ALA PHE LEU
SEQRES 25 D 410 THR ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU
SEQRES 26 D 410 GLU ILE LYS ARG HIS LEU PHE PHE LYS ASN ASP GLN TRP
SEQRES 27 D 410 ALA TRP GLU THR LEU ARG ASP THR VAL ALA PRO VAL VAL
SEQRES 28 D 410 PRO ASP LEU SER SER ASP ILE ASP THR SER ASN PHE ASP
SEQRES 29 D 410 ASP LEU GLU GLU ASP LYS GLY GLU GLU GLU THR PHE PRO
SEQRES 30 D 410 ILE PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE VAL
SEQRES 31 D 410 GLY PHE THR TYR TYR SER ASN ARG ARG TYR LEU SER SER
SEQRES 32 D 410 ALA ASN PRO ASN ASP ASN ARG
HET 07R A 1 23
HET EDO A 3 4
HET EDO B 2 4
HET 07R C 2 23
HET EDO D 1 4
HETNAM 07R 1-[(3-HYDROXYPHENYL)METHYL]-3-(4-PYRIDIN-4-YL-1,3-
HETNAM 2 07R THIAZOL-2-YL)UREA
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 07R 2(C16 H14 N4 O2 S)
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 10 HOH *40(H2 O)
HELIX 1 1 THR A 9 LEU A 18 1 10
HELIX 2 2 ASN A 26 ASP A 42 1 17
HELIX 3 3 ALA A 45 LYS A 48 5 4
HELIX 4 4 ASN A 49 ARG A 70 1 22
HELIX 5 5 LYS A 72 GLU A 74 5 3
HELIX 6 6 SER A 108 SER A 116 1 9
HELIX 7 7 PHE A 120 ALA A 131 1 12
HELIX 8 8 ASP A 160 TYR A 168 1 9
HELIX 9 9 PRO A 171 SER A 191 1 21
HELIX 10 10 LYS A 200 ASP A 202 5 3
HELIX 11 11 SER A 242 SER A 248 1 7
HELIX 12 12 ARG A 257 GLY A 274 1 18
HELIX 13 13 SER A 282 ASN A 292 1 11
HELIX 14 14 ASN A 292 LEU A 297 1 6
HELIX 15 15 SER A 306 LEU A 317 1 12
HELIX 16 16 ASP A 319 ARG A 323 5 5
HELIX 17 17 VAL A 329 ARG A 334 1 6
HELIX 18 18 HIS A 335 LYS A 339 5 5
HELIX 19 19 ALA A 344 LEU A 348 5 5
HELIX 20 20 GLN A 391 VAL A 395 5 5
HELIX 21 21 ARG B 10 ARG B 19 1 10
HELIX 22 22 ASN B 26 ASP B 42 1 17
HELIX 23 23 ALA B 45 LYS B 48 5 4
HELIX 24 24 ASN B 49 TYR B 59 1 11
HELIX 25 25 TYR B 59 ARG B 70 1 12
HELIX 26 26 LYS B 72 GLU B 74 5 3
HELIX 27 27 LYS B 109 LYS B 114 1 6
HELIX 28 28 PHE B 120 ALA B 131 1 12
HELIX 29 29 ASP B 160 TYR B 168 1 9
HELIX 30 30 PRO B 171 SER B 191 1 21
HELIX 31 31 LYS B 200 ASP B 202 5 3
HELIX 32 32 SER B 242 GLN B 249 1 8
HELIX 33 33 ARG B 257 GLY B 274 1 18
HELIX 34 34 SER B 282 ASN B 292 1 11
HELIX 35 35 ASN B 292 LEU B 297 1 6
HELIX 36 36 SER B 306 LEU B 317 1 12
HELIX 37 37 GLY B 328 ARG B 334 1 7
HELIX 38 38 HIS B 335 LYS B 339 5 5
HELIX 39 39 THR B 347 THR B 351 5 5
HELIX 40 40 GLN B 391 VAL B 395 5 5
HELIX 41 41 THR C 9 ASP C 20 1 12
HELIX 42 42 ASN C 26 ASP C 42 1 17
HELIX 43 43 ALA C 45 LYS C 48 5 4
HELIX 44 44 ASN C 49 LEU C 69 1 21
HELIX 45 45 LYS C 72 GLU C 74 5 3
HELIX 46 46 LYS C 109 SER C 116 1 8
HELIX 47 47 PHE C 120 ALA C 131 1 12
HELIX 48 48 LEU C 161 SER C 166 1 6
HELIX 49 49 PRO C 171 SER C 191 1 21
HELIX 50 50 THR C 237 ILE C 241 5 5
HELIX 51 51 SER C 242 LYS C 247 1 6
HELIX 52 52 ARG C 257 GLY C 274 1 18
HELIX 53 53 SER C 282 ASN C 292 1 11
HELIX 54 54 ASN C 292 LEU C 297 1 6
HELIX 55 55 SER C 306 LEU C 317 1 12
HELIX 56 56 VAL C 329 ARG C 334 1 6
HELIX 57 57 HIS C 335 LYS C 339 5 5
HELIX 58 58 GLN C 391 VAL C 395 5 5
HELIX 59 59 PHE D 11 ARG D 19 1 9
HELIX 60 60 ASN D 26 ASP D 42 1 17
HELIX 61 61 ASN D 49 ARG D 70 1 22
HELIX 62 62 LYS D 72 GLU D 74 5 3
HELIX 63 63 ALA D 119 ALA D 131 1 13
HELIX 64 64 LEU D 161 TYR D 168 1 8
HELIX 65 65 PRO D 171 SER D 191 1 21
HELIX 66 66 LYS D 200 ASP D 202 5 3
HELIX 67 67 THR D 237 ILE D 241 5 5
HELIX 68 68 SER D 242 SER D 248 1 7
HELIX 69 69 GLU D 258 GLY D 274 1 17
HELIX 70 70 SER D 282 ASN D 292 1 11
HELIX 71 71 ASN D 292 LEU D 297 1 6
HELIX 72 72 SER D 306 LEU D 317 1 12
HELIX 73 73 VAL D 329 ARG D 334 1 6
HELIX 74 74 HIS D 335 LYS D 339 5 5
HELIX 75 75 THR D 347 THR D 351 5 5
HELIX 76 76 GLN D 391 VAL D 395 5 5
SHEET 1 A 5 TYR A 76 ARG A 84 0
SHEET 2 A 5 GLU A 89 HIS A 95 -1 O LEU A 92 N VAL A 79
SHEET 3 A 5 VAL A 101 LYS A 105 -1 O MET A 104 N GLN A 91
SHEET 4 A 5 LEU A 149 GLU A 154 -1 O MET A 153 N ALA A 103
SHEET 5 A 5 LEU A 139 GLN A 144 -1 N PHE A 140 O VAL A 152
SHEET 1 B 2 PHE A 194 ILE A 195 0
SHEET 2 B 2 MET A 221 LYS A 222 -1 O MET A 221 N ILE A 195
SHEET 1 C 2 MET A 204 LEU A 206 0
SHEET 2 C 2 LEU A 212 LEU A 214 -1 O LYS A 213 N LEU A 205
SHEET 1 D 5 TYR B 76 ARG B 84 0
SHEET 2 D 5 GLY B 88 HIS B 95 -1 O ARG B 94 N GLU B 77
SHEET 3 D 5 VAL B 101 SER B 108 -1 O LEU B 106 N GLU B 89
SHEET 4 D 5 TYR B 148 MET B 153 -1 O MET B 153 N ALA B 103
SHEET 5 D 5 LEU B 139 GLN B 144 -1 N TYR B 141 O VAL B 152
SHEET 1 E 2 MET B 204 LEU B 206 0
SHEET 2 E 2 LEU B 212 LEU B 214 -1 O LYS B 213 N LEU B 205
SHEET 1 F 6 TYR C 76 ARG C 84 0
SHEET 2 F 6 GLU C 89 HIS C 95 -1 O LEU C 92 N VAL C 79
SHEET 3 F 6 LYS C 100 SER C 108 -1 O MET C 104 N GLN C 91
SHEET 4 F 6 TYR C 148 MET C 153 -1 O MET C 151 N LYS C 105
SHEET 5 F 6 LEU C 139 GLN C 144 -1 N TYR C 141 O VAL C 152
SHEET 6 F 6 TYR C 399 TYR C 400 -1 O TYR C 399 N ALA C 142
SHEET 1 G 2 PHE C 194 ILE C 195 0
SHEET 2 G 2 MET C 221 LYS C 222 -1 O MET C 221 N ILE C 195
SHEET 1 H 2 MET C 204 LEU C 206 0
SHEET 2 H 2 LEU C 212 LEU C 214 -1 O LYS C 213 N LEU C 205
SHEET 1 I 2 VAL C 229 ARG C 230 0
SHEET 2 I 2 TYR C 254 TYR C 255 -1 O TYR C 255 N VAL C 229
SHEET 1 J 6 TYR D 76 ARG D 84 0
SHEET 2 J 6 GLY D 88 HIS D 95 -1 O ARG D 94 N GLU D 77
SHEET 3 J 6 VAL D 101 SER D 108 -1 O MET D 104 N GLN D 91
SHEET 4 J 6 TYR D 148 MET D 153 -1 O MET D 153 N ALA D 103
SHEET 5 J 6 LEU D 139 GLN D 144 -1 N PHE D 140 O VAL D 152
SHEET 6 J 6 TYR D 399 TYR D 400 -1 O TYR D 399 N ALA D 142
SHEET 1 K 3 GLY D 159 ASP D 160 0
SHEET 2 K 3 MET D 204 LEU D 206 -1 O LEU D 206 N GLY D 159
SHEET 3 K 3 LEU D 212 LEU D 214 -1 O LYS D 213 N LEU D 205
CISPEP 1 GLN B 249 GLY B 250 0 16.32
CISPEP 2 ASP B 301 ASP B 302 0 19.14
CISPEP 3 ASN B 303 ASP B 304 0 7.94
SITE 1 AC1 15 GLY A 85 PHE A 87 GLY A 88 GLU A 89
SITE 2 AC1 15 VAL A 90 ALA A 103 LYS A 105 MET A 128
SITE 3 AC1 15 MET A 153 GLU A 154 TYR A 155 MET A 156
SITE 4 AC1 15 LEU A 205 ALA A 215 ASP A 216
SITE 1 AC2 4 ASP A 169 VAL A 170 MET A 271 LEU A 272
SITE 1 AC3 4 HIS B 95 THR B 98 TYR B 102 TYR B 141
SITE 1 AC4 11 GLY C 85 PHE C 87 GLY C 88 VAL C 90
SITE 2 AC4 11 ALA C 103 LYS C 105 MET C 153 GLU C 154
SITE 3 AC4 11 MET C 156 ASP C 216 PHE C 368
SITE 1 AC5 3 HIS D 95 THR D 98 TYR D 141
CRYST1 145.670 150.920 205.090 90.00 90.00 90.00 C 2 2 21 32
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 0.006865 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004876 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
