HEADER TRANSFERASE/TRANSFERASE INHIBITOR 23-DEC-11 3V8S
TITLE HUMAN RHO-ASSOCIATED PROTEIN KINASE 1 (ROCK 1) IN COMPLEX WITH
TITLE 2 INDAZOLE DERIVATIVE (COMPOUND 18)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: 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, DIMERIZATION, MYOSIN, TRANSFERASE, INHIBITOR, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.MARTIN,J.-YI.ZHU,E.SCHONBRUNN
REVDAT 3 13-SEP-23 3V8S 1 REMARK
REVDAT 2 21-MAR-12 3V8S 1 JRNL REMARK
REVDAT 1 08-FEB-12 3V8S 0
JRNL AUTH R.LI,M.P.MARTIN,Y.LIU,B.WANG,R.A.PATEL,J.Y.ZHU,N.SUN,
JRNL AUTH 2 R.PIREDDU,N.J.LAWRENCE,J.LI,E.B.HAURA,S.S.SUNG,W.C.GUIDA,
JRNL AUTH 3 E.SCHONBRUNN,S.M.SEBTI
JRNL TITL FRAGMENT-BASED AND STRUCTURE-GUIDED DISCOVERY AND
JRNL TITL 2 OPTIMIZATION OF RHO KINASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 55 2474 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22272748
JRNL DOI 10.1021/JM201289R
REMARK 2
REMARK 2 RESOLUTION. 2.29 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 94051
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1938
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 19.8519 - 5.4736 1.00 7004 151 0.1900 0.1916
REMARK 3 2 5.4736 - 4.3597 1.00 6880 146 0.1608 0.1826
REMARK 3 3 4.3597 - 3.8130 1.00 6813 141 0.1509 0.2326
REMARK 3 4 3.8130 - 3.4664 1.00 6758 142 0.1750 0.2091
REMARK 3 5 3.4664 - 3.2191 1.00 6809 139 0.1957 0.2859
REMARK 3 6 3.2191 - 3.0300 0.99 6733 137 0.2035 0.2554
REMARK 3 7 3.0300 - 2.8787 0.99 6672 137 0.2057 0.2382
REMARK 3 8 2.8787 - 2.7537 0.98 6599 139 0.2078 0.2789
REMARK 3 9 2.7537 - 2.6480 0.97 6580 133 0.2093 0.2944
REMARK 3 10 2.6480 - 2.5568 0.96 6394 135 0.2095 0.2722
REMARK 3 11 2.5568 - 2.4770 0.96 6497 139 0.2054 0.2594
REMARK 3 12 2.4770 - 2.4063 0.95 6378 141 0.2131 0.3047
REMARK 3 13 2.4063 - 2.3431 0.95 6353 136 0.2076 0.3135
REMARK 3 14 2.3431 - 2.2860 0.85 5643 122 0.2145 0.2187
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 48.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.63370
REMARK 3 B22 (A**2) : 5.59180
REMARK 3 B33 (A**2) : -9.22550
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 : 0.008 13276
REMARK 3 ANGLE : 1.255 17932
REMARK 3 CHIRALITY : 0.098 1880
REMARK 3 PLANARITY : 0.006 2326
REMARK 3 DIHEDRAL : 15.106 4926
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 3V8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069738.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-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) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
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 : MD2 MICRO DIFFRACTOMETER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96308
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.286
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
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: 3TV7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML ROCK1, 25 MM HEPES PH 7.4, 50
REMARK 280 MM MES PH 6.5, 2.5% TACSIMATE PH 7.0, 5% PEG 5000 MME, VAPOR
REMARK 280 DIFFUSION, HANGING 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 93.07000
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 93.07000
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 75.86000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.05500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 75.86000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.05500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.07000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 75.86000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.05500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.07000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 75.86000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.05500
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: 3670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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: 3700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 702 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 824 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 820 LIES ON A SPECIAL POSITION.
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 PHE A 7
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 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 PHE C 7
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 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: 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 238 C - N - CA ANGL. DEV. = 12.6 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 ALA A 86 -16.99 68.31
REMARK 500 ARG A 99 -1.44 74.71
REMARK 500 SER A 116 -142.62 55.25
REMARK 500 ARG A 197 -10.47 76.27
REMARK 500 ASP A 216 71.60 60.60
REMARK 500 ASP A 252 1.14 80.88
REMARK 500 ASP A 374 -114.96 55.92
REMARK 500 LYS A 375 -10.28 87.03
REMARK 500 GLU A 379 159.61 175.35
REMARK 500 THR A 380 177.42 173.30
REMARK 500 PHE A 381 139.98 81.62
REMARK 500 ALA B 86 -21.93 76.53
REMARK 500 ARG B 99 -2.45 70.85
REMARK 500 ASP B 145 -169.55 -126.76
REMARK 500 ARG B 197 -22.55 79.11
REMARK 500 ASP B 216 76.73 58.53
REMARK 500 ASN B 224 -169.45 -79.32
REMARK 500 ASP B 232 -73.13 -83.07
REMARK 500 ASP B 302 -71.42 -44.71
REMARK 500 GLU B 372 -73.18 -74.57
REMARK 500 GLU B 373 161.03 172.72
REMARK 500 LYS B 375 -7.90 62.74
REMARK 500 ALA C 86 -16.59 69.36
REMARK 500 ARG C 99 -1.07 74.58
REMARK 500 SER C 116 -90.79 80.18
REMARK 500 ASP C 117 97.16 -19.87
REMARK 500 ARG C 197 -10.72 74.86
REMARK 500 ASP C 216 70.46 61.35
REMARK 500 ASP C 252 -71.28 -50.25
REMARK 500 ASP C 374 -113.46 50.62
REMARK 500 LYS C 375 -7.49 88.03
REMARK 500 ARG D 99 -2.75 75.99
REMARK 500 ARG D 197 -23.23 77.83
REMARK 500 ASP D 216 76.40 58.27
REMARK 500 ASN D 303 170.98 175.05
REMARK 500 GLU D 372 -73.68 -74.57
REMARK 500 GLU D 373 160.36 174.76
REMARK 500 LYS D 375 -7.40 63.76
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 ASN D 303 ASP D 304 146.27
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 0HD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0HD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0HD C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0HD D 501
DBREF 3V8S A 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 3V8S B 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 3V8S C 6 415 UNP Q13464 ROCK1_HUMAN 6 415
DBREF 3V8S 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 0HD A 501 21
HET 0HD B 501 21
HET 0HD C 501 21
HET 0HD D 501 21
HETNAM 0HD 1-(1H-INDAZOL-5-YL)-3-(2-PHENYLETHYL)UREA
FORMUL 5 0HD 4(C16 H16 N4 O)
FORMUL 9 HOH *872(H2 O)
HELIX 1 1 GLU A 8 ASP A 20 1 13
HELIX 2 2 ASN A 26 ASP A 42 1 17
HELIX 3 3 PHE A 43 LYS A 48 1 6
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 LYS A 109 ARG A 115 1 7
HELIX 7 7 PHE A 120 ALA A 131 1 12
HELIX 8 8 LEU A 161 TYR A 168 1 8
HELIX 9 9 PRO A 171 MET A 192 1 22
HELIX 10 10 LYS A 200 ASP A 202 5 3
HELIX 11 11 THR A 237 ILE A 241 5 5
HELIX 12 12 SER A 242 SER A 248 1 7
HELIX 13 13 ARG A 257 GLY A 274 1 18
HELIX 14 14 SER A 282 ASN A 292 1 11
HELIX 15 15 ASN A 292 LEU A 297 1 6
HELIX 16 16 SER A 306 LEU A 317 1 12
HELIX 17 17 ASP A 319 ARG A 323 5 5
HELIX 18 18 GLY A 328 ARG A 334 1 7
HELIX 19 19 HIS A 335 LYS A 339 5 5
HELIX 20 20 THR A 347 THR A 351 5 5
HELIX 21 21 GLN A 391 VAL A 395 5 5
HELIX 22 22 THR B 9 ASP B 20 1 12
HELIX 23 23 ASN B 26 ASP B 42 1 17
HELIX 24 24 ALA B 45 LYS B 48 5 4
HELIX 25 25 ASN B 49 ARG B 70 1 22
HELIX 26 26 LYS B 72 GLU B 74 5 3
HELIX 27 27 LYS B 109 ARG B 115 1 7
HELIX 28 28 PHE B 121 ALA B 131 1 11
HELIX 29 29 LEU B 161 TYR B 168 1 8
HELIX 30 30 PRO B 171 MET B 192 1 22
HELIX 31 31 LYS B 200 ASP B 202 5 3
HELIX 32 32 SER B 242 GLY B 250 1 9
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 ASP B 319 ARG B 323 5 5
HELIX 38 38 VAL B 329 ARG B 334 1 6
HELIX 39 39 HIS B 335 LYS B 339 5 5
HELIX 40 40 THR B 347 THR B 351 5 5
HELIX 41 41 GLN B 391 VAL B 395 5 5
HELIX 42 42 THR C 9 ASP C 20 1 12
HELIX 43 43 ASN C 26 ASP C 42 1 17
HELIX 44 44 ALA C 45 LYS C 48 5 4
HELIX 45 45 ASN C 49 ARG C 70 1 22
HELIX 46 46 LYS C 72 GLU C 74 5 3
HELIX 47 47 LYS C 109 ARG C 115 1 7
HELIX 48 48 PHE C 120 ALA C 131 1 12
HELIX 49 49 LEU C 161 TYR C 168 1 8
HELIX 50 50 PRO C 171 MET C 192 1 22
HELIX 51 51 LYS C 200 ASP C 202 5 3
HELIX 52 52 SER C 242 GLN C 249 1 8
HELIX 53 53 ARG C 257 GLY C 274 1 18
HELIX 54 54 SER C 282 ASN C 292 1 11
HELIX 55 55 ASN C 292 LEU C 297 1 6
HELIX 56 56 SER C 306 LEU C 317 1 12
HELIX 57 57 ASP C 319 ARG C 323 5 5
HELIX 58 58 VAL C 329 ARG C 334 1 6
HELIX 59 59 HIS C 335 LYS C 339 5 5
HELIX 60 60 THR C 347 THR C 351 5 5
HELIX 61 61 GLN C 391 VAL C 395 5 5
HELIX 62 62 THR D 9 ASP D 20 1 12
HELIX 63 63 ASN D 26 ASP D 42 1 17
HELIX 64 64 ALA D 45 LYS D 48 5 4
HELIX 65 65 ASN D 49 ARG D 70 1 22
HELIX 66 66 LYS D 72 GLU D 74 5 3
HELIX 67 67 LYS D 109 ARG D 115 1 7
HELIX 68 68 PHE D 121 ALA D 131 1 11
HELIX 69 69 LEU D 161 TYR D 168 1 8
HELIX 70 70 PRO D 171 MET D 192 1 22
HELIX 71 71 LYS D 200 ASP D 202 5 3
HELIX 72 72 SER D 242 GLN D 249 1 8
HELIX 73 73 ARG D 257 GLY D 274 1 18
HELIX 74 74 SER D 282 ASN D 292 1 11
HELIX 75 75 ASN D 292 LEU D 297 1 6
HELIX 76 76 SER D 306 LEU D 317 1 12
HELIX 77 77 ASP D 319 ARG D 323 5 5
HELIX 78 78 VAL D 329 ARG D 334 1 6
HELIX 79 79 HIS D 335 LYS D 339 5 5
HELIX 80 80 THR D 347 THR D 351 5 5
HELIX 81 81 GLN D 391 VAL D 395 5 5
SHEET 1 A 6 TYR A 76 ARG A 84 0
SHEET 2 A 6 GLY A 88 HIS A 95 -1 O ARG A 94 N GLU A 77
SHEET 3 A 6 VAL A 101 SER A 108 -1 O MET A 104 N GLN A 91
SHEET 4 A 6 TYR A 148 MET A 153 -1 O MET A 153 N ALA A 103
SHEET 5 A 6 LEU A 139 GLN A 144 -1 N PHE A 140 O VAL A 152
SHEET 6 A 6 TYR A 399 TYR A 400 -1 O TYR A 399 N ALA A 142
SHEET 1 B 3 GLY A 159 ASP A 160 0
SHEET 2 B 3 MET A 204 LEU A 206 -1 O LEU A 206 N GLY A 159
SHEET 3 B 3 LEU A 212 LEU A 214 -1 O LYS A 213 N LEU A 205
SHEET 1 C 2 PHE A 194 ILE A 195 0
SHEET 2 C 2 MET A 221 LYS A 222 -1 O MET A 221 N ILE A 195
SHEET 1 D 2 MET A 228 ARG A 230 0
SHEET 2 D 2 TYR A 254 GLY A 256 -1 O TYR A 255 N VAL A 229
SHEET 1 E 6 TYR B 76 ARG B 84 0
SHEET 2 E 6 GLU B 89 HIS B 95 -1 O LEU B 92 N VAL B 79
SHEET 3 E 6 VAL B 101 SER B 108 -1 O LEU B 106 N GLU B 89
SHEET 4 E 6 TYR B 148 GLU B 154 -1 O MET B 153 N ALA B 103
SHEET 5 E 6 LEU B 139 GLN B 144 -1 N TYR B 141 O VAL B 152
SHEET 6 E 6 TYR B 399 TYR B 400 -1 O TYR B 399 N ALA B 142
SHEET 1 F 3 GLY B 159 ASP B 160 0
SHEET 2 F 3 MET B 204 LEU B 206 -1 O LEU B 206 N GLY B 159
SHEET 3 F 3 LEU B 212 LEU B 214 -1 O LYS B 213 N LEU B 205
SHEET 1 G 2 PHE B 194 ILE B 195 0
SHEET 2 G 2 MET B 221 LYS B 222 -1 O MET B 221 N ILE B 195
SHEET 1 H 2 MET B 228 VAL B 229 0
SHEET 2 H 2 TYR B 255 GLY B 256 -1 O TYR B 255 N VAL B 229
SHEET 1 I 6 TYR C 76 ARG C 84 0
SHEET 2 I 6 GLY C 88 HIS C 95 -1 O LEU C 92 N LYS C 80
SHEET 3 I 6 VAL C 101 SER C 108 -1 O MET C 104 N GLN C 91
SHEET 4 I 6 TYR C 148 MET C 153 -1 O MET C 153 N ALA C 103
SHEET 5 I 6 LEU C 139 GLN C 144 -1 N TYR C 141 O VAL C 152
SHEET 6 I 6 TYR C 399 TYR C 400 -1 O TYR C 399 N ALA C 142
SHEET 1 J 3 GLY C 159 ASP C 160 0
SHEET 2 J 3 MET C 204 LEU C 206 -1 O LEU C 206 N GLY C 159
SHEET 3 J 3 LEU C 212 LEU C 214 -1 O LYS C 213 N LEU C 205
SHEET 1 K 2 PHE C 194 ILE C 195 0
SHEET 2 K 2 MET C 221 LYS C 222 -1 O MET C 221 N ILE C 195
SHEET 1 L 2 MET C 228 ARG C 230 0
SHEET 2 L 2 TYR C 254 GLY C 256 -1 O TYR C 255 N VAL C 229
SHEET 1 M 6 TYR D 76 ARG D 84 0
SHEET 2 M 6 GLU D 89 HIS D 95 -1 O LEU D 92 N VAL D 79
SHEET 3 M 6 VAL D 101 SER D 108 -1 O LEU D 106 N GLU D 89
SHEET 4 M 6 TYR D 148 GLU D 154 -1 O MET D 153 N ALA D 103
SHEET 5 M 6 LEU D 139 GLN D 144 -1 N TYR D 141 O VAL D 152
SHEET 6 M 6 TYR D 399 TYR D 400 -1 O TYR D 399 N ALA D 142
SHEET 1 N 3 GLY D 159 ASP D 160 0
SHEET 2 N 3 MET D 204 LEU D 206 -1 O LEU D 206 N GLY D 159
SHEET 3 N 3 LEU D 212 LEU D 214 -1 O LYS D 213 N LEU D 205
SHEET 1 O 2 PHE D 194 ILE D 195 0
SHEET 2 O 2 MET D 221 LYS D 222 -1 O MET D 221 N ILE D 195
SHEET 1 P 2 MET D 228 VAL D 229 0
SHEET 2 P 2 TYR D 255 GLY D 256 -1 O TYR D 255 N VAL D 229
CISPEP 1 ASP A 301 ASP A 302 0 -9.26
CISPEP 2 ASP C 301 ASP C 302 0 -9.36
SITE 1 AC1 11 GLY A 85 GLY A 88 GLU A 89 VAL A 90
SITE 2 AC1 11 ALA A 103 GLU A 154 TYR A 155 MET A 156
SITE 3 AC1 11 LEU A 205 ASP A 216 HOH A 708
SITE 1 AC2 12 ARG B 84 GLY B 85 GLY B 88 VAL B 90
SITE 2 AC2 12 ALA B 103 LYS B 105 MET B 153 GLU B 154
SITE 3 AC2 12 TYR B 155 MET B 156 LEU B 205 ASP B 216
SITE 1 AC3 13 ARG C 84 GLY C 85 GLY C 88 GLU C 89
SITE 2 AC3 13 VAL C 90 ALA C 103 MET C 153 GLU C 154
SITE 3 AC3 13 TYR C 155 MET C 156 LEU C 205 ASP C 216
SITE 4 AC3 13 HOH C 710
SITE 1 AC4 12 ARG D 84 GLY D 85 GLY D 88 VAL D 90
SITE 2 AC4 12 ALA D 103 LYS D 105 MET D 153 GLU D 154
SITE 3 AC4 12 TYR D 155 MET D 156 LEU D 205 ASP D 216
CRYST1 151.720 152.110 186.140 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 0.006591 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005372 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
