HEADER TRANSFERASE/INHIBITOR 14-JUN-12 4FLH
TITLE CRYSTAL STRUCTURE OF HUMAN PI3K-GAMMA IN COMPLEX WITH AMG511
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC
COMPND 3 SUBUNIT GAMMA ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 144-1102;
COMPND 6 SYNONYM: PI3-KINASE SUBUNIT GAMMA, PI3K-GAMMA, PI3KGAMMA, PTDINS-3-
COMPND 7 KINASE SUBUNIT GAMMA, PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE
COMPND 8 110 KDA CATALYTIC SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110-GAMMA,
COMPND 9 P110GAMMA, PHOSPHOINOSITIDE-3-KINASE CATALYTIC GAMMA POLYPEPTIDE,
COMPND 10 SERINE/THREONINE PROTEIN KINASE PIK3CG, P120-PI3K;
COMPND 11 EC: 2.7.1.153, 2.7.11.1;
COMPND 12 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: PIK3CG;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS P110, PHOSPHOTRANSFERASE, CANCER, P85, PHOSPHORYLATION, TRANSFERASE-
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,J.TANG,P.YAKOWEC
REVDAT 4 28-FEB-24 4FLH 1 REMARK SEQADV
REVDAT 3 15-NOV-17 4FLH 1 REMARK
REVDAT 2 03-OCT-12 4FLH 1 JRNL
REVDAT 1 29-AUG-12 4FLH 0
JRNL AUTH M.H.NORMAN,K.L.ANDREWS,Y.Y.BO,S.K.BOOKER,S.CAENEPEEL,
JRNL AUTH 2 V.J.CEE,N.D.D'ANGELO,D.J.FREEMAN,B.J.HERBERICH,F.T.HONG,
JRNL AUTH 3 C.L.JACKSON,J.JIANG,B.A.LANMAN,L.LIU,J.D.MCCARTER,
JRNL AUTH 4 E.L.MULLADY,N.NISHIMURA,L.H.PETTUS,A.B.REED,T.S.MIGUEL,
JRNL AUTH 5 A.L.SMITH,M.M.STEC,S.TADESSE,A.TASKER,D.AIDASANI,X.ZHU,
JRNL AUTH 6 R.SUBRAMANIAN,N.A.TAMAYO,L.WANG,D.A.WHITTINGTON,B.WU,T.WU,
JRNL AUTH 7 R.P.WURZ,K.YANG,L.ZALAMEDA,N.ZHANG,P.E.HUGHES
JRNL TITL SELECTIVE CLASS I PHOSPHOINOSITIDE 3-KINASE INHIBITORS:
JRNL TITL 2 OPTIMIZATION OF A SERIES OF PYRIDYLTRIAZINES LEADING TO THE
JRNL TITL 3 IDENTIFICATION OF A CLINICAL CANDIDATE, AMG 511.
JRNL REF J.MED.CHEM. V. 55 7796 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22897589
JRNL DOI 10.1021/JM300846Z
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 32236
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1635
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2146
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6807
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 42
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.38000
REMARK 3 B22 (A**2) : 1.93000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.54000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.805
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.307
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.255
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.633
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7007 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4779 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9485 ; 1.080 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11650 ; 0.814 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 830 ; 5.676 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 325 ;36.392 ;24.338
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1266 ;15.314 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;16.979 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1072 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7571 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1396 ; 0.001 ; 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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
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 145 A 249
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7804 -14.2015 28.1223
REMARK 3 T TENSOR
REMARK 3 T11: 0.1383 T22: 0.1251
REMARK 3 T33: 0.6255 T12: -0.0249
REMARK 3 T13: -0.0089 T23: 0.1119
REMARK 3 L TENSOR
REMARK 3 L11: 3.6025 L22: 0.6972
REMARK 3 L33: 1.7418 L12: -0.8597
REMARK 3 L13: 0.6724 L23: -0.4138
REMARK 3 S TENSOR
REMARK 3 S11: 0.2463 S12: -0.0849 S13: -1.2647
REMARK 3 S21: -0.0612 S22: 0.1710 S23: 0.5448
REMARK 3 S31: 0.1344 S32: -0.2242 S33: -0.4173
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 269 A 321
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0139 -12.3975 31.5952
REMARK 3 T TENSOR
REMARK 3 T11: 0.1652 T22: 0.4784
REMARK 3 T33: 0.7690 T12: 0.0613
REMARK 3 T13: 0.1158 T23: 0.4144
REMARK 3 L TENSOR
REMARK 3 L11: 2.4496 L22: 2.7118
REMARK 3 L33: 2.6420 L12: -1.8528
REMARK 3 L13: 1.9047 L23: -0.3708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: -0.9135 S13: -1.1696
REMARK 3 S21: -0.1559 S22: 0.8181 S23: 0.8561
REMARK 3 S31: -0.3196 S32: -0.8428 S33: -0.8948
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 : A 352 A 436
REMARK 3 ORIGIN FOR THE GROUP (A): 67.3318 -5.5880 14.9866
REMARK 3 T TENSOR
REMARK 3 T11: 0.1576 T22: 0.7061
REMARK 3 T33: 0.1759 T12: 0.0228
REMARK 3 T13: 0.0360 T23: -0.1067
REMARK 3 L TENSOR
REMARK 3 L11: 1.0919 L22: 2.3112
REMARK 3 L33: 2.5535 L12: -0.1037
REMARK 3 L13: -0.3596 L23: -1.3270
REMARK 3 S TENSOR
REMARK 3 S11: 0.0653 S12: 0.4233 S13: -0.0084
REMARK 3 S21: 0.0613 S22: 0.0526 S23: -0.0788
REMARK 3 S31: -0.0638 S32: 0.5308 S33: -0.1179
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 : A 457 A 533
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2921 -8.5337 14.1221
REMARK 3 T TENSOR
REMARK 3 T11: 0.2748 T22: 0.9119
REMARK 3 T33: 0.1774 T12: 0.0324
REMARK 3 T13: 0.0627 T23: -0.1592
REMARK 3 L TENSOR
REMARK 3 L11: 1.6426 L22: 0.8887
REMARK 3 L33: 0.2205 L12: 0.4625
REMARK 3 L13: 0.1445 L23: 0.3737
REMARK 3 S TENSOR
REMARK 3 S11: -0.1018 S12: 0.9284 S13: -0.1593
REMARK 3 S21: 0.1592 S22: 0.1660 S23: -0.0056
REMARK 3 S31: 0.0471 S32: 0.1887 S33: -0.0643
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 : A 546 A 725
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4652 -10.0311 34.4150
REMARK 3 T TENSOR
REMARK 3 T11: 0.2974 T22: 0.2527
REMARK 3 T33: 0.3252 T12: 0.0480
REMARK 3 T13: 0.0161 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.9922 L22: 0.2786
REMARK 3 L33: 1.1575 L12: -0.2993
REMARK 3 L13: 1.4669 L23: -0.2068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0860 S12: 0.0215 S13: -0.4330
REMARK 3 S21: 0.0510 S22: 0.0597 S23: 0.1151
REMARK 3 S31: -0.0010 S32: 0.1053 S33: -0.1456
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 : A 726 A 885
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6992 5.3646 17.5422
REMARK 3 T TENSOR
REMARK 3 T11: 0.3000 T22: 0.3760
REMARK 3 T33: 0.2650 T12: 0.0704
REMARK 3 T13: 0.0371 T23: 0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 2.0293 L22: 1.1047
REMARK 3 L33: 0.7135 L12: -0.9628
REMARK 3 L13: 0.9330 L23: -0.5970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0321 S12: 0.3118 S13: -0.1295
REMARK 3 S21: 0.0614 S22: 0.0833 S23: 0.2150
REMARK 3 S31: -0.2107 S32: -0.0450 S33: -0.1154
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 : A 886 A 1092
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0097 19.7868 37.6364
REMARK 3 T TENSOR
REMARK 3 T11: 0.6666 T22: 0.2503
REMARK 3 T33: 0.2941 T12: 0.2168
REMARK 3 T13: -0.1273 T23: -0.0693
REMARK 3 L TENSOR
REMARK 3 L11: 2.0386 L22: 1.5229
REMARK 3 L33: 0.7673 L12: -0.6639
REMARK 3 L13: 0.9108 L23: -0.8578
REMARK 3 S TENSOR
REMARK 3 S11: -0.6732 S12: -0.2428 S13: 0.4825
REMARK 3 S21: 0.6447 S22: 0.3124 S23: -0.2123
REMARK 3 S31: -0.4591 S32: -0.1067 S33: 0.3609
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FLH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000073047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32540
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.56100
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 3350, 200 MM AMMONIUM SULFATE,
REMARK 280 2 MM DTT, 100 MM TRIS, PH 7.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 72.52950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.90150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.52950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.90150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A1341 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 GLY A 143
REMARK 465 SER A 144
REMARK 465 LYS A 251
REMARK 465 MET A 252
REMARK 465 ALA A 253
REMARK 465 LYS A 254
REMARK 465 LYS A 255
REMARK 465 LYS A 256
REMARK 465 SER A 257
REMARK 465 LEU A 258
REMARK 465 MET A 259
REMARK 465 ASP A 260
REMARK 465 ILE A 261
REMARK 465 PRO A 262
REMARK 465 GLU A 263
REMARK 465 SER A 264
REMARK 465 GLN A 265
REMARK 465 SER A 266
REMARK 465 GLU A 267
REMARK 465 GLN A 268
REMARK 465 GLU A 322
REMARK 465 TRP A 323
REMARK 465 PRO A 324
REMARK 465 LEU A 325
REMARK 465 VAL A 326
REMARK 465 ASP A 327
REMARK 465 ASP A 328
REMARK 465 CYS A 329
REMARK 465 THR A 330
REMARK 465 GLY A 331
REMARK 465 VAL A 332
REMARK 465 THR A 333
REMARK 465 GLY A 334
REMARK 465 TYR A 335
REMARK 465 HIS A 336
REMARK 465 GLU A 337
REMARK 465 GLN A 338
REMARK 465 LEU A 339
REMARK 465 THR A 340
REMARK 465 ILE A 341
REMARK 465 HIS A 342
REMARK 465 GLY A 343
REMARK 465 LYS A 344
REMARK 465 ASP A 345
REMARK 465 HIS A 346
REMARK 465 GLU A 347
REMARK 465 SER A 348
REMARK 465 VAL A 349
REMARK 465 PHE A 350
REMARK 465 THR A 351
REMARK 465 PRO A 374
REMARK 465 ARG A 375
REMARK 465 ASN A 376
REMARK 465 THR A 377
REMARK 465 LYS A 437
REMARK 465 ALA A 438
REMARK 465 PRO A 439
REMARK 465 ALA A 440
REMARK 465 LEU A 441
REMARK 465 SER A 442
REMARK 465 SER A 443
REMARK 465 LYS A 444
REMARK 465 ALA A 445
REMARK 465 SER A 446
REMARK 465 ALA A 447
REMARK 465 GLU A 448
REMARK 465 SER A 449
REMARK 465 PRO A 450
REMARK 465 SER A 451
REMARK 465 SER A 452
REMARK 465 GLU A 453
REMARK 465 SER A 454
REMARK 465 LYS A 455
REMARK 465 GLY A 456
REMARK 465 GLY A 489
REMARK 465 LYS A 490
REMARK 465 GLY A 491
REMARK 465 GLU A 492
REMARK 465 ASP A 493
REMARK 465 GLN A 494
REMARK 465 GLY A 495
REMARK 465 ASN A 522
REMARK 465 TYR A 523
REMARK 465 CYS A 524
REMARK 465 HIS A 525
REMARK 465 PRO A 534
REMARK 465 THR A 535
REMARK 465 PRO A 536
REMARK 465 ASP A 537
REMARK 465 PRO A 538
REMARK 465 GLU A 539
REMARK 465 GLY A 540
REMARK 465 ASP A 541
REMARK 465 ARG A 542
REMARK 465 VAL A 543
REMARK 465 ARG A 544
REMARK 465 ALA A 545
REMARK 465 LYS A 756
REMARK 465 TYR A 757
REMARK 465 LEU A 969
REMARK 465 GLY A 970
REMARK 465 ASN A 971
REMARK 465 TYR A 972
REMARK 465 LYS A 973
REMARK 465 SER A 974
REMARK 465 PHE A 975
REMARK 465 LEU A 976
REMARK 465 GLY A 977
REMARK 465 ILE A 978
REMARK 465 ASN A 979
REMARK 465 GLY A 1093
REMARK 465 ILE A 1094
REMARK 465 LYS A 1095
REMARK 465 GLN A 1096
REMARK 465 GLY A 1097
REMARK 465 GLU A 1098
REMARK 465 LYS A 1099
REMARK 465 HIS A 1100
REMARK 465 SER A 1101
REMARK 465 ALA A 1102
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 457 CG CD CE NZ
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 HIS A 199 53.66 37.38
REMARK 500 ASN A 217 73.02 54.50
REMARK 500 ARG A 226 -100.86 -139.80
REMARK 500 THR A 228 -58.39 -145.08
REMARK 500 ASP A 470 -169.57 -78.04
REMARK 500 PHE A 473 15.18 57.48
REMARK 500 ARG A 579 -65.29 -25.77
REMARK 500 ARG A 613 53.15 -97.69
REMARK 500 ARG A 614 52.79 -103.09
REMARK 500 ALA A 797 80.00 -103.64
REMARK 500 LEU A 823 51.33 -107.53
REMARK 500 CYS A 869 118.31 -160.82
REMARK 500 ASP A 964 75.63 53.25
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 SO4 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 14K A 1205
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F1S RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH SIMILAR COMPOUND
REMARK 900 RELATED ID: 4DK5 RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH SIMILAR COMPOUND
REMARK 900 RELATED ID: 4FJY RELATED DB: PDB
REMARK 900 RELATED ID: 4FJZ RELATED DB: PDB
DBREF 4FLH A 144 1102 UNP P48736 PK3CG_HUMAN 144 1102
SEQADV 4FLH GLY A 143 UNP P48736 EXPRESSION TAG
SEQRES 1 A 960 GLY SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR
SEQRES 2 A 960 ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL
SEQRES 3 A 960 HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL
SEQRES 4 A 960 THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS
SEQRES 5 A 960 LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU
SEQRES 6 A 960 PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE
SEQRES 7 A 960 PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE
SEQRES 8 A 960 LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN
SEQRES 9 A 960 SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET
SEQRES 10 A 960 ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU
SEQRES 11 A 960 ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR
SEQRES 12 A 960 PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS
SEQRES 13 A 960 ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO
SEQRES 14 A 960 ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO
SEQRES 15 A 960 LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU
SEQRES 16 A 960 GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE
SEQRES 17 A 960 THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL
SEQRES 18 A 960 LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN
SEQRES 19 A 960 THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS
SEQRES 20 A 960 GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS
SEQRES 21 A 960 PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU
SEQRES 22 A 960 PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU
SEQRES 23 A 960 LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU
SEQRES 24 A 960 SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER
SEQRES 25 A 960 LYS GLY LYS VAL GLN LEU LEU TYR TYR VAL ASN LEU LEU
SEQRES 26 A 960 LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR
SEQRES 27 A 960 VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP
SEQRES 28 A 960 GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR
SEQRES 29 A 960 ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU
SEQRES 30 A 960 LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS
SEQRES 31 A 960 GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA
SEQRES 32 A 960 GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE
SEQRES 33 A 960 ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP
SEQRES 34 A 960 LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS
SEQRES 35 A 960 HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS
SEQRES 36 A 960 TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU
SEQRES 37 A 960 LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP
SEQRES 38 A 960 VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER
SEQRES 39 A 960 ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU
SEQRES 40 A 960 SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN
SEQRES 41 A 960 LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER
SEQRES 42 A 960 ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN
SEQRES 43 A 960 LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER
SEQRES 44 A 960 GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA
SEQRES 45 A 960 VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA
SEQRES 46 A 960 MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU
SEQRES 47 A 960 MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER
SEQRES 48 A 960 ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN
SEQRES 49 A 960 LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU
SEQRES 50 A 960 PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS
SEQRES 51 A 960 ALA GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA
SEQRES 52 A 960 SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA
SEQRES 53 A 960 ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE
SEQRES 54 A 960 PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE
SEQRES 55 A 960 LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR
SEQRES 56 A 960 GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE
SEQRES 57 A 960 SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS
SEQRES 58 A 960 ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL
SEQRES 59 A 960 GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS
SEQRES 60 A 960 TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN
SEQRES 61 A 960 ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR
SEQRES 62 A 960 CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS
SEQRES 63 A 960 ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE
SEQRES 64 A 960 HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER
SEQRES 65 A 960 PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU
SEQRES 66 A 960 THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS
SEQRES 67 A 960 LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS
SEQRES 68 A 960 VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU
SEQRES 69 A 960 LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET
SEQRES 70 A 960 PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG
SEQRES 71 A 960 ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS
SEQRES 72 A 960 LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS
SEQRES 73 A 960 GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL
SEQRES 74 A 960 LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA
HET SO4 A1201 5
HET SO4 A1202 5
HET SO4 A1203 5
HET SO4 A1204 5
HET 14K A1205 36
HETNAM SO4 SULFATE ION
HETNAM 14K 4-(2-[(5-FLUORO-6-METHOXYPYRIDIN-3-YL)AMINO]-5-{(1R)-1-
HETNAM 2 14K [4-(METHYLSULFONYL)PIPERAZIN-1-YL]ETHYL}PYRIDIN-3-YL)-
HETNAM 3 14K 6-METHYL-1,3,5-TRIAZIN-2-AMINE
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 14K C22 H28 F N9 O3 S
FORMUL 7 HOH *42(H2 O)
HELIX 1 1 GLU A 145 GLY A 159 1 15
HELIX 2 2 ASP A 171 LEU A 180 1 10
HELIX 3 3 LEU A 180 ARG A 191 1 12
HELIX 4 4 ASP A 192 HIS A 199 1 8
HELIX 5 5 PRO A 208 LYS A 213 1 6
HELIX 6 6 THR A 240 THR A 250 1 11
HELIX 7 7 PRO A 286 ASN A 289 5 4
HELIX 8 8 PHE A 290 ASN A 299 1 10
HELIX 9 9 ASP A 312 GLU A 317 5 6
HELIX 10 10 SER A 353 CYS A 357 5 5
HELIX 11 11 LYS A 421 LEU A 423 5 3
HELIX 12 12 ASN A 498 THR A 503 5 6
HELIX 13 13 PRO A 548 THR A 561 1 14
HELIX 14 14 THR A 568 PHE A 578 1 11
HELIX 15 15 PHE A 578 LEU A 583 1 6
HELIX 16 16 LYS A 584 LYS A 587 5 4
HELIX 17 17 ALA A 588 SER A 594 1 7
HELIX 18 18 GLN A 600 ARG A 613 1 14
HELIX 19 19 ARG A 614 SER A 620 1 7
HELIX 20 20 ASP A 623 LEU A 630 1 8
HELIX 21 21 ASP A 637 GLU A 649 1 13
HELIX 22 22 GLU A 652 VAL A 667 1 16
HELIX 23 23 LYS A 668 GLU A 670 5 3
HELIX 24 24 SER A 675 ARG A 687 1 13
HELIX 25 25 ASN A 688 SER A 706 1 19
HELIX 26 26 TYR A 709 ARG A 722 1 14
HELIX 27 27 GLY A 725 SER A 753 1 29
HELIX 28 28 SER A 760 SER A 777 1 18
HELIX 29 29 ILE A 798 CYS A 801 5 4
HELIX 30 30 LEU A 838 GLU A 858 1 21
HELIX 31 31 ILE A 888 VAL A 896 1 9
HELIX 32 32 GLU A 905 SER A 915 1 11
HELIX 33 33 THR A 917 GLY A 943 1 27
HELIX 34 34 THR A 988 GLY A 996 1 9
HELIX 35 35 SER A 1003 HIS A 1022 1 20
HELIX 36 36 HIS A 1023 MET A 1039 1 17
HELIX 37 37 SER A 1044 GLU A 1049 1 6
HELIX 38 38 GLU A 1049 LEU A 1055 1 7
HELIX 39 39 ASN A 1060 GLY A 1079 1 20
HELIX 40 40 TRP A 1080 VAL A 1091 1 12
SHEET 1 A 4 GLN A 231 VAL A 235 0
SHEET 2 A 4 ILE A 220 HIS A 225 -1 N ILE A 224 O GLN A 231
SHEET 3 A 4 ILE A 303 ASP A 308 1 O VAL A 305 N VAL A 223
SHEET 4 A 4 VAL A 271 VAL A 274 -1 N VAL A 271 O ASP A 308
SHEET 1 B 4 GLU A 407 LYS A 419 0
SHEET 2 B 4 LYS A 360 ASP A 369 -1 N PHE A 361 O PHE A 416
SHEET 3 B 4 SER A 515 LEU A 520 -1 O SER A 517 N ARG A 366
SHEET 4 B 4 GLY A 478 HIS A 483 -1 N GLY A 478 O LEU A 520
SHEET 1 C 3 GLN A 392 ARG A 398 0
SHEET 2 C 3 THR A 380 HIS A 389 -1 N ILE A 387 O LEU A 394
SHEET 3 C 3 LYS A 402 PRO A 403 -1 O LYS A 402 N VAL A 381
SHEET 1 D 5 GLN A 392 ARG A 398 0
SHEET 2 D 5 THR A 380 HIS A 389 -1 N ILE A 387 O LEU A 394
SHEET 3 D 5 LEU A 428 GLY A 436 -1 O ASN A 430 N ASN A 386
SHEET 4 D 5 GLN A 459 LEU A 467 -1 O LEU A 466 N LEU A 429
SHEET 5 D 5 TRP A 485 GLN A 486 -1 O TRP A 485 N TYR A 463
SHEET 1 E 4 PHE A 783 VAL A 785 0
SHEET 2 E 4 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 E 4 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 E 4 LYS A 802 VAL A 803 -1 N LYS A 802 O TRP A 812
SHEET 1 F 6 PHE A 783 VAL A 785 0
SHEET 2 F 6 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 F 6 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 F 6 ILE A 828 HIS A 834 -1 O ILE A 828 N PHE A 815
SHEET 5 F 6 ILE A 876 GLU A 880 -1 O ILE A 879 N ILE A 831
SHEET 6 F 6 CYS A 869 GLY A 873 -1 N ILE A 870 O MET A 878
SHEET 1 G 3 ALA A 885 THR A 887 0
SHEET 2 G 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 G 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
CISPEP 1 SER A 777 GLN A 778 0 9.34
SITE 1 AC1 5 PRO A 206 LEU A 207 TRP A 212 LYS A 288
SITE 2 AC1 5 LYS A1066
SITE 1 AC2 3 TRP A 576 ARG A 579 LYS A 606
SITE 1 AC3 5 LEU A 657 PHE A 694 PHE A 698 GLN A 846
SITE 2 AC3 5 ARG A 849
SITE 1 AC4 5 ARG A 947 HIS A 948 ASN A 951 TRP A1086
SITE 2 AC4 5 LEU A1090
SITE 1 AC5 16 LYS A 802 MET A 804 ALA A 805 ILE A 831
SITE 2 AC5 16 LYS A 833 ASP A 841 TYR A 867 GLU A 880
SITE 3 AC5 16 ILE A 881 VAL A 882 THR A 887 MET A 953
SITE 4 AC5 16 ILE A 963 ASP A 964 HOH A1318 HOH A1320
CRYST1 145.059 67.803 107.523 90.00 95.27 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006894 0.000000 0.000636 0.00000
SCALE2 0.000000 0.014749 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009340 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
