HEADER TRANSFERASE 12-DEC-16 5U7Q
TITLE IDENTIFICATION OF A NEW CLASS OF POTENT CDC7 INHIBITORS DESIGNED BY
TITLE 2 PUTATIVE PHARMACOPHORE MODEL: SYNTHESIS AND BIOLOGICAL EVALUATION OF
TITLE 3 2,3-DIHYDROTHIENO[3,2-D]PYRIMIDIN-4(1H)-ONES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO-ASSOCIATED PROTEIN KINASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 23-417;
COMPND 5 SYNONYM: RHO KINASE 2,RHO-ASSOCIATED,COILED-COIL-CONTAINING PROTEIN
COMPND 6 KINASE 2,COILED-COIL-CONTAINING PROTEIN KINASE II,ROCK-II,P164 ROCK-
COMPND 7 2;
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: ROCK2, KIAA0619;
SOURCE 6 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 274590;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PFASTBACHTB
KEYWDS SERINE/THREONINE KINASE, APO-PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.D.HOFFMAN
REVDAT 4 06-MAR-24 5U7Q 1 REMARK
REVDAT 3 22-NOV-17 5U7Q 1 REMARK
REVDAT 2 05-APR-17 5U7Q 1 JRNL
REVDAT 1 29-MAR-17 5U7Q 0
JRNL AUTH O.KURASAWA,Y.OGURO,T.MIYAZAKI,M.HOMMA,K.MORI,K.IWAI,H.HARA,
JRNL AUTH 2 R.SKENE,I.HOFFMAN,A.OHASHI,S.YOSHIDA,T.ISHIKAWA,N.CHO
JRNL TITL IDENTIFICATION OF A NEW CLASS OF POTENT CDC7 INHIBITORS
JRNL TITL 2 DESIGNED BY PUTATIVE PHARMACOPHORE MODEL: SYNTHESIS AND
JRNL TITL 3 BIOLOGICAL EVALUATION OF
JRNL TITL 4 2,3-DIHYDROTHIENO[3,2-D]PYRIMIDIN-4(1H)-ONES.
JRNL REF BIOORG. MED. CHEM. V. 25 2133 2017
JRNL REFN ESSN 1464-3391
JRNL PMID 28284870
JRNL DOI 10.1016/J.BMC.2017.02.021
REMARK 2
REMARK 2 RESOLUTION. 3.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 48123
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2611
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.20
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2650
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12530
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.78000
REMARK 3 B22 (A**2) : -2.85000
REMARK 3 B33 (A**2) : -0.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.381
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.303
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.328
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12840 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12086 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17355 ; 1.661 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27829 ; 1.565 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1537 ; 7.114 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 639 ;34.061 ;24.069
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2235 ;17.788 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;20.909 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1837 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14469 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3035 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 28 416 B 28 416 45034 0.110 0.050
REMARK 3 2 A 25 416 C 25 416 46150 0.100 0.050
REMARK 3 3 A 27 417 D 27 417 45228 0.110 0.050
REMARK 3 4 B 28 416 C 28 416 46314 0.090 0.050
REMARK 3 5 B 28 417 D 28 417 46550 0.080 0.050
REMARK 3 6 C 27 416 D 27 416 45824 0.090 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 25 A 173
REMARK 3 ORIGIN FOR THE GROUP (A): 59.2756 -16.3328 15.7980
REMARK 3 T TENSOR
REMARK 3 T11: 0.0788 T22: 0.0414
REMARK 3 T33: 0.3352 T12: -0.0184
REMARK 3 T13: -0.0424 T23: 0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 3.3551 L22: 1.9913
REMARK 3 L33: 2.9516 L12: 1.5604
REMARK 3 L13: 1.7728 L23: 2.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0678 S12: 0.0820 S13: -0.2099
REMARK 3 S21: -0.0963 S22: 0.0762 S23: -0.4589
REMARK 3 S31: -0.2596 S32: 0.2508 S33: -0.0083
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 174 A 417
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5575 -16.4642 11.3073
REMARK 3 T TENSOR
REMARK 3 T11: 0.0522 T22: 0.1694
REMARK 3 T33: 0.1727 T12: 0.0268
REMARK 3 T13: -0.0818 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 3.2812 L22: 2.4055
REMARK 3 L33: 2.0623 L12: 0.4141
REMARK 3 L13: 0.0927 L23: 0.1124
REMARK 3 S TENSOR
REMARK 3 S11: -0.0047 S12: 0.3188 S13: -0.0728
REMARK 3 S21: -0.1650 S22: -0.0382 S23: 0.2851
REMARK 3 S31: -0.1380 S32: -0.3837 S33: 0.0429
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 28 B 173
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2390 -16.7788 40.7845
REMARK 3 T TENSOR
REMARK 3 T11: 0.1676 T22: 0.0673
REMARK 3 T33: 0.3361 T12: -0.0060
REMARK 3 T13: -0.0973 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 3.7863 L22: 2.4220
REMARK 3 L33: 2.7459 L12: -1.3201
REMARK 3 L13: 1.9722 L23: -2.4018
REMARK 3 S TENSOR
REMARK 3 S11: -0.1296 S12: 0.1423 S13: 0.0894
REMARK 3 S21: 0.1261 S22: 0.1820 S23: 0.3211
REMARK 3 S31: -0.3106 S32: -0.1435 S33: -0.0524
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 174 B 417
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3449 -18.4814 46.7595
REMARK 3 T TENSOR
REMARK 3 T11: 0.0996 T22: 0.2135
REMARK 3 T33: 0.2902 T12: -0.0211
REMARK 3 T13: -0.0654 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 3.4243 L22: 1.7688
REMARK 3 L33: 1.5117 L12: -0.0761
REMARK 3 L13: 0.0636 L23: -0.4867
REMARK 3 S TENSOR
REMARK 3 S11: -0.0152 S12: -0.1053 S13: 0.0271
REMARK 3 S21: 0.0755 S22: -0.0756 S23: -0.3353
REMARK 3 S31: -0.0989 S32: 0.3385 S33: 0.0908
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 25 C 173
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0043 21.1715 74.3374
REMARK 3 T TENSOR
REMARK 3 T11: 0.5161 T22: 0.0969
REMARK 3 T33: 0.2308 T12: -0.1105
REMARK 3 T13: -0.1034 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.7778 L22: 1.2237
REMARK 3 L33: 4.2315 L12: -1.0762
REMARK 3 L13: 1.1084 L23: -1.9392
REMARK 3 S TENSOR
REMARK 3 S11: 0.0986 S12: -0.2901 S13: -0.3389
REMARK 3 S21: 0.2304 S22: 0.1114 S23: 0.1340
REMARK 3 S31: -0.0900 S32: -0.0957 S33: -0.2099
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 174 C 417
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1098 21.4775 46.6344
REMARK 3 T TENSOR
REMARK 3 T11: 0.2010 T22: 0.1584
REMARK 3 T33: 0.1874 T12: -0.0417
REMARK 3 T13: 0.0196 T23: -0.0715
REMARK 3 L TENSOR
REMARK 3 L11: 1.5226 L22: 2.7712
REMARK 3 L33: 3.1044 L12: 0.1130
REMARK 3 L13: -0.2718 L23: -0.0211
REMARK 3 S TENSOR
REMARK 3 S11: 0.0533 S12: 0.2786 S13: -0.0890
REMARK 3 S21: -0.2883 S22: 0.0128 S23: -0.3856
REMARK 3 S31: -0.0821 S32: -0.0234 S33: -0.0661
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 27 D 173
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3411 21.8367 -16.3406
REMARK 3 T TENSOR
REMARK 3 T11: 0.4266 T22: 0.1292
REMARK 3 T33: 0.3439 T12: -0.0000
REMARK 3 T13: -0.0758 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 1.1899 L22: 2.0974
REMARK 3 L33: 4.1590 L12: 1.2458
REMARK 3 L13: 0.8887 L23: 1.6801
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: 0.1937 S13: -0.3148
REMARK 3 S21: -0.3812 S22: 0.2067 S23: 0.0337
REMARK 3 S31: 0.2078 S32: -0.1964 S33: -0.1542
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 174 D 417
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6175 23.4917 11.8808
REMARK 3 T TENSOR
REMARK 3 T11: 0.3006 T22: 0.1679
REMARK 3 T33: 0.2327 T12: 0.0632
REMARK 3 T13: -0.0008 T23: 0.0531
REMARK 3 L TENSOR
REMARK 3 L11: 0.7995 L22: 2.1682
REMARK 3 L33: 3.3532 L12: 0.3628
REMARK 3 L13: -0.7485 L23: -0.5832
REMARK 3 S TENSOR
REMARK 3 S11: 0.0656 S12: -0.0875 S13: -0.0133
REMARK 3 S21: 0.2268 S22: 0.1264 S23: 0.2495
REMARK 3 S31: -0.2317 S32: -0.1118 S33: -0.1920
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5U7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225454.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9764848
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51367
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.83300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 70.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1 M SODIUM MALONATE PH 7.0, 0.1 M
REMARK 280 HEPES PH 7.0, 0.5% V/V JEFFAMINE ED-2001 PH 7.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 73.23150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 91.19400
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -12.41390
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 111.72848
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 23
REMARK 465 ALA A 24
REMARK 465 ASP A 389
REMARK 465 ASP A 390
REMARK 465 LYS A 391
REMARK 465 GLY A 392
REMARK 465 ASP A 393
REMARK 465 GLY B 23
REMARK 465 ALA B 24
REMARK 465 SER B 25
REMARK 465 ARG B 26
REMARK 465 GLN B 27
REMARK 465 ASP B 389
REMARK 465 ASP B 390
REMARK 465 LYS B 391
REMARK 465 GLY B 392
REMARK 465 ASP B 393
REMARK 465 ASP C 389
REMARK 465 ASP C 390
REMARK 465 LYS C 391
REMARK 465 GLY C 392
REMARK 465 ASP C 393
REMARK 465 GLY D 23
REMARK 465 ALA D 24
REMARK 465 SER D 25
REMARK 465 ARG D 26
REMARK 465 HIS D 246
REMARK 465 CYS D 247
REMARK 465 ASP D 248
REMARK 465 ASP D 389
REMARK 465 ASP D 390
REMARK 465 LYS D 391
REMARK 465 GLY D 392
REMARK 465 ASP D 393
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL D 300 O TYR D 303 2.14
REMARK 500 OH TYR A 256 OE1 GLU A 286 2.18
REMARK 500 OD1 ASP C 240 OG1 THR C 242 2.18
REMARK 500 OH TYR C 256 OE1 GLU C 286 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 142 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 268 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 PHE A 403 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG B 213 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 CYS B 247 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 PHE B 270 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 PHE B 270 CB - CG - CD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG C 28 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 240 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP C 357 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG C 417 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 35 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG D 213 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 TYR D 303 N - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 SER D 304 N - CA - CB ANGL. DEV. = 13.1 DEGREES
REMARK 500 LYS D 355 CA - CB - CG ANGL. DEV. = 15.9 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 GLN A 27 20.30 -70.77
REMARK 500 LEU A 30 -70.42 -50.66
REMARK 500 ASP A 214 52.50 -161.73
REMARK 500 ASP A 268 71.68 0.47
REMARK 500 PHE A 270 84.30 -160.99
REMARK 500 ASP A 308 42.99 -95.66
REMARK 500 ALA A 319 100.60 -53.53
REMARK 500 GLU A 395 114.59 166.22
REMARK 500 LYS A 401 -63.32 -92.73
REMARK 500 PHE A 403 114.40 165.51
REMARK 500 LEU B 30 -75.73 -38.75
REMARK 500 ASP B 214 53.11 -161.49
REMARK 500 HIS B 246 58.03 -114.29
REMARK 500 CYS B 247 -154.97 59.04
REMARK 500 THR B 253 109.20 0.71
REMARK 500 ASP B 268 -68.32 -132.90
REMARK 500 ASP B 308 43.64 -96.19
REMARK 500 ALA B 319 100.82 -42.69
REMARK 500 GLU B 395 117.53 132.64
REMARK 500 ALA C 24 50.82 -94.74
REMARK 500 ARG C 28 -78.57 -20.62
REMARK 500 LEU C 30 -74.65 -36.88
REMARK 500 ASP C 214 51.36 -160.97
REMARK 500 ASP C 268 70.79 1.09
REMARK 500 PHE C 270 85.98 -161.07
REMARK 500 ASP C 308 43.70 -96.61
REMARK 500 ALA C 319 99.98 -53.43
REMARK 500 GLU C 395 115.64 137.39
REMARK 500 LEU D 30 -76.18 -43.85
REMARK 500 ASP D 214 52.06 -160.63
REMARK 500 ALA D 250 133.20 37.56
REMARK 500 VAL D 251 128.46 129.84
REMARK 500 PRO D 254 -74.55 -69.88
REMARK 500 ASP D 255 -59.82 26.46
REMARK 500 ASP D 268 89.69 23.40
REMARK 500 SER D 304 -55.14 118.27
REMARK 500 ASP D 308 43.48 -96.31
REMARK 500 ALA D 319 100.64 -42.78
REMARK 500 GLU D 395 118.12 131.46
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 HIS B 246 CYS B 247 139.10
REMARK 500 GLY B 269 PHE B 270 -130.29
REMARK 500 VAL D 251 GLY D 252 128.23
REMARK 500 GLY D 252 THR D 253 140.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U7R RELATED DB: PDB
DBREF 5U7Q A 23 417 UNP O75116 ROCK2_HUMAN 23 417
DBREF 5U7Q B 23 417 UNP O75116 ROCK2_HUMAN 23 417
DBREF 5U7Q C 23 417 UNP O75116 ROCK2_HUMAN 23 417
DBREF 5U7Q D 23 417 UNP O75116 ROCK2_HUMAN 23 417
SEQRES 1 A 395 GLY ALA SER ARG GLN ARG LYS LEU GLU ALA LEU ILE ARG
SEQRES 2 A 395 ASP PRO ARG SER PRO ILE ASN VAL GLU SER LEU LEU ASP
SEQRES 3 A 395 GLY LEU ASN SER LEU VAL LEU ASP LEU ASP PHE PRO ALA
SEQRES 4 A 395 LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU ASN ARG
SEQRES 5 A 395 TYR GLU LYS ILE VAL LYS LYS ILE ARG GLY LEU GLN MET
SEQRES 6 A 395 LYS ALA GLU ASP TYR ASP VAL VAL LYS VAL ILE GLY ARG
SEQRES 7 A 395 GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS ALA
SEQRES 8 A 395 SER GLN LYS VAL TYR ALA MET LYS LEU LEU SER LYS PHE
SEQRES 9 A 395 GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP GLU
SEQRES 10 A 395 GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP VAL
SEQRES 11 A 395 VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR LEU
SEQRES 12 A 395 TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU VAL
SEQRES 13 A 395 ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP ALA
SEQRES 14 A 395 LYS PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP ALA
SEQRES 15 A 395 ILE HIS SER MET GLY LEU ILE HIS ARG ASP VAL LYS PRO
SEQRES 16 A 395 ASP ASN MET LEU LEU ASP LYS HIS GLY HIS LEU LYS LEU
SEQRES 17 A 395 ALA ASP PHE GLY THR CYS MET LYS MET ASP GLU THR GLY
SEQRES 18 A 395 MET VAL HIS CYS ASP THR ALA VAL GLY THR PRO ASP TYR
SEQRES 19 A 395 ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP GLY
SEQRES 20 A 395 PHE TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY VAL
SEQRES 21 A 395 PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE TYR
SEQRES 22 A 395 ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET ASP
SEQRES 23 A 395 HIS LYS ASN SER LEU CYS PHE PRO GLU ASP ALA GLU ILE
SEQRES 24 A 395 SER LYS HIS ALA LYS ASN LEU ILE CYS ALA PHE LEU THR
SEQRES 25 A 395 ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU GLU
SEQRES 26 A 395 ILE ARG GLN HIS PRO PHE PHE LYS ASN ASP GLN TRP HIS
SEQRES 27 A 395 TRP ASP ASN ILE ARG GLU THR ALA ALA PRO VAL VAL PRO
SEQRES 28 A 395 GLU LEU SER SER ASP ILE ASP SER SER ASN PHE ASP ASP
SEQRES 29 A 395 ILE GLU ASP ASP LYS GLY ASP VAL GLU THR PHE PRO ILE
SEQRES 30 A 395 PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE ILE GLY
SEQRES 31 A 395 PHE THR TYR TYR ARG
SEQRES 1 B 395 GLY ALA SER ARG GLN ARG LYS LEU GLU ALA LEU ILE ARG
SEQRES 2 B 395 ASP PRO ARG SER PRO ILE ASN VAL GLU SER LEU LEU ASP
SEQRES 3 B 395 GLY LEU ASN SER LEU VAL LEU ASP LEU ASP PHE PRO ALA
SEQRES 4 B 395 LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU ASN ARG
SEQRES 5 B 395 TYR GLU LYS ILE VAL LYS LYS ILE ARG GLY LEU GLN MET
SEQRES 6 B 395 LYS ALA GLU ASP TYR ASP VAL VAL LYS VAL ILE GLY ARG
SEQRES 7 B 395 GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS ALA
SEQRES 8 B 395 SER GLN LYS VAL TYR ALA MET LYS LEU LEU SER LYS PHE
SEQRES 9 B 395 GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP GLU
SEQRES 10 B 395 GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP VAL
SEQRES 11 B 395 VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR LEU
SEQRES 12 B 395 TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU VAL
SEQRES 13 B 395 ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP ALA
SEQRES 14 B 395 LYS PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP ALA
SEQRES 15 B 395 ILE HIS SER MET GLY LEU ILE HIS ARG ASP VAL LYS PRO
SEQRES 16 B 395 ASP ASN MET LEU LEU ASP LYS HIS GLY HIS LEU LYS LEU
SEQRES 17 B 395 ALA ASP PHE GLY THR CYS MET LYS MET ASP GLU THR GLY
SEQRES 18 B 395 MET VAL HIS CYS ASP THR ALA VAL GLY THR PRO ASP TYR
SEQRES 19 B 395 ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP GLY
SEQRES 20 B 395 PHE TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY VAL
SEQRES 21 B 395 PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE TYR
SEQRES 22 B 395 ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET ASP
SEQRES 23 B 395 HIS LYS ASN SER LEU CYS PHE PRO GLU ASP ALA GLU ILE
SEQRES 24 B 395 SER LYS HIS ALA LYS ASN LEU ILE CYS ALA PHE LEU THR
SEQRES 25 B 395 ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU GLU
SEQRES 26 B 395 ILE ARG GLN HIS PRO PHE PHE LYS ASN ASP GLN TRP HIS
SEQRES 27 B 395 TRP ASP ASN ILE ARG GLU THR ALA ALA PRO VAL VAL PRO
SEQRES 28 B 395 GLU LEU SER SER ASP ILE ASP SER SER ASN PHE ASP ASP
SEQRES 29 B 395 ILE GLU ASP ASP LYS GLY ASP VAL GLU THR PHE PRO ILE
SEQRES 30 B 395 PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE ILE GLY
SEQRES 31 B 395 PHE THR TYR TYR ARG
SEQRES 1 C 395 GLY ALA SER ARG GLN ARG LYS LEU GLU ALA LEU ILE ARG
SEQRES 2 C 395 ASP PRO ARG SER PRO ILE ASN VAL GLU SER LEU LEU ASP
SEQRES 3 C 395 GLY LEU ASN SER LEU VAL LEU ASP LEU ASP PHE PRO ALA
SEQRES 4 C 395 LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU ASN ARG
SEQRES 5 C 395 TYR GLU LYS ILE VAL LYS LYS ILE ARG GLY LEU GLN MET
SEQRES 6 C 395 LYS ALA GLU ASP TYR ASP VAL VAL LYS VAL ILE GLY ARG
SEQRES 7 C 395 GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS ALA
SEQRES 8 C 395 SER GLN LYS VAL TYR ALA MET LYS LEU LEU SER LYS PHE
SEQRES 9 C 395 GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP GLU
SEQRES 10 C 395 GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP VAL
SEQRES 11 C 395 VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR LEU
SEQRES 12 C 395 TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU VAL
SEQRES 13 C 395 ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP ALA
SEQRES 14 C 395 LYS PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP ALA
SEQRES 15 C 395 ILE HIS SER MET GLY LEU ILE HIS ARG ASP VAL LYS PRO
SEQRES 16 C 395 ASP ASN MET LEU LEU ASP LYS HIS GLY HIS LEU LYS LEU
SEQRES 17 C 395 ALA ASP PHE GLY THR CYS MET LYS MET ASP GLU THR GLY
SEQRES 18 C 395 MET VAL HIS CYS ASP THR ALA VAL GLY THR PRO ASP TYR
SEQRES 19 C 395 ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP GLY
SEQRES 20 C 395 PHE TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY VAL
SEQRES 21 C 395 PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE TYR
SEQRES 22 C 395 ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET ASP
SEQRES 23 C 395 HIS LYS ASN SER LEU CYS PHE PRO GLU ASP ALA GLU ILE
SEQRES 24 C 395 SER LYS HIS ALA LYS ASN LEU ILE CYS ALA PHE LEU THR
SEQRES 25 C 395 ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU GLU
SEQRES 26 C 395 ILE ARG GLN HIS PRO PHE PHE LYS ASN ASP GLN TRP HIS
SEQRES 27 C 395 TRP ASP ASN ILE ARG GLU THR ALA ALA PRO VAL VAL PRO
SEQRES 28 C 395 GLU LEU SER SER ASP ILE ASP SER SER ASN PHE ASP ASP
SEQRES 29 C 395 ILE GLU ASP ASP LYS GLY ASP VAL GLU THR PHE PRO ILE
SEQRES 30 C 395 PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE ILE GLY
SEQRES 31 C 395 PHE THR TYR TYR ARG
SEQRES 1 D 395 GLY ALA SER ARG GLN ARG LYS LEU GLU ALA LEU ILE ARG
SEQRES 2 D 395 ASP PRO ARG SER PRO ILE ASN VAL GLU SER LEU LEU ASP
SEQRES 3 D 395 GLY LEU ASN SER LEU VAL LEU ASP LEU ASP PHE PRO ALA
SEQRES 4 D 395 LEU ARG LYS ASN LYS ASN ILE ASP ASN PHE LEU ASN ARG
SEQRES 5 D 395 TYR GLU LYS ILE VAL LYS LYS ILE ARG GLY LEU GLN MET
SEQRES 6 D 395 LYS ALA GLU ASP TYR ASP VAL VAL LYS VAL ILE GLY ARG
SEQRES 7 D 395 GLY ALA PHE GLY GLU VAL GLN LEU VAL ARG HIS LYS ALA
SEQRES 8 D 395 SER GLN LYS VAL TYR ALA MET LYS LEU LEU SER LYS PHE
SEQRES 9 D 395 GLU MET ILE LYS ARG SER ASP SER ALA PHE PHE TRP GLU
SEQRES 10 D 395 GLU ARG ASP ILE MET ALA PHE ALA ASN SER PRO TRP VAL
SEQRES 11 D 395 VAL GLN LEU PHE TYR ALA PHE GLN ASP ASP ARG TYR LEU
SEQRES 12 D 395 TYR MET VAL MET GLU TYR MET PRO GLY GLY ASP LEU VAL
SEQRES 13 D 395 ASN LEU MET SER ASN TYR ASP VAL PRO GLU LYS TRP ALA
SEQRES 14 D 395 LYS PHE TYR THR ALA GLU VAL VAL LEU ALA LEU ASP ALA
SEQRES 15 D 395 ILE HIS SER MET GLY LEU ILE HIS ARG ASP VAL LYS PRO
SEQRES 16 D 395 ASP ASN MET LEU LEU ASP LYS HIS GLY HIS LEU LYS LEU
SEQRES 17 D 395 ALA ASP PHE GLY THR CYS MET LYS MET ASP GLU THR GLY
SEQRES 18 D 395 MET VAL HIS CYS ASP THR ALA VAL GLY THR PRO ASP TYR
SEQRES 19 D 395 ILE SER PRO GLU VAL LEU LYS SER GLN GLY GLY ASP GLY
SEQRES 20 D 395 PHE TYR GLY ARG GLU CYS ASP TRP TRP SER VAL GLY VAL
SEQRES 21 D 395 PHE LEU TYR GLU MET LEU VAL GLY ASP THR PRO PHE TYR
SEQRES 22 D 395 ALA ASP SER LEU VAL GLY THR TYR SER LYS ILE MET ASP
SEQRES 23 D 395 HIS LYS ASN SER LEU CYS PHE PRO GLU ASP ALA GLU ILE
SEQRES 24 D 395 SER LYS HIS ALA LYS ASN LEU ILE CYS ALA PHE LEU THR
SEQRES 25 D 395 ASP ARG GLU VAL ARG LEU GLY ARG ASN GLY VAL GLU GLU
SEQRES 26 D 395 ILE ARG GLN HIS PRO PHE PHE LYS ASN ASP GLN TRP HIS
SEQRES 27 D 395 TRP ASP ASN ILE ARG GLU THR ALA ALA PRO VAL VAL PRO
SEQRES 28 D 395 GLU LEU SER SER ASP ILE ASP SER SER ASN PHE ASP ASP
SEQRES 29 D 395 ILE GLU ASP ASP LYS GLY ASP VAL GLU THR PHE PRO ILE
SEQRES 30 D 395 PRO LYS ALA PHE VAL GLY ASN GLN LEU PRO PHE ILE GLY
SEQRES 31 D 395 PHE THR TYR TYR ARG
FORMUL 5 HOH *10(H2 O)
HELIX 1 AA1 GLN A 27 ASP A 36 1 10
HELIX 2 AA2 ASN A 42 ASP A 58 1 17
HELIX 3 AA3 ALA A 61 LYS A 64 5 4
HELIX 4 AA4 ASN A 65 GLN A 86 1 22
HELIX 5 AA5 LYS A 88 GLU A 90 5 3
HELIX 6 AA6 LYS A 125 ARG A 131 1 7
HELIX 7 AA7 PHE A 136 ALA A 147 1 12
HELIX 8 AA8 ASP A 176 SER A 182 1 7
HELIX 9 AA9 PRO A 187 MET A 208 1 22
HELIX 10 AB1 LYS A 216 ASP A 218 5 3
HELIX 11 AB2 THR A 253 ILE A 257 5 5
HELIX 12 AB3 SER A 258 SER A 264 1 7
HELIX 13 AB4 GLN A 265 GLY A 267 5 3
HELIX 14 AB5 ARG A 273 GLY A 290 1 18
HELIX 15 AB6 SER A 298 ASP A 308 1 11
HELIX 16 AB7 ASP A 308 LEU A 313 1 6
HELIX 17 AB8 SER A 322 LEU A 333 1 12
HELIX 18 AB9 ASP A 335 ARG A 339 5 5
HELIX 19 AC1 VAL A 345 GLN A 350 1 6
HELIX 20 AC2 HIS A 351 LYS A 355 5 5
HELIX 21 AC3 ASN A 363 THR A 367 5 5
HELIX 22 AC4 GLN A 407 ILE A 411 5 5
HELIX 23 AC5 LYS B 29 ASP B 36 1 8
HELIX 24 AC6 ASN B 42 ASP B 58 1 17
HELIX 25 AC7 ALA B 61 LYS B 64 5 4
HELIX 26 AC8 ASN B 65 GLN B 86 1 22
HELIX 27 AC9 LYS B 88 GLU B 90 5 3
HELIX 28 AD1 LYS B 125 ARG B 131 1 7
HELIX 29 AD2 PHE B 136 ALA B 147 1 12
HELIX 30 AD3 ASP B 176 SER B 182 1 7
HELIX 31 AD4 PRO B 187 MET B 208 1 22
HELIX 32 AD5 LYS B 216 ASP B 218 5 3
HELIX 33 AD6 SER B 258 GLN B 265 1 8
HELIX 34 AD7 ARG B 273 GLY B 290 1 18
HELIX 35 AD8 SER B 298 ASP B 308 1 11
HELIX 36 AD9 ASP B 308 LEU B 313 1 6
HELIX 37 AE1 SER B 322 LEU B 333 1 12
HELIX 38 AE2 ASP B 335 ARG B 339 5 5
HELIX 39 AE3 VAL B 345 GLN B 350 1 6
HELIX 40 AE4 HIS B 351 LYS B 355 5 5
HELIX 41 AE5 ASN B 363 THR B 367 5 5
HELIX 42 AE6 GLN B 407 ILE B 411 5 5
HELIX 43 AE7 ARG C 26 ASP C 36 1 11
HELIX 44 AE8 ASN C 42 ASP C 58 1 17
HELIX 45 AE9 ALA C 61 LYS C 64 5 4
HELIX 46 AF1 ASN C 65 GLN C 86 1 22
HELIX 47 AF2 LYS C 88 GLU C 90 5 3
HELIX 48 AF3 LYS C 125 ARG C 131 1 7
HELIX 49 AF4 PHE C 136 ALA C 147 1 12
HELIX 50 AF5 ASP C 176 SER C 182 1 7
HELIX 51 AF6 PRO C 187 MET C 208 1 22
HELIX 52 AF7 LYS C 216 ASP C 218 5 3
HELIX 53 AF8 THR C 253 ILE C 257 5 5
HELIX 54 AF9 SER C 258 SER C 264 1 7
HELIX 55 AG1 GLN C 265 GLY C 267 5 3
HELIX 56 AG2 ARG C 273 GLY C 290 1 18
HELIX 57 AG3 SER C 298 ASP C 308 1 11
HELIX 58 AG4 ASP C 308 LEU C 313 1 6
HELIX 59 AG5 SER C 322 LEU C 333 1 12
HELIX 60 AG6 ASP C 335 ARG C 339 5 5
HELIX 61 AG7 VAL C 345 GLN C 350 1 6
HELIX 62 AG8 HIS C 351 LYS C 355 5 5
HELIX 63 AG9 ASN C 363 THR C 367 5 5
HELIX 64 AH1 GLN C 407 ILE C 411 5 5
HELIX 65 AH2 ARG D 28 ASP D 36 1 9
HELIX 66 AH3 ASN D 42 ASP D 58 1 17
HELIX 67 AH4 ALA D 61 LYS D 64 5 4
HELIX 68 AH5 ASN D 65 GLN D 86 1 22
HELIX 69 AH6 LYS D 88 GLU D 90 5 3
HELIX 70 AH7 LYS D 125 ARG D 131 1 7
HELIX 71 AH8 PHE D 136 ALA D 147 1 12
HELIX 72 AH9 ASP D 176 SER D 182 1 7
HELIX 73 AI1 PRO D 187 MET D 208 1 22
HELIX 74 AI2 LYS D 216 ASP D 218 5 3
HELIX 75 AI3 SER D 258 GLN D 265 1 8
HELIX 76 AI4 ARG D 273 GLY D 290 1 18
HELIX 77 AI5 SER D 298 ILE D 306 1 9
HELIX 78 AI6 ASP D 308 LEU D 313 1 6
HELIX 79 AI7 SER D 322 LEU D 333 1 12
HELIX 80 AI8 ASP D 335 ARG D 339 5 5
HELIX 81 AI9 VAL D 345 GLN D 350 1 6
HELIX 82 AJ1 HIS D 351 LYS D 355 5 5
HELIX 83 AJ2 ASN D 363 THR D 367 5 5
HELIX 84 AJ3 GLN D 407 ILE D 411 5 5
SHEET 1 AA1 6 TYR A 92 ARG A 100 0
SHEET 2 AA1 6 GLU A 105 HIS A 111 -1 O LEU A 108 N LYS A 96
SHEET 3 AA1 6 VAL A 117 SER A 124 -1 O MET A 120 N GLN A 107
SHEET 4 AA1 6 TYR A 164 MET A 169 -1 O MET A 169 N ALA A 119
SHEET 5 AA1 6 LEU A 155 GLN A 160 -1 N TYR A 157 O VAL A 168
SHEET 6 AA1 6 TYR A 415 TYR A 416 -1 O TYR A 415 N ALA A 158
SHEET 1 AA2 2 LEU A 210 ILE A 211 0
SHEET 2 AA2 2 MET A 237 LYS A 238 -1 O MET A 237 N ILE A 211
SHEET 1 AA3 2 MET A 220 LEU A 222 0
SHEET 2 AA3 2 LEU A 228 LEU A 230 -1 O LYS A 229 N LEU A 221
SHEET 1 AA4 2 VAL A 245 CYS A 247 0
SHEET 2 AA4 2 GLY A 269 TYR A 271 -1 O TYR A 271 N VAL A 245
SHEET 1 AA5 6 TYR B 92 ARG B 100 0
SHEET 2 AA5 6 GLU B 105 HIS B 111 -1 O LEU B 108 N LYS B 96
SHEET 3 AA5 6 VAL B 117 SER B 124 -1 O MET B 120 N GLN B 107
SHEET 4 AA5 6 TYR B 164 MET B 169 -1 O MET B 169 N ALA B 119
SHEET 5 AA5 6 LEU B 155 GLN B 160 -1 N TYR B 157 O VAL B 168
SHEET 6 AA5 6 TYR B 415 TYR B 416 -1 O TYR B 415 N ALA B 158
SHEET 1 AA6 2 LEU B 210 ILE B 211 0
SHEET 2 AA6 2 MET B 237 LYS B 238 -1 O MET B 237 N ILE B 211
SHEET 1 AA7 2 MET B 220 LEU B 222 0
SHEET 2 AA7 2 LEU B 228 LEU B 230 -1 O LYS B 229 N LEU B 221
SHEET 1 AA8 2 MET B 244 HIS B 246 0
SHEET 2 AA8 2 PHE B 270 GLY B 272 -1 O TYR B 271 N VAL B 245
SHEET 1 AA9 6 TYR C 92 ARG C 100 0
SHEET 2 AA9 6 GLU C 105 HIS C 111 -1 O LEU C 108 N LYS C 96
SHEET 3 AA9 6 VAL C 117 SER C 124 -1 O MET C 120 N GLN C 107
SHEET 4 AA9 6 TYR C 164 MET C 169 -1 O MET C 169 N ALA C 119
SHEET 5 AA9 6 LEU C 155 GLN C 160 -1 N TYR C 157 O VAL C 168
SHEET 6 AA9 6 TYR C 415 TYR C 416 -1 O TYR C 415 N ALA C 158
SHEET 1 AB1 2 LEU C 210 ILE C 211 0
SHEET 2 AB1 2 MET C 237 LYS C 238 -1 O MET C 237 N ILE C 211
SHEET 1 AB2 2 MET C 220 LEU C 222 0
SHEET 2 AB2 2 LEU C 228 LEU C 230 -1 O LYS C 229 N LEU C 221
SHEET 1 AB3 2 MET C 244 CYS C 247 0
SHEET 2 AB3 2 GLY C 269 GLY C 272 -1 O TYR C 271 N VAL C 245
SHEET 1 AB4 6 TYR D 92 ARG D 100 0
SHEET 2 AB4 6 GLU D 105 HIS D 111 -1 O LEU D 108 N LYS D 96
SHEET 3 AB4 6 VAL D 117 SER D 124 -1 O MET D 120 N GLN D 107
SHEET 4 AB4 6 TYR D 164 MET D 169 -1 O MET D 169 N ALA D 119
SHEET 5 AB4 6 LEU D 155 GLN D 160 -1 N TYR D 157 O VAL D 168
SHEET 6 AB4 6 TYR D 415 TYR D 416 -1 O TYR D 415 N ALA D 158
SHEET 1 AB5 2 LEU D 210 ILE D 211 0
SHEET 2 AB5 2 MET D 237 LYS D 238 -1 O MET D 237 N ILE D 211
SHEET 1 AB6 2 MET D 220 LEU D 222 0
SHEET 2 AB6 2 LEU D 228 LEU D 230 -1 O LYS D 229 N LEU D 221
SHEET 1 AB7 2 MET D 244 VAL D 245 0
SHEET 2 AB7 2 TYR D 271 GLY D 272 -1 O TYR D 271 N VAL D 245
CRYST1 91.194 146.463 112.416 90.00 96.34 90.00 P 1 21 1 8
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 0.010966 0.000000 0.001217 0.00000
SCALE2 0.000000 0.006828 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008950 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
