HEADER TRANSFERASE 31-JAN-17 5X2F
TITLE CRYSTAL STRUCTURE OF EGFR 696-1022 T790M/V948R IN COMPLEX WITH SKLB(6)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 696-1022;
COMPND 5 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE
COMPND 6 ERBB-1;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EGFR, ERBB, ERBB1, HER1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS EGFR, T790M, V948R, SKLB, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.H.YUN
REVDAT 4 27-MAR-24 5X2F 1 REMARK
REVDAT 3 11-APR-18 5X2F 1 JRNL
REVDAT 2 21-FEB-18 5X2F 1 JRNL
REVDAT 1 07-FEB-18 5X2F 0
JRNL AUTH S.J.ZHU,P.ZHAO,J.YANG,R.MA,X.E.YAN,S.Y.YANG,J.W.YANG,C.H.YUN
JRNL TITL STRUCTURAL INSIGHTS INTO DRUG DEVELOPMENT STRATEGY TARGETING
JRNL TITL 2 EGFR T790M/C797S.
JRNL REF ONCOTARGET V. 9 13652 2018
JRNL REFN ESSN 1949-2553
JRNL PMID 29568384
JRNL DOI 10.18632/ONCOTARGET.24113
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 55505
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2833
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.2380 - 5.9651 0.99 3004 155 0.1765 0.2548
REMARK 3 2 5.9651 - 4.7373 1.00 2946 191 0.1749 0.2213
REMARK 3 3 4.7373 - 4.1392 1.00 2955 170 0.1534 0.1778
REMARK 3 4 4.1392 - 3.7611 1.00 2943 152 0.1702 0.1959
REMARK 3 5 3.7611 - 3.4917 1.00 2954 157 0.1809 0.2108
REMARK 3 6 3.4917 - 3.2859 0.99 2930 164 0.1962 0.2357
REMARK 3 7 3.2859 - 3.1214 0.97 2824 171 0.2113 0.2571
REMARK 3 8 3.1214 - 2.9856 0.95 2809 141 0.2221 0.2790
REMARK 3 9 2.9856 - 2.8707 0.92 2744 151 0.2282 0.2453
REMARK 3 10 2.8707 - 2.7717 0.89 2613 140 0.2340 0.2336
REMARK 3 11 2.7717 - 2.6850 0.86 2531 129 0.2467 0.2864
REMARK 3 12 2.6850 - 2.6083 0.84 2492 136 0.2392 0.2925
REMARK 3 13 2.6083 - 2.5396 0.83 2427 122 0.2521 0.2796
REMARK 3 14 2.5396 - 2.4777 0.82 2407 123 0.2570 0.3016
REMARK 3 15 2.4777 - 2.4214 0.81 2391 123 0.2661 0.2840
REMARK 3 16 2.4214 - 2.3698 0.81 2384 116 0.2576 0.3150
REMARK 3 17 2.3698 - 2.3224 0.81 2380 117 0.2550 0.2526
REMARK 3 18 2.3224 - 2.2786 0.80 2326 147 0.2646 0.3213
REMARK 3 19 2.2786 - 2.2379 0.79 2329 123 0.2752 0.3126
REMARK 3 20 2.2379 - 2.2000 0.76 2283 105 0.2731 0.2847
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 10080
REMARK 3 ANGLE : 1.325 13655
REMARK 3 CHIRALITY : 0.125 1519
REMARK 3 PLANARITY : 0.013 1710
REMARK 3 DIHEDRAL : 20.054 3815
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5X2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300002819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55540
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 89.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 (%): 40.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS 5.0, 22.5% PEG 3350, 5MM
REMARK 280 TCEP, VAPOR DIFFUSION, HANGING 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 51.29650
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
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: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 692
REMARK 465 SER A 693
REMARK 465 THR A 694
REMARK 465 SER A 695
REMARK 465 GLY A 696
REMARK 465 GLU A 697
REMARK 465 ALA A 698
REMARK 465 PRO A 699
REMARK 465 GLY A 863
REMARK 465 ALA A 864
REMARK 465 GLU A 865
REMARK 465 GLU A 866
REMARK 465 LYS A 867
REMARK 465 GLU A 868
REMARK 465 TYR A 869
REMARK 465 HIS A 870
REMARK 465 ALA A 871
REMARK 465 GLU A 872
REMARK 465 GLY A 873
REMARK 465 GLY A 874
REMARK 465 ASP A 1008
REMARK 465 ASP A 1009
REMARK 465 GLU A 1015
REMARK 465 TYR A 1016
REMARK 465 LEU A 1017
REMARK 465 ILE A 1018
REMARK 465 PRO A 1019
REMARK 465 GLN A 1020
REMARK 465 GLN A 1021
REMARK 465 GLY A 1022
REMARK 465 GLY B 692
REMARK 465 SER B 693
REMARK 465 THR B 694
REMARK 465 SER B 695
REMARK 465 GLY B 696
REMARK 465 GLU B 697
REMARK 465 ALA B 698
REMARK 465 VAL B 1011
REMARK 465 ASP B 1012
REMARK 465 ALA B 1013
REMARK 465 ASP B 1014
REMARK 465 GLU B 1015
REMARK 465 TYR B 1016
REMARK 465 LEU B 1017
REMARK 465 ILE B 1018
REMARK 465 PRO B 1019
REMARK 465 GLN B 1020
REMARK 465 GLN B 1021
REMARK 465 GLY B 1022
REMARK 465 GLY C 692
REMARK 465 SER C 693
REMARK 465 THR C 694
REMARK 465 SER C 695
REMARK 465 GLY C 696
REMARK 465 GLU C 697
REMARK 465 ALA C 698
REMARK 465 PRO C 699
REMARK 465 GLY C 863
REMARK 465 ALA C 864
REMARK 465 GLU C 865
REMARK 465 GLU C 866
REMARK 465 LYS C 867
REMARK 465 GLU C 868
REMARK 465 TYR C 869
REMARK 465 HIS C 870
REMARK 465 ALA C 871
REMARK 465 GLU C 872
REMARK 465 GLY C 873
REMARK 465 GLY C 874
REMARK 465 LYS C 875
REMARK 465 GLU C 1015
REMARK 465 TYR C 1016
REMARK 465 LEU C 1017
REMARK 465 ILE C 1018
REMARK 465 PRO C 1019
REMARK 465 GLN C 1020
REMARK 465 GLN C 1021
REMARK 465 GLY C 1022
REMARK 465 GLY D 692
REMARK 465 SER D 693
REMARK 465 THR D 694
REMARK 465 SER D 695
REMARK 465 GLY D 696
REMARK 465 GLU D 868
REMARK 465 TYR D 869
REMARK 465 HIS D 870
REMARK 465 ALA D 871
REMARK 465 GLU D 872
REMARK 465 GLY D 873
REMARK 465 GLY D 874
REMARK 465 MET D 1007
REMARK 465 ASP D 1008
REMARK 465 GLU D 1015
REMARK 465 TYR D 1016
REMARK 465 LEU D 1017
REMARK 465 ILE D 1018
REMARK 465 PRO D 1019
REMARK 465 GLN D 1020
REMARK 465 GLN D 1021
REMARK 465 GLY D 1022
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 754 CG CD CE NZ
REMARK 470 ARG A 832 NE CZ NH1 NH2
REMARK 470 LYS A 875 CG CD CE NZ
REMARK 470 HIS A 988 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A1010 CG1 CG2
REMARK 470 ASP A1012 CG OD1 OD2
REMARK 470 ASP A1014 CG OD1 OD2
REMARK 470 LYS B 713 CG CD CE NZ
REMARK 470 GLU B 734 CG CD OE1 OE2
REMARK 470 GLU B 749 CG CD OE1 OE2
REMARK 470 THR B 751 OG1 CG2
REMARK 470 GLU B 758 CG CD OE1 OE2
REMARK 470 ASP B 807 CG OD1 OD2
REMARK 470 GLU B 865 CD OE1 OE2
REMARK 470 LYS B 867 CG CD CE NZ
REMARK 470 LYS B 913 NZ
REMARK 470 LYS B 949 CE NZ
REMARK 470 LYS B 970 CE NZ
REMARK 470 HIS B 988 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B1009 CG OD1 OD2
REMARK 470 VAL B1010 CG1 CG2
REMARK 470 PHE C 723 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 748 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 749 CG CD OE1 OE2
REMARK 470 SER C 784 OG
REMARK 470 THR C 785 OG1 CG2
REMARK 470 ASN C 808 OD1 ND2
REMARK 470 LYS C 960 CE NZ
REMARK 470 ARG C 986 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 988 CG ND1 CD2 CE1 NE2
REMARK 470 VAL C1010 CG1 CG2
REMARK 470 GLU D 697 CG CD OE1 OE2
REMARK 470 ASN D 700 CG OD1 ND2
REMARK 470 GLN D 701 CG CD OE1 NE2
REMARK 470 ARG D 748 CD NE CZ NH1 NH2
REMARK 470 GLU D 749 CD OE1 OE2
REMARK 470 SER D 752 OG
REMARK 470 LYS D 757 CG CD CE NZ
REMARK 470 THR D 783 OG1 CG2
REMARK 470 GLU D 865 CG CD OE1 OE2
REMARK 470 LYS D 875 CG CD CE NZ
REMARK 470 GLN D 982 CG CD OE1 NE2
REMARK 470 ARG D 986 CD NE CZ NH1 NH2
REMARK 470 ASP D1009 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO D 753 C - N - CD ANGL. DEV. = -17.1 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 THR A 783 -122.73 -131.00
REMARK 500 HIS A 805 50.75 -105.29
REMARK 500 ARG A 836 -11.58 82.94
REMARK 500 ASP A 837 36.40 -142.16
REMARK 500 THR B 783 -146.96 -118.40
REMARK 500 ARG B 836 -11.42 82.16
REMARK 500 ASP B 837 23.89 -142.24
REMARK 500 ASP B 855 16.33 80.54
REMARK 500 ASP B1003 72.46 -150.21
REMARK 500 ALA C 722 -128.59 62.95
REMARK 500 SER C 784 -45.22 -131.91
REMARK 500 ARG C 836 -3.44 79.01
REMARK 500 ASP C 837 43.14 -156.46
REMARK 500 SER D 784 -84.21 -126.33
REMARK 500 ARG D 836 -10.18 82.78
REMARK 500 ASP D 837 36.03 -142.22
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 GLU A 749 ALA A 750 127.79
REMARK 500 THR D 751 SER D 752 -143.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1292 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH D1302 DISTANCE = 5.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU C 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU D 1101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5X26 RELATED DB: PDB
REMARK 900 RELATED ID: 5X27 RELATED DB: PDB
REMARK 900 RELATED ID: 5X28 RELATED DB: PDB
REMARK 900 RELATED ID: 5X2A RELATED DB: PDB
REMARK 900 RELATED ID: 5X2C RELATED DB: PDB
REMARK 900 RELATED ID: 5X2K RELATED DB: PDB
DBREF 5X2F A 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5X2F B 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5X2F C 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5X2F D 696 1022 UNP P00533 EGFR_HUMAN 696 1022
SEQADV 5X2F GLY A 692 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER A 693 UNP P00533 EXPRESSION TAG
SEQADV 5X2F THR A 694 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER A 695 UNP P00533 EXPRESSION TAG
SEQADV 5X2F MET A 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5X2F ARG A 948 UNP P00533 VAL 948 ENGINEERED MUTATION
SEQADV 5X2F GLY B 692 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER B 693 UNP P00533 EXPRESSION TAG
SEQADV 5X2F THR B 694 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER B 695 UNP P00533 EXPRESSION TAG
SEQADV 5X2F MET B 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5X2F ARG B 948 UNP P00533 VAL 948 ENGINEERED MUTATION
SEQADV 5X2F GLY C 692 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER C 693 UNP P00533 EXPRESSION TAG
SEQADV 5X2F THR C 694 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER C 695 UNP P00533 EXPRESSION TAG
SEQADV 5X2F MET C 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5X2F ARG C 948 UNP P00533 VAL 948 ENGINEERED MUTATION
SEQADV 5X2F GLY D 692 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER D 693 UNP P00533 EXPRESSION TAG
SEQADV 5X2F THR D 694 UNP P00533 EXPRESSION TAG
SEQADV 5X2F SER D 695 UNP P00533 EXPRESSION TAG
SEQADV 5X2F MET D 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5X2F ARG D 948 UNP P00533 VAL 948 ENGINEERED MUTATION
SEQRES 1 A 331 GLY SER THR SER GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 A 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 A 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 A 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 A 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 A 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 A 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 A 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 A 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 A 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 A 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 A 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 A 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 A 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 A 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 A 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 A 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 A 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 A 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 A 331 CYS THR ILE ASP VAL TYR MET ILE MET ARG LYS CYS TRP
SEQRES 21 A 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 A 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 A 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 A 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 A 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 A 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 B 331 GLY SER THR SER GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 B 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 B 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 B 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 B 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 B 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 B 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 B 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 B 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 B 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 B 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 B 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 B 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 B 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 B 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 B 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 B 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 B 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 B 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 B 331 CYS THR ILE ASP VAL TYR MET ILE MET ARG LYS CYS TRP
SEQRES 21 B 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 B 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 B 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 B 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 B 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 B 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 C 331 GLY SER THR SER GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 C 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 C 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 C 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 C 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 C 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 C 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 C 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 C 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 C 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 C 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 C 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 C 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 C 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 C 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 C 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 C 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 C 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 C 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 C 331 CYS THR ILE ASP VAL TYR MET ILE MET ARG LYS CYS TRP
SEQRES 21 C 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 C 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 C 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 C 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 C 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 C 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 D 331 GLY SER THR SER GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 D 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 D 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 D 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 D 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 D 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 D 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 D 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 D 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 D 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 D 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 D 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 D 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 D 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 D 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 D 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 D 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 D 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 D 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 D 331 CYS THR ILE ASP VAL TYR MET ILE MET ARG LYS CYS TRP
SEQRES 21 D 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 D 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 D 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 D 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 D 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 D 331 LEU ILE PRO GLN GLN GLY
HET 7XU A3001 36
HET 7XU B1101 36
HET 7XU C1101 36
HET 7XU D1101 36
HETNAM 7XU 9-CYCLOHEXYL-N2-[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]-N8-
HETNAM 2 7XU PHENYL-PURINE-2,8-DIAMINE
FORMUL 5 7XU 4(C28 H34 N8)
FORMUL 9 HOH *380(H2 O)
HELIX 1 AA1 ASN A 700 LEU A 704 5 5
HELIX 2 AA2 LYS A 708 THR A 710 5 3
HELIX 3 AA3 ALA A 755 SER A 768 1 14
HELIX 4 AA4 CYS A 797 HIS A 805 1 9
HELIX 5 AA5 GLY A 810 ARG A 831 1 22
HELIX 6 AA6 ALA A 839 ARG A 841 5 3
HELIX 7 AA7 GLY A 857 LEU A 862 1 6
HELIX 8 AA8 PRO A 877 MET A 881 5 5
HELIX 9 AA9 ALA A 882 ARG A 889 1 8
HELIX 10 AB1 THR A 892 THR A 909 1 18
HELIX 11 AB2 PRO A 919 GLY A 930 1 12
HELIX 12 AB3 THR A 940 TRP A 951 1 12
HELIX 13 AB4 ASP A 954 ARG A 958 5 5
HELIX 14 AB5 LYS A 960 ASP A 974 1 15
HELIX 15 AB6 ASP A 974 LEU A 979 1 6
HELIX 16 AB7 SER A 991 ASP A 1003 1 13
HELIX 17 AB8 LYS B 708 THR B 710 5 3
HELIX 18 AB9 ALA B 755 SER B 768 1 14
HELIX 19 AC1 CYS B 797 HIS B 805 1 9
HELIX 20 AC2 GLY B 810 ARG B 831 1 22
HELIX 21 AC3 ALA B 839 ARG B 841 5 3
HELIX 22 AC4 GLY B 857 GLY B 863 1 7
HELIX 23 AC5 GLU B 865 HIS B 870 1 6
HELIX 24 AC6 PRO B 877 MET B 881 5 5
HELIX 25 AC7 ALA B 882 ARG B 889 1 8
HELIX 26 AC8 THR B 892 THR B 909 1 18
HELIX 27 AC9 PRO B 919 SER B 921 5 3
HELIX 28 AD1 GLU B 922 LYS B 929 1 8
HELIX 29 AD2 THR B 940 TRP B 951 1 12
HELIX 30 AD3 ASP B 954 ARG B 958 5 5
HELIX 31 AD4 LYS B 960 ASP B 974 1 15
HELIX 32 AD5 ASP B 974 LEU B 979 1 6
HELIX 33 AD6 SER B 991 ASP B 1003 1 13
HELIX 34 AD7 ASN C 700 LEU C 704 5 5
HELIX 35 AD8 LYS C 708 THR C 710 5 3
HELIX 36 AD9 SER C 752 SER C 768 1 17
HELIX 37 AE1 CYS C 797 HIS C 805 1 9
HELIX 38 AE2 GLY C 810 ARG C 831 1 22
HELIX 39 AE3 ALA C 839 ARG C 841 5 3
HELIX 40 AE4 GLY C 857 LEU C 862 1 6
HELIX 41 AE5 PRO C 877 MET C 881 5 5
HELIX 42 AE6 ALA C 882 ARG C 889 1 8
HELIX 43 AE7 THR C 892 THR C 909 1 18
HELIX 44 AE8 PRO C 919 LYS C 929 1 11
HELIX 45 AE9 THR C 940 TRP C 951 1 12
HELIX 46 AF1 ASP C 954 ARG C 958 5 5
HELIX 47 AF2 LYS C 960 ASP C 974 1 15
HELIX 48 AF3 ASP C 974 LEU C 979 1 6
HELIX 49 AF4 SER C 991 ASP C 1003 1 13
HELIX 50 AF5 ALA D 698 LEU D 704 1 7
HELIX 51 AF6 ALA D 755 VAL D 769 1 15
HELIX 52 AF7 CYS D 797 HIS D 805 1 9
HELIX 53 AF8 LYS D 806 ILE D 809 5 4
HELIX 54 AF9 GLY D 810 ARG D 831 1 22
HELIX 55 AG1 ALA D 839 ARG D 841 5 3
HELIX 56 AG2 GLY D 857 GLY D 863 1 7
HELIX 57 AG3 PRO D 877 MET D 881 5 5
HELIX 58 AG4 ALA D 882 ARG D 889 1 8
HELIX 59 AG5 THR D 892 THR D 909 1 18
HELIX 60 AG6 PRO D 919 SER D 921 5 3
HELIX 61 AG7 GLU D 922 LYS D 929 1 8
HELIX 62 AG8 THR D 940 TRP D 951 1 12
HELIX 63 AG9 ASP D 954 ARG D 958 5 5
HELIX 64 AH1 LYS D 960 ASP D 974 1 15
HELIX 65 AH2 ASP D 974 LEU D 979 1 6
HELIX 66 AH3 SER D 991 ASP D 1003 1 13
SHEET 1 AA1 6 ARG A 705 ILE A 706 0
SHEET 2 AA1 6 GLY A 779 LEU A 782 1 O ILE A 780 N ARG A 705
SHEET 3 AA1 6 VAL A 786 MET A 790 -1 O ILE A 789 N GLY A 779
SHEET 4 AA1 6 ILE A 740 LEU A 747 -1 N LEU A 747 O VAL A 786
SHEET 5 AA1 6 GLY A 724 TRP A 731 -1 N TYR A 727 O ILE A 744
SHEET 6 AA1 6 PHE A 712 SER A 720 -1 N LEU A 718 O VAL A 726
SHEET 1 AA2 2 VAL A 843 THR A 847 0
SHEET 2 AA2 2 HIS A 850 ILE A 853 -1 O LYS A 852 N LEU A 844
SHEET 1 AA3 6 ARG B 705 ILE B 706 0
SHEET 2 AA3 6 GLY B 779 LEU B 782 1 O ILE B 780 N ARG B 705
SHEET 3 AA3 6 VAL B 786 MET B 790 -1 O ILE B 789 N GLY B 779
SHEET 4 AA3 6 ILE B 740 LEU B 747 -1 N ALA B 743 O MET B 790
SHEET 5 AA3 6 GLY B 724 TRP B 731 -1 N TRP B 731 O ILE B 740
SHEET 6 AA3 6 PHE B 712 SER B 720 -1 N LYS B 713 O LEU B 730
SHEET 1 AA4 2 VAL B 843 THR B 847 0
SHEET 2 AA4 2 HIS B 850 ILE B 853 -1 O LYS B 852 N LEU B 844
SHEET 1 AA5 6 ARG C 705 ILE C 706 0
SHEET 2 AA5 6 GLY C 779 CYS C 781 1 O ILE C 780 N ARG C 705
SHEET 3 AA5 6 GLN C 787 GLN C 791 -1 O ILE C 789 N GLY C 779
SHEET 4 AA5 6 ILE C 740 GLU C 746 -1 N ALA C 743 O MET C 790
SHEET 5 AA5 6 GLY C 724 TRP C 731 -1 N TYR C 727 O ILE C 744
SHEET 6 AA5 6 PHE C 712 GLY C 721 -1 N GLY C 719 O VAL C 726
SHEET 1 AA6 2 VAL C 843 THR C 847 0
SHEET 2 AA6 2 HIS C 850 ILE C 853 -1 O LYS C 852 N LEU C 844
SHEET 1 AA7 6 ARG D 705 ILE D 706 0
SHEET 2 AA7 6 GLY D 779 CYS D 781 1 O ILE D 780 N ARG D 705
SHEET 3 AA7 6 GLN D 787 MET D 790 -1 O ILE D 789 N GLY D 779
SHEET 4 AA7 6 ILE D 740 LEU D 747 -1 N ALA D 743 O MET D 790
SHEET 5 AA7 6 GLY D 724 TRP D 731 -1 N GLY D 729 O VAL D 742
SHEET 6 AA7 6 PHE D 712 SER D 720 -1 N LEU D 718 O VAL D 726
SHEET 1 AA8 2 VAL D 843 THR D 847 0
SHEET 2 AA8 2 HIS D 850 ILE D 853 -1 O LYS D 852 N LEU D 844
SITE 1 AC1 12 ALA A 743 LYS A 745 MET A 790 GLN A 791
SITE 2 AC1 12 LEU A 792 MET A 793 PRO A 794 GLY A 796
SITE 3 AC1 12 LEU A 844 ASP A 855 HOH A3126 HOH A3141
SITE 1 AC2 10 LEU B 718 LYS B 745 MET B 790 GLN B 791
SITE 2 AC2 10 LEU B 792 MET B 793 PRO B 794 GLY B 796
SITE 3 AC2 10 ASP B 855 HOH B1221
SITE 1 AC3 13 LEU C 718 GLY C 719 VAL C 726 ALA C 743
SITE 2 AC3 13 LYS C 745 MET C 790 GLN C 791 LEU C 792
SITE 3 AC3 13 MET C 793 PRO C 794 GLY C 796 ASP C 855
SITE 4 AC3 13 HOH C1227
SITE 1 AC4 13 ARG B 962 LEU D 718 ALA D 743 LYS D 745
SITE 2 AC4 13 MET D 790 GLN D 791 LEU D 792 MET D 793
SITE 3 AC4 13 PRO D 794 GLY D 796 LEU D 844 ASP D 855
SITE 4 AC4 13 HOH D1256
CRYST1 71.499 102.593 87.026 90.00 102.64 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 0.013986 0.000000 0.003136 0.00000
SCALE2 0.000000 0.009747 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011776 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
