HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-AUG-16 5SXD
TITLE CRYSTAL STRUCTURE OF PI3KALPHA IN COMPLEX WITH FRAGMENT 22
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC
COMPND 3 SUBUNIT ALPHA ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PTDINS-3-KINASE SUBUNIT ALPHA,PHOSPHATIDYLINOSITOL 4,5-
COMPND 6 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT ALPHA,P110ALPHA,
COMPND 7 PHOSPHOINOSITIDE-3-KINASE CATALYTIC ALPHA POLYPEPTIDE,
COMPND 8 SERINE/THREONINE PROTEIN KINASE PIK3CA;
COMPND 9 EC: 2.7.1.153,2.7.11.1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;
COMPND 13 CHAIN: B;
COMPND 14 FRAGMENT: RESIDUES 322-600;
COMPND 15 SYNONYM: PTDINS-3-KINASE REGULATORY SUBUNIT ALPHA,
COMPND 16 PHOSPHATIDYLINOSITOL 3-KINASE 85 KDA REGULATORY SUBUNIT ALPHA,PTDINS-
COMPND 17 3-KINASE REGULATORY SUBUNIT P85-ALPHA;
COMPND 18 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: PIK3CA;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT-A;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: PIK3R1, GRB1;
SOURCE 17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT-A
KEYWDS LIPID KINASE, PHOSPHOINOSITIDE, 3-KINASE, SIGNALING, TRANSFERASE,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.B.GABELLI,B.VOGELSTEIN,M.S.MILLER,L.M.AMZEL
REVDAT 4 04-OCT-23 5SXD 1 REMARK
REVDAT 3 04-DEC-19 5SXD 1 REMARK
REVDAT 2 20-SEP-17 5SXD 1 REMARK
REVDAT 1 15-FEB-17 5SXD 0
JRNL AUTH M.S.MILLER,S.MAHESHWARI,F.M.MCROBB,K.W.KINZLER,L.M.AMZEL,
JRNL AUTH 2 B.VOGELSTEIN,S.B.GABELLI
JRNL TITL IDENTIFICATION OF ALLOSTERIC BINDING SITES FOR PI3K ALPHA
JRNL TITL 2 ONCOGENIC MUTANT SPECIFIC INHIBITOR DESIGN.
JRNL REF BIOORG. MED. CHEM. V. 25 1481 2017
JRNL REFN ESSN 1464-3391
JRNL PMID 28129991
JRNL DOI 10.1016/J.BMC.2017.01.012
REMARK 2
REMARK 2 RESOLUTION. 3.50 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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 24555
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1331
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) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1716
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10683
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 137.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.69000
REMARK 3 B22 (A**2) : 0.44000
REMARK 3 B33 (A**2) : -3.14000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.651
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.470
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.964
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10920 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10496 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14722 ; 1.519 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24166 ; 1.001 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1281 ; 7.377 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 546 ;37.962 ;24.194
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2051 ;19.017 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 76 ;16.262 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1592 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12115 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2547 ; 0.002 ; 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): 5166 ; 9.023 ;13.418
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5165 ; 9.010 ;13.417
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6433 ;14.104 ;20.086
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 : NULL
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 : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5SXD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223288.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-14
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 : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25936
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 91.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.88300
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: REFMAC
REMARK 200 STARTING MODEL: 4OVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAFORMATE, PH 7.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 57.43650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.98650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.22100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.98650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.43650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.22100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 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 MET A -27
REMARK 465 GLU A -10
REMARK 465 ASN A -9
REMARK 465 LEU A -8
REMARK 465 TYR A -7
REMARK 465 PHE A -6
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 ARG A 309
REMARK 465 ARG A 310
REMARK 465 ILE A 311
REMARK 465 SER A 312
REMARK 465 THR A 313
REMARK 465 ALA A 314
REMARK 465 THR A 315
REMARK 465 PRO A 316
REMARK 465 TYR A 317
REMARK 465 MET A 318
REMARK 465 ASN A 319
REMARK 465 GLY A 320
REMARK 465 GLU A 321
REMARK 465 LYS A 410
REMARK 465 GLY A 411
REMARK 465 ARG A 412
REMARK 465 LYS A 413
REMARK 465 GLY A 414
REMARK 465 ALA A 415
REMARK 465 LYS A 416
REMARK 465 GLU A 417
REMARK 465 GLU A 418
REMARK 465 TYR A 947
REMARK 465 MET A 1055
REMARK 465 ASP A 1056
REMARK 465 TRP A 1057
REMARK 465 ILE A 1058
REMARK 465 PHE A 1059
REMARK 465 HIS A 1060
REMARK 465 THR A 1061
REMARK 465 ILE A 1062
REMARK 465 LYS A 1063
REMARK 465 GLN A 1064
REMARK 465 HIS A 1065
REMARK 465 ALA A 1066
REMARK 465 LEU A 1067
REMARK 465 ASN A 1068
REMARK 465 MET B 322
REMARK 465 ASN B 323
REMARK 465 ASN B 324
REMARK 465 ASN B 325
REMARK 465 MET B 326
REMARK 465 TRP B 335
REMARK 465 GLY B 336
REMARK 465 ASP B 337
REMARK 465 ILE B 338
REMARK 465 SER B 339
REMARK 465 ALA B 360
REMARK 465 SER B 361
REMARK 465 ARG B 386
REMARK 465 ASP B 387
REMARK 465 GLY B 391
REMARK 465 PHE B 392
REMARK 465 SER B 393
REMARK 465 ASP B 394
REMARK 465 PRO B 395
REMARK 465 LYS B 419
REMARK 465 LEU B 420
REMARK 465 ASP B 421
REMARK 465 SER B 429
REMARK 465 LYS B 430
REMARK 465 TYR B 431
REMARK 465 GLN B 432
REMARK 465 GLN B 433
REMARK 465 ASP B 434
REMARK 465 LYS B 587
REMARK 465 GLY B 588
REMARK 465 VAL B 589
REMARK 465 ARG B 590
REMARK 465 GLN B 591
REMARK 465 GLY B 599
REMARK 465 ASN B 600
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 PRO A -13 84.16 -57.30
REMARK 500 MET A 1 75.23 66.78
REMARK 500 PRO A 3 -106.45 -78.62
REMARK 500 ARG A 4 164.76 67.37
REMARK 500 ARG A 38 -45.36 -23.66
REMARK 500 ALA A 77 26.86 80.48
REMARK 500 ARG A 93 71.76 61.76
REMARK 500 PHE A 95 -75.15 68.52
REMARK 500 ASN A 107 -35.35 -14.16
REMARK 500 ARG A 108 81.56 -64.29
REMARK 500 LEU A 113 57.96 -102.67
REMARK 500 MET A 130 44.98 -102.54
REMARK 500 ASP A 133 121.71 -20.95
REMARK 500 VAL A 198 -75.11 -120.99
REMARK 500 ASN A 201 -61.60 175.06
REMARK 500 ASN A 202 -62.00 -23.01
REMARK 500 ASP A 214 43.41 -88.63
REMARK 500 ARG A 226 -70.58 -49.09
REMARK 500 ASP A 258 58.48 -91.45
REMARK 500 LYS A 264 97.35 -61.74
REMARK 500 TYR A 294 -9.19 -57.40
REMARK 500 TYR A 307 65.33 -65.76
REMARK 500 SER A 326 138.06 -38.98
REMARK 500 ASN A 331 77.46 -115.40
REMARK 500 LEU A 339 -99.01 -124.98
REMARK 500 THR A 342 -52.69 -120.98
REMARK 500 TYR A 343 42.20 -107.96
REMARK 500 ASP A 352 -70.83 -65.39
REMARK 500 HIS A 362 44.44 -150.37
REMARK 500 VAL A 376 52.25 28.21
REMARK 500 CYS A 378 -74.84 70.70
REMARK 500 SER A 379 86.50 -58.24
REMARK 500 ASN A 380 82.20 60.39
REMARK 500 ASN A 384 77.54 -112.04
REMARK 500 HIS A 450 -72.22 -41.88
REMARK 500 LEU A 456 -36.23 -130.05
REMARK 500 ASN A 457 73.43 65.00
REMARK 500 GLU A 469 70.54 -69.67
REMARK 500 PRO A 471 96.67 -48.54
REMARK 500 PHE A 480 48.52 -102.75
REMARK 500 SER A 481 -0.89 57.92
REMARK 500 TYR A 508 -119.54 41.13
REMARK 500 SER A 514 -64.68 36.43
REMARK 500 ALA A 518 -15.96 76.06
REMARK 500 ASP A 520 -158.71 81.81
REMARK 500 ILE A 561 72.19 -111.45
REMARK 500 LEU A 623 109.55 -50.91
REMARK 500 GLU A 722 -57.94 69.42
REMARK 500 ASN A 756 96.40 -169.92
REMARK 500 ASN A 763 97.75 45.62
REMARK 500
REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 113 ASN A 114 145.96
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 71F B 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5SW8 RELATED DB: PDB
REMARK 900 RELATED ID: 5SWG RELATED DB: PDB
REMARK 900 RELATED ID: 5SWO RELATED DB: PDB
REMARK 900 RELATED ID: 5SWP RELATED DB: PDB
REMARK 900 RELATED ID: 5SWR RELATED DB: PDB
REMARK 900 RELATED ID: 5SWT RELATED DB: PDB
REMARK 900 RELATED ID: 5SX8 RELATED DB: PDB
REMARK 900 RELATED ID: 5SX9 RELATED DB: PDB
REMARK 900 RELATED ID: 5SXA RELATED DB: PDB
REMARK 900 RELATED ID: 5SXB RELATED DB: PDB
REMARK 900 RELATED ID: 5SXC RELATED DB: PDB
REMARK 900 RELATED ID: 5SXE RELATED DB: PDB
REMARK 900 RELATED ID: 5SXF RELATED DB: PDB
REMARK 900 RELATED ID: 5SXI RELATED DB: PDB
REMARK 900 RELATED ID: 5SXJ RELATED DB: PDB
REMARK 900 RELATED ID: 5SXK RELATED DB: PDB
DBREF 5SXD A 1 1068 UNP P42336 PK3CA_HUMAN 1 1068
DBREF 5SXD B 322 600 UNP P27986 P85A_HUMAN 322 600
SEQADV 5SXD MET A -27 UNP P42336 INITIATING METHIONINE
SEQADV 5SXD SER A -26 UNP P42336 EXPRESSION TAG
SEQADV 5SXD TYR A -25 UNP P42336 EXPRESSION TAG
SEQADV 5SXD TYR A -24 UNP P42336 EXPRESSION TAG
SEQADV 5SXD HIS A -23 UNP P42336 EXPRESSION TAG
SEQADV 5SXD HIS A -22 UNP P42336 EXPRESSION TAG
SEQADV 5SXD HIS A -21 UNP P42336 EXPRESSION TAG
SEQADV 5SXD HIS A -20 UNP P42336 EXPRESSION TAG
SEQADV 5SXD HIS A -19 UNP P42336 EXPRESSION TAG
SEQADV 5SXD HIS A -18 UNP P42336 EXPRESSION TAG
SEQADV 5SXD ASP A -17 UNP P42336 EXPRESSION TAG
SEQADV 5SXD TYR A -16 UNP P42336 EXPRESSION TAG
SEQADV 5SXD ASP A -15 UNP P42336 EXPRESSION TAG
SEQADV 5SXD ILE A -14 UNP P42336 EXPRESSION TAG
SEQADV 5SXD PRO A -13 UNP P42336 EXPRESSION TAG
SEQADV 5SXD THR A -12 UNP P42336 EXPRESSION TAG
SEQADV 5SXD THR A -11 UNP P42336 EXPRESSION TAG
SEQADV 5SXD GLU A -10 UNP P42336 EXPRESSION TAG
SEQADV 5SXD ASN A -9 UNP P42336 EXPRESSION TAG
SEQADV 5SXD LEU A -8 UNP P42336 EXPRESSION TAG
SEQADV 5SXD TYR A -7 UNP P42336 EXPRESSION TAG
SEQADV 5SXD PHE A -6 UNP P42336 EXPRESSION TAG
SEQADV 5SXD GLN A -5 UNP P42336 EXPRESSION TAG
SEQADV 5SXD GLY A -4 UNP P42336 EXPRESSION TAG
SEQADV 5SXD ALA A -3 UNP P42336 EXPRESSION TAG
SEQADV 5SXD MET A -2 UNP P42336 EXPRESSION TAG
SEQADV 5SXD GLY A -1 UNP P42336 EXPRESSION TAG
SEQADV 5SXD SER A 0 UNP P42336 EXPRESSION TAG
SEQRES 1 A 1096 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 1096 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 1096 GLY SER MET PRO PRO ARG PRO SER SEP GLY GLU LEU TRP
SEQRES 4 A 1096 GLY ILE HIS LEU MET PRO PRO ARG ILE LEU VAL GLU CYS
SEQRES 5 A 1096 LEU LEU PRO ASN GLY MET ILE VAL THR LEU GLU CYS LEU
SEQRES 6 A 1096 ARG GLU ALA THR LEU ILE THR ILE LYS HIS GLU LEU PHE
SEQRES 7 A 1096 LYS GLU ALA ARG LYS TYR PRO LEU HIS GLN LEU LEU GLN
SEQRES 8 A 1096 ASP GLU SER SER TYR ILE PHE VAL SER VAL THR GLN GLU
SEQRES 9 A 1096 ALA GLU ARG GLU GLU PHE PHE ASP GLU THR ARG ARG LEU
SEQRES 10 A 1096 CYS ASP LEU ARG LEU PHE GLN PRO PHE LEU LYS VAL ILE
SEQRES 11 A 1096 GLU PRO VAL GLY ASN ARG GLU GLU LYS ILE LEU ASN ARG
SEQRES 12 A 1096 GLU ILE GLY PHE ALA ILE GLY MET PRO VAL CYS GLU PHE
SEQRES 13 A 1096 ASP MET VAL LYS ASP PRO GLU VAL GLN ASP PHE ARG ARG
SEQRES 14 A 1096 ASN ILE LEU ASN VAL CYS LYS GLU ALA VAL ASP LEU ARG
SEQRES 15 A 1096 ASP LEU ASN SER PRO HIS SER ARG ALA MET TYR VAL TYR
SEQRES 16 A 1096 PRO PRO ASN VAL GLU SER SER PRO GLU LEU PRO LYS HIS
SEQRES 17 A 1096 ILE TYR ASN LYS LEU ASP LYS GLY GLN ILE ILE VAL VAL
SEQRES 18 A 1096 ILE TRP VAL ILE VAL SER PRO ASN ASN ASP LYS GLN LYS
SEQRES 19 A 1096 TYR THR LEU LYS ILE ASN HIS ASP CYS VAL PRO GLU GLN
SEQRES 20 A 1096 VAL ILE ALA GLU ALA ILE ARG LYS LYS THR ARG SER MET
SEQRES 21 A 1096 LEU LEU SER SER GLU GLN LEU LYS LEU CYS VAL LEU GLU
SEQRES 22 A 1096 TYR GLN GLY LYS TYR ILE LEU LYS VAL CYS GLY CYS ASP
SEQRES 23 A 1096 GLU TYR PHE LEU GLU LYS TYR PRO LEU SER GLN TYR LYS
SEQRES 24 A 1096 TYR ILE ARG SER CYS ILE MET LEU GLY ARG MET PRO ASN
SEQRES 25 A 1096 LEU MET LEU MET ALA LYS GLU SER LEU TYR SER GLN LEU
SEQRES 26 A 1096 PRO MET ASP CYS PHE THR MET PRO SER TYR SER ARG ARG
SEQRES 27 A 1096 ILE SER THR ALA THR PRO TYR MET ASN GLY GLU THR SER
SEQRES 28 A 1096 THR LYS SER LEU TRP VAL ILE ASN SER ALA LEU ARG ILE
SEQRES 29 A 1096 LYS ILE LEU CYS ALA THR TYR VAL ASN VAL ASN ILE ARG
SEQRES 30 A 1096 ASP ILE ASP LYS ILE TYR VAL ARG THR GLY ILE TYR HIS
SEQRES 31 A 1096 GLY GLY GLU PRO LEU CYS ASP ASN VAL ASN THR GLN ARG
SEQRES 32 A 1096 VAL PRO CYS SER ASN PRO ARG TRP ASN GLU TRP LEU ASN
SEQRES 33 A 1096 TYR ASP ILE TYR ILE PRO ASP LEU PRO ARG ALA ALA ARG
SEQRES 34 A 1096 LEU CYS LEU SER ILE CYS SER VAL LYS GLY ARG LYS GLY
SEQRES 35 A 1096 ALA LYS GLU GLU HIS CYS PRO LEU ALA TRP GLY ASN ILE
SEQRES 36 A 1096 ASN LEU PHE ASP TYR THR ASP THR LEU VAL SER GLY LYS
SEQRES 37 A 1096 MET ALA LEU ASN LEU TRP PRO VAL PRO HIS GLY LEU GLU
SEQRES 38 A 1096 ASP LEU LEU ASN PRO ILE GLY VAL THR GLY SER ASN PRO
SEQRES 39 A 1096 ASN LYS GLU THR PRO CYS LEU GLU LEU GLU PHE ASP TRP
SEQRES 40 A 1096 PHE SER SER VAL VAL LYS PHE PRO ASP MET SER VAL ILE
SEQRES 41 A 1096 GLU GLU HIS ALA ASN TRP SER VAL SER ARG GLU ALA GLY
SEQRES 42 A 1096 PHE SER TYR SER HIS ALA GLY LEU SER ASN ARG LEU ALA
SEQRES 43 A 1096 ARG ASP ASN GLU LEU ARG GLU ASN ASP LYS GLU GLN LEU
SEQRES 44 A 1096 LYS ALA ILE SER THR ARG ASP PRO LEU SER GLU ILE THR
SEQRES 45 A 1096 GLU GLN GLU LYS ASP PHE LEU TRP SER HIS ARG HIS TYR
SEQRES 46 A 1096 CYS VAL THR ILE PRO GLU ILE LEU PRO LYS LEU LEU LEU
SEQRES 47 A 1096 SER VAL LYS TRP ASN SER ARG ASP GLU VAL ALA GLN MET
SEQRES 48 A 1096 TYR CYS LEU VAL LYS ASP TRP PRO PRO ILE LYS PRO GLU
SEQRES 49 A 1096 GLN ALA MET GLU LEU LEU ASP CYS ASN TYR PRO ASP PRO
SEQRES 50 A 1096 MET VAL ARG GLY PHE ALA VAL ARG CYS LEU GLU LYS TYR
SEQRES 51 A 1096 LEU THR ASP ASP LYS LEU SER GLN TYR LEU ILE GLN LEU
SEQRES 52 A 1096 VAL GLN VAL LEU LYS TYR GLU GLN TYR LEU ASP ASN LEU
SEQRES 53 A 1096 LEU VAL ARG PHE LEU LEU LYS LYS ALA LEU THR ASN GLN
SEQRES 54 A 1096 ARG ILE GLY HIS PHE PHE PHE TRP HIS LEU LYS SER GLU
SEQRES 55 A 1096 MET HIS ASN LYS THR VAL SER GLN ARG PHE GLY LEU LEU
SEQRES 56 A 1096 LEU GLU SER TYR CYS ARG ALA CYS GLY MET TYR LEU LYS
SEQRES 57 A 1096 HIS LEU ASN ARG GLN VAL GLU ALA MET GLU LYS LEU ILE
SEQRES 58 A 1096 ASN LEU THR ASP ILE LEU LYS GLN GLU LYS LYS ASP GLU
SEQRES 59 A 1096 THR GLN LYS VAL GLN MET LYS PHE LEU VAL GLU GLN MET
SEQRES 60 A 1096 ARG ARG PRO ASP PHE MET ASP ALA LEU GLN GLY PHE LEU
SEQRES 61 A 1096 SER PRO LEU ASN PRO ALA HIS GLN LEU GLY ASN LEU ARG
SEQRES 62 A 1096 LEU GLU GLU CYS ARG ILE MET SER SER ALA LYS ARG PRO
SEQRES 63 A 1096 LEU TRP LEU ASN TRP GLU ASN PRO ASP ILE MET SEP GLU
SEQRES 64 A 1096 LEU LEU PHE GLN ASN ASN GLU ILE ILE PHE LYS ASN GLY
SEQRES 65 A 1096 ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN ILE ILE
SEQRES 66 A 1096 ARG ILE MET GLU ASN ILE TRP GLN ASN GLN GLY LEU ASP
SEQRES 67 A 1096 LEU ARG MET LEU PRO TYR GLY CYS LEU SER ILE GLY ASP
SEQRES 68 A 1096 CYS VAL GLY LEU ILE GLU VAL VAL ARG ASN SER HIS THR
SEQRES 69 A 1096 ILE MET GLN ILE GLN CYS LYS GLY GLY LEU LYS GLY ALA
SEQRES 70 A 1096 LEU GLN PHE ASN SER HIS THR LEU HIS GLN TRP LEU LYS
SEQRES 71 A 1096 ASP LYS ASN LYS GLY GLU ILE TYR ASP ALA ALA ILE ASP
SEQRES 72 A 1096 LEU PHE THR ARG SER CYS ALA GLY TYR CYS VAL ALA THR
SEQRES 73 A 1096 PHE ILE LEU GLY ILE GLY ASP ARG HIS ASN SER ASN ILE
SEQRES 74 A 1096 MET VAL LYS ASP ASP GLY GLN LEU PHE HIS ILE ASP PHE
SEQRES 75 A 1096 GLY HIS PHE LEU ASP HIS LYS LYS LYS LYS PHE GLY TYR
SEQRES 76 A 1096 LYS ARG GLU ARG VAL PRO PHE VAL LEU THR GLN ASP PHE
SEQRES 77 A 1096 LEU ILE VAL ILE SER LYS GLY ALA GLN GLU CYS THR LYS
SEQRES 78 A 1096 THR ARG GLU PHE GLU ARG PHE GLN GLU MET CYS TYR LYS
SEQRES 79 A 1096 ALA TYR LEU ALA ILE ARG GLN HIS ALA ASN LEU PHE ILE
SEQRES 80 A 1096 ASN LEU PHE SER MET MET LEU GLY SER GLY MET PRO GLU
SEQRES 81 A 1096 LEU GLN SER PHE ASP ASP ILE ALA TYR ILE ARG LYS THR
SEQRES 82 A 1096 LEU ALA LEU ASP LYS THR GLU GLN GLU ALA LEU GLU TYR
SEQRES 83 A 1096 PHE MET LYS GLN MET ASN ASP ALA HIS HIS GLY GLY TRP
SEQRES 84 A 1096 THR THR LYS MET ASP TRP ILE PHE HIS THR ILE LYS GLN
SEQRES 85 A 1096 HIS ALA LEU ASN
SEQRES 1 B 279 MET ASN ASN ASN MET SER LEU GLN ASP ALA GLU TRP TYR
SEQRES 2 B 279 TRP GLY ASP ILE SER ARG GLU GLU VAL ASN GLU LYS LEU
SEQRES 3 B 279 ARG ASP THR ALA ASP GLY THR PHE LEU VAL ARG ASP ALA
SEQRES 4 B 279 SER THR LYS MET HIS GLY ASP TYR THR LEU THR LEU ARG
SEQRES 5 B 279 LYS GLY GLY ASN ASN LYS LEU ILE LYS ILE PHE HIS ARG
SEQRES 6 B 279 ASP GLY LYS TYR GLY PHE SER ASP PRO LEU THR PHE SER
SEQRES 7 B 279 SER VAL VAL GLU LEU ILE ASN HIS TYR ARG ASN GLU SER
SEQRES 8 B 279 LEU ALA GLN TYR ASN PRO LYS LEU ASP VAL LYS LEU LEU
SEQRES 9 B 279 TYR PRO VAL SER LYS TYR GLN GLN ASP GLN VAL VAL LYS
SEQRES 10 B 279 GLU ASP ASN ILE GLU ALA VAL GLY LYS LYS LEU HIS GLU
SEQRES 11 B 279 TYR ASN THR GLN PHE GLN GLU LYS SER ARG GLU TYR ASP
SEQRES 12 B 279 ARG LEU TYR GLU GLU TYR THR ARG THR SER GLN GLU ILE
SEQRES 13 B 279 GLN MET LYS ARG THR ALA ILE GLU ALA PHE ASN GLU THR
SEQRES 14 B 279 ILE LYS ILE PHE GLU GLU GLN CYS GLN THR GLN GLU ARG
SEQRES 15 B 279 TYR SER LYS GLU TYR ILE GLU LYS PHE LYS ARG GLU GLY
SEQRES 16 B 279 ASN GLU LYS GLU ILE GLN ARG ILE MET HIS ASN TYR ASP
SEQRES 17 B 279 LYS LEU LYS SER ARG ILE SER GLU ILE ILE ASP SER ARG
SEQRES 18 B 279 ARG ARG LEU GLU GLU ASP LEU LYS LYS GLN ALA ALA GLU
SEQRES 19 B 279 TYR ARG GLU ILE ASP LYS ARG MET ASN SER ILE LYS PRO
SEQRES 20 B 279 ASP LEU ILE GLN LEU ARG LYS THR ARG ASP GLN TYR LEU
SEQRES 21 B 279 MET TRP LEU THR GLN LYS GLY VAL ARG GLN LYS LYS LEU
SEQRES 22 B 279 ASN GLU TRP LEU GLY ASN
MODRES 5SXD SEP A 7 SER MODIFIED RESIDUE
MODRES 5SXD SEP A 790 SER MODIFIED RESIDUE
HET SEP A 7 10
HET SEP A 790 10
HET 71F B 701 11
HETNAM SEP PHOSPHOSERINE
HETNAM 71F 2-METHOXYBENZOIC ACID
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 71F C8 H8 O3
HELIX 1 AA1 THR A 41 ALA A 53 1 13
HELIX 2 AA2 LEU A 58 LEU A 62 5 5
HELIX 3 AA3 ASP A 64 TYR A 68 5 5
HELIX 4 AA4 ARG A 88 ARG A 93 5 6
HELIX 5 AA5 GLU A 109 LEU A 113 5 5
HELIX 6 AA6 ASN A 114 GLY A 122 1 9
HELIX 7 AA7 VAL A 125 MET A 130 1 6
HELIX 8 AA8 ASP A 133 ASP A 155 1 23
HELIX 9 AA9 PRO A 159 TYR A 167 1 9
HELIX 10 AB1 PRO A 178 ASN A 183 1 6
HELIX 11 AB2 VAL A 216 ARG A 230 1 15
HELIX 12 AB3 SER A 235 GLY A 248 1 14
HELIX 13 AB4 PRO A 266 GLN A 269 5 4
HELIX 14 AB5 TYR A 270 LEU A 279 1 10
HELIX 15 AB6 LYS A 290 LEU A 297 1 8
HELIX 16 AB7 TRP A 328 ILE A 330 5 3
HELIX 17 AB8 PRO A 394 LEU A 396 5 3
HELIX 18 AB9 ASP A 488 GLY A 505 1 18
HELIX 19 AC1 ARG A 524 ARG A 537 1 14
HELIX 20 AC2 THR A 544 HIS A 554 1 11
HELIX 21 AC3 ARG A 555 GLU A 563 5 9
HELIX 22 AC4 ILE A 564 LEU A 570 1 7
HELIX 23 AC5 SER A 576 ASP A 589 1 14
HELIX 24 AC6 LYS A 594 MET A 599 1 6
HELIX 25 AC7 GLU A 600 ASP A 603 5 4
HELIX 26 AC8 ASP A 608 TYR A 622 1 15
HELIX 27 AC9 THR A 624 TYR A 631 1 8
HELIX 28 AD1 TYR A 631 LEU A 639 1 9
HELIX 29 AD2 LYS A 640 GLU A 642 5 3
HELIX 30 AD3 ASN A 647 ASN A 660 1 14
HELIX 31 AD4 ASN A 660 GLU A 674 1 15
HELIX 32 AD5 VAL A 680 CYS A 695 1 16
HELIX 33 AD6 MET A 697 LYS A 720 1 24
HELIX 34 AD7 THR A 727 ARG A 741 1 15
HELIX 35 AD8 ARG A 741 GLY A 750 1 10
HELIX 36 AD9 MET A 789 PHE A 794 1 6
HELIX 37 AE1 LEU A 807 ASN A 826 1 20
HELIX 38 AE2 ILE A 857 GLY A 865 1 9
HELIX 39 AE3 HIS A 875 ASP A 883 1 9
HELIX 40 AE4 GLY A 887 GLY A 912 1 26
HELIX 41 AE5 HIS A 940 LYS A 944 5 5
HELIX 42 AE6 THR A 957 SER A 965 1 9
HELIX 43 AE7 GLU A 970 LYS A 973 5 4
HELIX 44 AE8 THR A 974 GLN A 993 1 20
HELIX 45 AE9 HIS A 994 MET A 1005 1 12
HELIX 46 AF1 MET A 1010 GLN A 1014 5 5
HELIX 47 AF2 SER A 1015 ALA A 1027 1 13
HELIX 48 AF3 THR A 1031 HIS A 1048 1 18
HELIX 49 AF4 GLU B 341 ARG B 348 1 8
HELIX 50 AF5 SER B 400 GLU B 411 1 12
HELIX 51 AF6 GLN B 435 GLU B 439 5 5
HELIX 52 AF7 ILE B 442 LYS B 506 1 65
HELIX 53 AF8 ASN B 517 THR B 585 1 69
SHEET 1 AA1 5 ILE A 31 LEU A 37 0
SHEET 2 AA1 5 ARG A 19 LEU A 25 -1 N VAL A 22 O LEU A 34
SHEET 3 AA1 5 PHE A 98 ILE A 102 1 O VAL A 101 N LEU A 25
SHEET 4 AA1 5 ILE A 69 VAL A 73 -1 N VAL A 71 O LYS A 100
SHEET 5 AA1 5 ARG A 79 PHE A 82 -1 O PHE A 82 N PHE A 70
SHEET 1 AA2 2 GLN A 189 ILE A 191 0
SHEET 2 AA2 2 LYS A 210 ASN A 212 -1 O ILE A 211 N ILE A 190
SHEET 1 AA3 5 LYS A 204 TYR A 207 0
SHEET 2 AA3 5 ILE A 194 ILE A 197 -1 N ILE A 194 O TYR A 207
SHEET 3 AA3 5 LEU A 285 ALA A 289 1 O LEU A 287 N TRP A 195
SHEET 4 AA3 5 TYR A 250 VAL A 254 -1 N ILE A 251 O MET A 288
SHEET 5 AA3 5 CYS A 257 PHE A 261 -1 O PHE A 261 N LEU A 252
SHEET 1 AA4 2 LYS A 325 SER A 326 0
SHEET 2 AA4 2 VAL A 484 LYS A 485 1 O LYS A 485 N LYS A 325
SHEET 1 AA5 4 TRP A 386 TYR A 392 0
SHEET 2 AA5 4 ALA A 333 ILE A 338 -1 N LEU A 334 O TYR A 389
SHEET 3 AA5 4 LEU A 475 PHE A 477 -1 O GLU A 476 N LYS A 337
SHEET 4 AA5 4 GLY A 439 MET A 441 -1 N GLY A 439 O PHE A 477
SHEET 1 AA6 5 ASN A 370 VAL A 371 0
SHEET 2 AA6 5 LYS A 353 TYR A 361 -1 N THR A 358 O ASN A 370
SHEET 3 AA6 5 ARG A 401 VAL A 409 -1 O CYS A 407 N TYR A 355
SHEET 4 AA6 5 CYS A 420 ASN A 428 -1 O LEU A 422 N ILE A 406
SHEET 5 AA6 5 TRP A 446 PRO A 447 -1 O TRP A 446 N TRP A 424
SHEET 1 AA7 4 PHE A 751 LEU A 752 0
SHEET 2 AA7 4 GLN A 760 LEU A 764 -1 O LEU A 761 N PHE A 751
SHEET 3 AA7 4 LEU A 779 GLU A 784 -1 O GLU A 784 N ASN A 763
SHEET 4 AA7 4 ARG A 770 ILE A 771 -1 N ARG A 770 O TRP A 780
SHEET 1 AA8 6 PHE A 751 LEU A 752 0
SHEET 2 AA8 6 GLN A 760 LEU A 764 -1 O LEU A 761 N PHE A 751
SHEET 3 AA8 6 LEU A 779 GLU A 784 -1 O GLU A 784 N ASN A 763
SHEET 4 AA8 6 ASN A 796 PHE A 801 -1 O ASN A 797 N TRP A 783
SHEET 5 AA8 6 VAL A 845 GLU A 849 -1 O ILE A 848 N ILE A 800
SHEET 6 AA8 6 CYS A 838 GLY A 842 -1 N ILE A 841 O VAL A 845
SHEET 1 AA9 3 SER A 854 THR A 856 0
SHEET 2 AA9 3 ILE A 921 LYS A 924 -1 O VAL A 923 N HIS A 855
SHEET 3 AA9 3 LEU A 929 HIS A 931 -1 O PHE A 930 N MET A 922
SHEET 1 AB1 3 PHE B 355 ARG B 358 0
SHEET 2 AB1 3 TYR B 368 ARG B 373 -1 O THR B 369 N ARG B 358
SHEET 3 AB1 3 ASN B 378 ILE B 383 -1 O ILE B 381 N LEU B 370
LINK C SER A 6 N SEP A 7 1555 1555 1.33
LINK C SEP A 7 N GLY A 8 1555 1555 1.33
LINK C MET A 789 N SEP A 790 1555 1555 1.33
LINK C SEP A 790 N GLU A 791 1555 1555 1.33
CISPEP 1 ARG A 4 PRO A 5 0 -14.37
CISPEP 2 SER A 158 PRO A 159 0 10.96
CISPEP 3 SER A 199 PRO A 200 0 4.08
SITE 1 AC1 3 ASN A 605 ASN B 377 ASN B 378
CRYST1 114.873 116.442 149.973 90.00 90.00 90.00 P 21 21 21 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 0.008705 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
