HEADER TRANSFERASE 23-AUG-16 5GTY
TITLE CRYSTAL STRUCTURE OF EGFR 696-1022 T790M IN COMPLEX WITH LXX-6-26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A, B, D, E, F, G, H, C;
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
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, LXX-6-26, INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.YAN,C.H.YUN
REVDAT 4 08-NOV-23 5GTY 1 REMARK
REVDAT 3 29-NOV-17 5GTY 1 JRNL
REVDAT 2 04-OCT-17 5GTY 1 REMARK
REVDAT 1 06-SEP-17 5GTY 0
JRNL AUTH C.HU,A.WANG,H.WU,Z.QI,X.LI,X.E.YAN,C.CHEN,K.YU,F.ZOU,W.WANG,
JRNL AUTH 2 W.WANG,J.WU,J.LIU,B.WANG,L.WANG,T.REN,S.ZHANG,C.H.YUN,J.LIU,
JRNL AUTH 3 Q.LIU
JRNL TITL DISCOVERY AND CHARACTERIZATION OF A NOVEL IRREVERSIBLE EGFR
JRNL TITL 2 MUTANTS SELECTIVE AND POTENT KINASE INHIBITOR CHMFL-EGFR-26
JRNL TITL 3 WITH A DISTINCT BINDING MODE.
JRNL REF ONCOTARGET V. 8 18359 2017
JRNL REFN ESSN 1949-2553
JRNL PMID 28407693
JRNL DOI 10.18632/ONCOTARGET.15443
REMARK 2
REMARK 2 RESOLUTION. 3.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2400)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 41554
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2094
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 49.8167 - 7.7355 0.93 2683 148 0.2894 0.2960
REMARK 3 2 7.7355 - 6.1435 0.99 2777 146 0.2959 0.2861
REMARK 3 3 6.1435 - 5.3680 0.99 2789 126 0.2690 0.2636
REMARK 3 4 5.3680 - 4.8776 0.99 2690 172 0.2433 0.2589
REMARK 3 5 4.8776 - 4.5283 0.98 2704 155 0.2344 0.2673
REMARK 3 6 4.5283 - 4.2614 0.99 2748 134 0.2175 0.2300
REMARK 3 7 4.2614 - 4.0481 0.98 2679 149 0.2153 0.2253
REMARK 3 8 4.0481 - 3.8720 0.97 2718 127 0.2283 0.2467
REMARK 3 9 3.8720 - 3.7230 0.97 2643 143 0.2497 0.2925
REMARK 3 10 3.7230 - 3.5945 0.95 2596 138 0.2604 0.3207
REMARK 3 11 3.5945 - 3.4822 0.94 2596 135 0.2608 0.3262
REMARK 3 12 3.4822 - 3.3827 0.94 2591 124 0.2688 0.3039
REMARK 3 13 3.3827 - 3.2936 0.94 2577 132 0.2770 0.3259
REMARK 3 14 3.2936 - 3.2133 0.92 2548 124 0.3048 0.3379
REMARK 3 15 3.2133 - 3.1402 0.79 2121 141 0.2925 0.3468
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.540
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 : 0.010 19400
REMARK 3 ANGLE : 1.342 26317
REMARK 3 CHIRALITY : 0.087 2955
REMARK 3 PLANARITY : 0.013 3290
REMARK 3 DIHEDRAL : 28.214 7344
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 5GTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1300001424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97776
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42443
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2JIT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M CACL2, 0.1M B-TRIS PH 6.2, 24%
REMARK 280 PEG 550MME, 5MM TCEP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 35.89800
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, H, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, G
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 ALA A 693
REMARK 465 MET A 694
REMARK 465 GLY A 695
REMARK 465 GLY A 696
REMARK 465 GLU A 697
REMARK 465 ALA A 698
REMARK 465 PRO A 699
REMARK 465 ALA A 750
REMARK 465 THR A 751
REMARK 465 SER A 752
REMARK 465 PRO A 753
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 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 ALA B 693
REMARK 465 MET B 694
REMARK 465 GLY B 695
REMARK 465 GLY B 696
REMARK 465 GLU B 697
REMARK 465 ALA B 698
REMARK 465 PRO B 699
REMARK 465 ALA B 750
REMARK 465 THR B 751
REMARK 465 SER B 752
REMARK 465 PRO B 753
REMARK 465 GLY B 863
REMARK 465 ALA B 864
REMARK 465 GLU B 865
REMARK 465 GLU B 866
REMARK 465 LYS B 867
REMARK 465 GLU B 868
REMARK 465 TYR B 869
REMARK 465 HIS B 870
REMARK 465 ALA B 871
REMARK 465 GLU B 872
REMARK 465 GLY B 873
REMARK 465 GLY B 874
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 D 692
REMARK 465 ALA D 693
REMARK 465 MET D 694
REMARK 465 GLY D 695
REMARK 465 GLY D 696
REMARK 465 GLU D 697
REMARK 465 ALA D 698
REMARK 465 PRO D 699
REMARK 465 ASN D 700
REMARK 465 ALA D 750
REMARK 465 THR D 751
REMARK 465 SER D 752
REMARK 465 PRO D 753
REMARK 465 LYS D 754
REMARK 465 GLY D 863
REMARK 465 ALA D 864
REMARK 465 GLU D 865
REMARK 465 GLU D 866
REMARK 465 LYS D 867
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 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 465 GLY E 692
REMARK 465 ALA E 693
REMARK 465 MET E 694
REMARK 465 GLY E 695
REMARK 465 GLY E 696
REMARK 465 GLU E 697
REMARK 465 ALA E 698
REMARK 465 PRO E 699
REMARK 465 ASN E 700
REMARK 465 ALA E 750
REMARK 465 THR E 751
REMARK 465 SER E 752
REMARK 465 PRO E 753
REMARK 465 LYS E 754
REMARK 465 GLY E 863
REMARK 465 ALA E 864
REMARK 465 GLU E 865
REMARK 465 GLU E 866
REMARK 465 LYS E 867
REMARK 465 GLU E 868
REMARK 465 TYR E 869
REMARK 465 HIS E 870
REMARK 465 ALA E 871
REMARK 465 GLU E 872
REMARK 465 GLY E 873
REMARK 465 GLY E 874
REMARK 465 GLU E 1015
REMARK 465 TYR E 1016
REMARK 465 LEU E 1017
REMARK 465 ILE E 1018
REMARK 465 PRO E 1019
REMARK 465 GLN E 1020
REMARK 465 GLN E 1021
REMARK 465 GLY E 1022
REMARK 465 GLY F 692
REMARK 465 ALA F 693
REMARK 465 MET F 694
REMARK 465 GLY F 695
REMARK 465 GLY F 696
REMARK 465 GLU F 697
REMARK 465 ALA F 698
REMARK 465 PRO F 699
REMARK 465 ALA F 750
REMARK 465 THR F 751
REMARK 465 SER F 752
REMARK 465 PRO F 753
REMARK 465 GLY F 863
REMARK 465 ALA F 864
REMARK 465 GLU F 865
REMARK 465 GLU F 866
REMARK 465 LYS F 867
REMARK 465 GLU F 868
REMARK 465 TYR F 869
REMARK 465 HIS F 870
REMARK 465 ALA F 871
REMARK 465 GLU F 872
REMARK 465 GLY F 873
REMARK 465 GLY F 874
REMARK 465 LYS F 875
REMARK 465 ASP F 1014
REMARK 465 GLU F 1015
REMARK 465 TYR F 1016
REMARK 465 LEU F 1017
REMARK 465 ILE F 1018
REMARK 465 PRO F 1019
REMARK 465 GLN F 1020
REMARK 465 GLN F 1021
REMARK 465 GLY F 1022
REMARK 465 GLY G 692
REMARK 465 ALA G 693
REMARK 465 MET G 694
REMARK 465 GLY G 695
REMARK 465 GLY G 696
REMARK 465 GLU G 697
REMARK 465 ALA G 698
REMARK 465 ALA G 750
REMARK 465 THR G 751
REMARK 465 SER G 752
REMARK 465 PRO G 753
REMARK 465 LYS G 754
REMARK 465 GLY G 863
REMARK 465 ALA G 864
REMARK 465 GLU G 865
REMARK 465 GLU G 866
REMARK 465 LYS G 867
REMARK 465 GLU G 868
REMARK 465 TYR G 869
REMARK 465 HIS G 870
REMARK 465 ALA G 871
REMARK 465 GLU G 872
REMARK 465 GLY G 873
REMARK 465 GLY G 874
REMARK 465 GLU G 1015
REMARK 465 TYR G 1016
REMARK 465 LEU G 1017
REMARK 465 ILE G 1018
REMARK 465 PRO G 1019
REMARK 465 GLN G 1020
REMARK 465 GLN G 1021
REMARK 465 GLY G 1022
REMARK 465 GLY H 692
REMARK 465 ALA H 693
REMARK 465 MET H 694
REMARK 465 GLY H 695
REMARK 465 GLY H 696
REMARK 465 GLU H 697
REMARK 465 ALA H 698
REMARK 465 PRO H 699
REMARK 465 THR H 751
REMARK 465 SER H 752
REMARK 465 PRO H 753
REMARK 465 LYS H 754
REMARK 465 GLY H 863
REMARK 465 ALA H 864
REMARK 465 GLU H 865
REMARK 465 GLU H 866
REMARK 465 LYS H 867
REMARK 465 GLU H 868
REMARK 465 TYR H 869
REMARK 465 HIS H 870
REMARK 465 ALA H 871
REMARK 465 GLU H 872
REMARK 465 GLY H 873
REMARK 465 GLY H 874
REMARK 465 ASP H 1012
REMARK 465 LEU H 1017
REMARK 465 ILE H 1018
REMARK 465 PRO H 1019
REMARK 465 GLN H 1020
REMARK 465 GLN H 1021
REMARK 465 GLY H 1022
REMARK 465 GLY C 692
REMARK 465 ALA C 693
REMARK 465 MET C 694
REMARK 465 GLY C 695
REMARK 465 GLY C 696
REMARK 465 GLU C 697
REMARK 465 ALA C 698
REMARK 465 PRO C 699
REMARK 465 ALA C 750
REMARK 465 THR C 751
REMARK 465 SER C 752
REMARK 465 PRO C 753
REMARK 465 LEU C 862
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 VAL C 876
REMARK 465 ASP C 1014
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 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 ASN A 700 CG OD1 ND2
REMARK 470 LYS A 708 CE NZ
REMARK 470 GLU A 749 CG CD OE1 OE2
REMARK 470 LYS A 754 CG CD CE NZ
REMARK 470 SER A 768 OG
REMARK 470 LEU A 782 CG CD1 CD2
REMARK 470 LYS A 860 CG CD CE NZ
REMARK 470 LEU A 862 CG CD1 CD2
REMARK 470 LYS A 875 CD CE NZ
REMARK 470 LYS A 879 CG CD CE NZ
REMARK 470 LYS A 960 CE NZ
REMARK 470 ARG A 986 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 988 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 989 CG CD1 CD2
REMARK 470 GLU A1004 OE1 OE2
REMARK 470 ASP A1014 CG OD1 OD2
REMARK 470 ASN B 700 CG OD1 ND2
REMARK 470 LEU B 703 CD1 CD2
REMARK 470 LYS B 708 CE NZ
REMARK 470 ILE B 732 CG1 CG2 CD1
REMARK 470 LYS B 739 CD CE NZ
REMARK 470 ARG B 748 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 749 CG CD OE1 OE2
REMARK 470 LYS B 754 CG CD CE NZ
REMARK 470 LYS B 757 CG CD CE NZ
REMARK 470 LYS B 860 CG CD CE NZ
REMARK 470 LEU B 862 CG CD1 CD2
REMARK 470 LYS B 875 CG CD CE NZ
REMARK 470 LYS B 879 CG CD CE NZ
REMARK 470 GLU B 922 CG CD OE1 OE2
REMARK 470 LYS B 949 CG CD CE NZ
REMARK 470 ARG B 958 NH2
REMARK 470 ARG B 962 CZ NH1 NH2
REMARK 470 GLN B 976 CG CD OE1 NE2
REMARK 470 HIS B 988 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 989 CG CD1 CD2
REMARK 470 ASP B1009 CG OD1 OD2
REMARK 470 VAL B1010 CG1 CG2
REMARK 470 ASP B1014 CG OD1 OD2
REMARK 470 GLU D 709 CG CD OE1 OE2
REMARK 470 LYS D 737 CG CD CE NZ
REMARK 470 ARG D 748 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 749 CG CD OE1 OE2
REMARK 470 GLU D 758 CG CD OE1 OE2
REMARK 470 ILE D 759 CG1 CG2 CD1
REMARK 470 LEU D 760 CG CD1 CD2
REMARK 470 LEU D 782 CG CD1 CD2
REMARK 470 ILE D 809 CG1 CG2 CD1
REMARK 470 ARG D 832 CD NE CZ NH1 NH2
REMARK 470 GLN D 849 CG CD OE1 NE2
REMARK 470 LYS D 860 CG CD CE NZ
REMARK 470 LEU D 861 CG CD1 CD2
REMARK 470 LEU D 862 CG CD1 CD2
REMARK 470 LYS D 875 CG CD CE NZ
REMARK 470 GLN D 894 CD OE1 NE2
REMARK 470 ILE D 923 CG1 CG2 CD1
REMARK 470 LYS D 929 CE NZ
REMARK 470 ARG D 958 NE CZ NH1 NH2
REMARK 470 LYS D 960 CE NZ
REMARK 470 ARG D 962 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 967 CG CD OE1 OE2
REMARK 470 LYS D 970 CE NZ
REMARK 470 GLN D 982 CG CD OE1 NE2
REMARK 470 GLU D 985 CG CD OE1 OE2
REMARK 470 HIS D 988 CG ND1 CD2 CE1 NE2
REMARK 470 LEU D 989 CG CD1 CD2
REMARK 470 ARG D 999 NE CZ NH1 NH2
REMARK 470 MET D1007 CG SD CE
REMARK 470 ASP D1009 CG OD1 OD2
REMARK 470 VAL D1010 CG1 CG2
REMARK 470 VAL D1011 CG1 CG2
REMARK 470 LYS E 708 CE NZ
REMARK 470 SER E 720 OG
REMARK 470 LYS E 737 CG CD CE NZ
REMARK 470 GLU E 749 CG CD OE1 OE2
REMARK 470 LYS E 757 CG CD CE NZ
REMARK 470 GLU E 758 CG CD OE1 OE2
REMARK 470 LEU E 760 CG CD1 CD2
REMARK 470 GLU E 762 CG CD OE1 OE2
REMARK 470 ARG E 803 CZ NH1 NH2
REMARK 470 ARG E 832 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 846 NZ
REMARK 470 LYS E 860 CG CD CE NZ
REMARK 470 LEU E 862 CG CD1 CD2
REMARK 470 LYS E 875 CG CD CE NZ
REMARK 470 GLN E 894 CD OE1 NE2
REMARK 470 THR E 940 CB OG1 CG2
REMARK 470 ASP E 942 OD1 OD2
REMARK 470 LYS E 960 CE NZ
REMARK 470 GLU E 967 CG CD OE1 OE2
REMARK 470 LYS E 970 CG CD CE NZ
REMARK 470 GLN E 982 CG CD OE1 NE2
REMARK 470 ASP E 984 CG OD1 OD2
REMARK 470 GLU E 985 CG CD OE1 OE2
REMARK 470 HIS E 988 CG ND1 CD2 CE1 NE2
REMARK 470 LEU E 989 CG CD1 CD2
REMARK 470 MET E1007 CG SD CE
REMARK 470 ASP E1008 CG OD1 OD2
REMARK 470 ASP E1009 CG OD1 OD2
REMARK 470 VAL E1010 CG1 CG2
REMARK 470 VAL E1011 CG1 CG2
REMARK 470 LYS F 708 CG CD CE NZ
REMARK 470 ILE F 715 CG1 CG2 CD1
REMARK 470 PHE F 723 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE F 732 CG1 CG2 CD1
REMARK 470 GLU F 734 CG CD OE1 OE2
REMARK 470 LYS F 737 CG CD CE NZ
REMARK 470 GLU F 749 CG CD OE1 OE2
REMARK 470 LYS F 754 CG CD CE NZ
REMARK 470 LYS F 757 CG CD CE NZ
REMARK 470 GLU F 762 OE1 OE2
REMARK 470 SER F 768 OG
REMARK 470 LYS F 860 CG CD CE NZ
REMARK 470 GLN F 894 CD OE1 NE2
REMARK 470 ASP F 896 OD1
REMARK 470 GLU F 906 OE1 OE2
REMARK 470 THR F 940 CB OG1 CG2
REMARK 470 LYS F 960 CE NZ
REMARK 470 ARG F 962 CZ NH1 NH2
REMARK 470 HIS F 988 CG ND1 CD2 CE1 NE2
REMARK 470 ASP F1008 OD1
REMARK 470 ASP F1009 CG OD1 OD2
REMARK 470 LYS G 708 CG CD CE NZ
REMARK 470 PHE G 723 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE G 732 CG1 CG2 CD1
REMARK 470 ARG G 748 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 749 CG CD OE1 OE2
REMARK 470 LYS G 846 NZ
REMARK 470 LYS G 860 CG CD CE NZ
REMARK 470 LEU G 862 CG CD1 CD2
REMARK 470 LYS G 875 CG CD CE NZ
REMARK 470 VAL G 897 CG1 CG2
REMARK 470 ARG G 958 NH1 NH2
REMARK 470 LYS G 960 CE NZ
REMARK 470 GLU G 967 CD OE1 OE2
REMARK 470 HIS G 988 CG ND1 CD2 CE1 NE2
REMARK 470 ASN H 700 CG OD1 ND2
REMARK 470 LYS H 708 CE NZ
REMARK 470 PHE H 723 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG H 748 CD NE CZ NH1 NH2
REMARK 470 GLU H 749 CG CD OE1 OE2
REMARK 470 LYS H 846 CE NZ
REMARK 470 LYS H 860 CE NZ
REMARK 470 LYS H 875 CG CD CE NZ
REMARK 470 GLN H 894 CD OE1 NE2
REMARK 470 THR H 940 CB OG1 CG2
REMARK 470 ARG H 958 NH2
REMARK 470 LYS H 960 CE NZ
REMARK 470 ARG H 962 CZ NH1 NH2
REMARK 470 GLU H 967 CG CD OE1 OE2
REMARK 470 HIS H 988 CG ND1 CD2 CE1 NE2
REMARK 470 LEU H 989 CG CD1 CD2
REMARK 470 TYR H1016 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 708 CG CD CE NZ
REMARK 470 GLU C 711 CG CD OE1 OE2
REMARK 470 PHE C 723 CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE C 732 CG1 CG2 CD1
REMARK 470 GLU C 734 CG CD OE1 OE2
REMARK 470 LYS C 737 CE NZ
REMARK 470 GLU C 749 CG CD OE1 OE2
REMARK 470 LYS C 757 CG CD CE NZ
REMARK 470 LYS C 860 CG CD CE NZ
REMARK 470 LEU C 861 CG CD1 CD2
REMARK 470 GLU C 906 OE1
REMARK 470 LYS C 960 CE NZ
REMARK 470 HIS C 988 CG ND1 CD2 CE1 NE2
REMARK 470 LEU C 989 CG CD1 CD2
REMARK 470 ASP C1008 CG OD1 OD2
REMARK 470 ASP C1009 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU C 884 NH2 ARG C 958 1.02
REMARK 500 O ILE B 809 CE MET B 987 2.04
REMARK 500 CD GLU C 884 NH2 ARG C 958 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 967 CA GLU A 967 C -0.158
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 914 C - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO A 936 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 PRO B 936 C - N - CD ANGL. DEV. = -12.8 DEGREES
REMARK 500 PRO F 936 C - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO F 990 C - N - CD ANGL. DEV. = -16.8 DEGREES
REMARK 500 PRO G 936 C - N - CD ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG G 999 N - CA - CB ANGL. DEV. = 15.8 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 -177.95 -170.54
REMARK 500 ARG A 836 -11.45 82.50
REMARK 500 ASP A 837 68.48 -158.16
REMARK 500 ASP A 855 10.32 83.79
REMARK 500 ARG B 832 15.45 80.29
REMARK 500 ASP B 855 3.85 84.63
REMARK 500 THR D 783 -163.66 -172.89
REMARK 500 ARG D 836 -12.61 79.94
REMARK 500 ASP D 837 35.94 -142.25
REMARK 500 ASP D 855 4.97 81.14
REMARK 500 MET D1007 -133.06 54.28
REMARK 500 SER E 784 -38.29 -36.21
REMARK 500 ARG E 836 -57.08 73.37
REMARK 500 PHE F 910 46.67 71.35
REMARK 500 MET F1002 -50.54 -120.76
REMARK 500 ARG G 836 -56.78 72.49
REMARK 500 THR H 783 -158.36 -160.20
REMARK 500 ARG H 836 -10.31 80.90
REMARK 500 ASP H 837 76.09 -152.19
REMARK 500 THR C 783 -160.86 -165.78
REMARK 500 ARG C 836 -10.44 76.23
REMARK 500 ASP C 837 72.92 -157.34
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 B1236 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B1237 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH D1219 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH E1242 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH F1249 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH F1250 DISTANCE = 9.44 ANGSTROMS
REMARK 525 HOH G1248 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH H1227 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH C1235 DISTANCE = 6.28 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 816 A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 816 B 1101 and CYS B
REMARK 800 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 816 C 1101 and CYS C
REMARK 800 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 816 D 1101 and CYS D
REMARK 800 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 816 E 1101 and CYS E
REMARK 800 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 816 F 1101 and CYS F
REMARK 800 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 816 G 1101 and CYS G
REMARK 800 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 816 H 1101 and CYS H
REMARK 800 797
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GMP RELATED DB: PDB
REMARK 900 RELATED ID: 5GNK RELATED DB: PDB
REMARK 900 RELATED ID: 5GTZ RELATED DB: PDB
DBREF 5GTY A 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5GTY B 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5GTY D 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5GTY E 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5GTY F 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5GTY G 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5GTY H 696 1022 UNP P00533 EGFR_HUMAN 696 1022
DBREF 5GTY C 696 1022 UNP P00533 EGFR_HUMAN 696 1022
SEQADV 5GTY GLY A 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA A 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET A 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY A 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET A 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5GTY GLY B 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA B 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET B 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY B 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET B 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5GTY GLY D 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA D 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET D 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY D 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET D 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5GTY GLY E 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA E 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET E 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY E 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET E 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5GTY GLY F 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA F 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET F 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY F 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET F 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5GTY GLY G 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA G 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET G 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY G 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET G 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5GTY GLY H 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA H 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET H 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY H 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET H 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5GTY GLY C 692 UNP P00533 EXPRESSION TAG
SEQADV 5GTY ALA C 693 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET C 694 UNP P00533 EXPRESSION TAG
SEQADV 5GTY GLY C 695 UNP P00533 EXPRESSION TAG
SEQADV 5GTY MET C 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQRES 1 A 331 GLY ALA MET GLY 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 VAL 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 ALA MET GLY 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 VAL 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 D 331 GLY ALA MET GLY 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 VAL 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
SEQRES 1 E 331 GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 E 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 E 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 E 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 E 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 E 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 E 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 E 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 E 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 E 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 E 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 E 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 E 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 E 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 E 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 E 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 E 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 E 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 E 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 E 331 CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP
SEQRES 21 E 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 E 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 E 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 E 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 E 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 E 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 F 331 GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 F 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 F 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 F 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 F 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 F 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 F 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 F 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 F 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 F 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 F 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 F 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 F 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 F 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 F 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 F 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 F 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 F 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 F 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 F 331 CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP
SEQRES 21 F 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 F 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 F 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 F 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 F 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 F 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 G 331 GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 G 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 G 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 G 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 G 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 G 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 G 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 G 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 G 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 G 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 G 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 G 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 G 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 G 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 G 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 G 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 G 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 G 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 G 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 G 331 CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP
SEQRES 21 G 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 G 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 G 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 G 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 G 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 G 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 H 331 GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 H 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 H 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 H 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 H 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 H 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 H 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 H 331 THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE
SEQRES 9 H 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 H 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 H 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 H 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 H 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS
SEQRES 14 H 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 H 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 H 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 H 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 H 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 H 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 H 331 CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP
SEQRES 21 H 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 H 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 H 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 H 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 H 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 H 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 C 331 GLY ALA MET GLY 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 VAL 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
HET 816 A1101 36
HET 816 B1101 36
HET 816 D1101 36
HET 816 E1101 36
HET 816 F1101 36
HET 816 G1101 36
HET EDO G1102 4
HET 816 H1101 36
HET EDO H1102 4
HET EDO H1103 4
HET EDO H1104 4
HET 816 C1101 36
HETNAM 816 1-[(3R)-3-[4-AZANYL-3-[3-CHLORANYL-4-[(6-METHYLPYRIDIN-
HETNAM 2 816 2-YL)METHOXY]PHENYL]PYRAZOLO[3,4-D]PYRIMIDIN-1-
HETNAM 3 816 YL]PIPERIDIN-1-YL]PROP-2-EN-1-ONE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 816 8(C26 H26 CL N7 O2)
FORMUL 15 EDO 4(C2 H6 O2)
FORMUL 21 HOH *303(H2 O)
HELIX 1 AA1 LYS A 708 THR A 710 5 3
HELIX 2 AA2 ALA A 755 ALA A 767 1 13
HELIX 3 AA3 CYS A 797 HIS A 805 1 9
HELIX 4 AA4 GLY A 810 ARG A 831 1 22
HELIX 5 AA5 ALA A 839 ARG A 841 5 3
HELIX 6 AA6 GLY A 857 LEU A 862 1 6
HELIX 7 AA7 ALA A 882 ARG A 889 1 8
HELIX 8 AA8 THR A 892 THR A 909 1 18
HELIX 9 AA9 PRO A 919 GLY A 930 1 12
HELIX 10 AB1 THR A 940 TRP A 951 1 12
HELIX 11 AB2 LYS A 960 ASP A 974 1 15
HELIX 12 AB3 ASP A 974 LEU A 979 1 6
HELIX 13 AB4 SER A 991 ASP A 1003 1 13
HELIX 14 AB5 LYS B 708 THR B 710 5 3
HELIX 15 AB6 ALA B 755 VAL B 769 1 15
HELIX 16 AB7 CYS B 797 HIS B 805 1 9
HELIX 17 AB8 GLY B 810 ARG B 831 1 22
HELIX 18 AB9 GLY B 857 LEU B 862 1 6
HELIX 19 AC1 ALA B 882 ARG B 889 1 8
HELIX 20 AC2 THR B 892 THR B 909 1 18
HELIX 21 AC3 PRO B 919 GLY B 930 1 12
HELIX 22 AC4 THR B 940 TRP B 951 1 12
HELIX 23 AC5 LYS B 960 ARG B 973 1 14
HELIX 24 AC6 ASP B 974 LEU B 979 1 6
HELIX 25 AC7 SER B 991 ASP B 1003 1 13
HELIX 26 AC8 LYS D 708 THR D 710 5 3
HELIX 27 AC9 ASN D 756 SER D 768 1 13
HELIX 28 AD1 LEU D 798 HIS D 805 1 8
HELIX 29 AD2 LYS D 806 ILE D 809 5 4
HELIX 30 AD3 GLY D 810 ARG D 831 1 22
HELIX 31 AD4 GLY D 857 LEU D 862 1 6
HELIX 32 AD5 ALA D 882 ARG D 889 1 8
HELIX 33 AD6 THR D 892 THR D 909 1 18
HELIX 34 AD7 PRO D 919 GLY D 930 1 12
HELIX 35 AD8 THR D 940 TRP D 951 1 12
HELIX 36 AD9 ASP D 954 ARG D 958 5 5
HELIX 37 AE1 LYS D 960 ASP D 974 1 15
HELIX 38 AE2 ASP D 974 LEU D 979 1 6
HELIX 39 AE3 SER D 991 ASP D 1003 1 13
HELIX 40 AE4 ASN E 756 VAL E 769 1 14
HELIX 41 AE5 LEU E 798 HIS E 805 1 8
HELIX 42 AE6 GLY E 810 ARG E 831 1 22
HELIX 43 AE7 GLY E 857 LEU E 862 1 6
HELIX 44 AE8 ALA E 882 ARG E 889 1 8
HELIX 45 AE9 THR E 892 THR E 909 1 18
HELIX 46 AF1 PRO E 919 GLY E 930 1 12
HELIX 47 AF2 THR E 940 TRP E 951 1 12
HELIX 48 AF3 LYS E 960 ASP E 974 1 15
HELIX 49 AF4 ASP E 974 LEU E 979 1 6
HELIX 50 AF5 SER E 991 MET E 1002 1 12
HELIX 51 AF6 LYS F 708 THR F 710 5 3
HELIX 52 AF7 ALA F 755 VAL F 769 1 15
HELIX 53 AF8 CYS F 797 HIS F 805 1 9
HELIX 54 AF9 GLY F 810 ARG F 831 1 22
HELIX 55 AG1 GLY F 857 LEU F 862 1 6
HELIX 56 AG2 ALA F 882 ARG F 889 1 8
HELIX 57 AG3 THR F 892 PHE F 910 1 19
HELIX 58 AG4 PRO F 919 GLY F 930 1 12
HELIX 59 AG5 THR F 940 TRP F 951 1 12
HELIX 60 AG6 LYS F 960 ASP F 974 1 15
HELIX 61 AG7 ASP F 974 LEU F 979 1 6
HELIX 62 AG8 SER F 991 MET F 1002 1 12
HELIX 63 AG9 ASN G 756 VAL G 769 1 14
HELIX 64 AH1 CYS G 797 HIS G 805 1 9
HELIX 65 AH2 GLY G 810 ARG G 832 1 23
HELIX 66 AH3 GLY G 857 LEU G 862 1 6
HELIX 67 AH4 ALA G 882 ARG G 889 1 8
HELIX 68 AH5 THR G 892 THR G 909 1 18
HELIX 69 AH6 PRO G 919 GLY G 930 1 12
HELIX 70 AH7 THR G 940 TRP G 951 1 12
HELIX 71 AH8 ASP G 954 ARG G 958 5 5
HELIX 72 AH9 LYS G 960 ASP G 974 1 15
HELIX 73 AI1 ASP G 974 LEU G 979 1 6
HELIX 74 AI2 SER G 991 MET G 1002 1 12
HELIX 75 AI3 ASN H 756 VAL H 769 1 14
HELIX 76 AI4 CYS H 797 HIS H 805 1 9
HELIX 77 AI5 GLY H 810 ARG H 831 1 22
HELIX 78 AI6 GLY H 857 LEU H 862 1 6
HELIX 79 AI7 ALA H 882 ARG H 889 1 8
HELIX 80 AI8 THR H 892 THR H 909 1 18
HELIX 81 AI9 PRO H 919 SER H 921 5 3
HELIX 82 AJ1 GLU H 922 GLY H 930 1 9
HELIX 83 AJ2 THR H 940 TRP H 951 1 12
HELIX 84 AJ3 LYS H 960 ASP H 974 1 15
HELIX 85 AJ4 ASP H 974 LEU H 979 1 6
HELIX 86 AJ5 SER H 991 MET H 1002 1 12
HELIX 87 AJ6 ALA C 755 VAL C 769 1 15
HELIX 88 AJ7 CYS C 797 LYS C 806 1 10
HELIX 89 AJ8 GLY C 810 ARG C 831 1 22
HELIX 90 AJ9 ALA C 882 ARG C 889 1 8
HELIX 91 AK1 THR C 892 THR C 909 1 18
HELIX 92 AK2 PRO C 919 GLY C 930 1 12
HELIX 93 AK3 THR C 940 TRP C 951 1 12
HELIX 94 AK4 ASP C 954 ARG C 958 5 5
HELIX 95 AK5 LYS C 960 ASP C 974 1 15
HELIX 96 AK6 ASP C 974 LEU C 979 1 6
HELIX 97 AK7 SER C 991 MET C 1002 1 12
SHEET 1 AA1 6 ARG A 705 ILE A 706 0
SHEET 2 AA1 6 GLY A 779 CYS A 781 1 O ILE A 780 N ARG A 705
SHEET 3 AA1 6 GLN A 787 GLN A 791 -1 O ILE A 789 N GLY A 779
SHEET 4 AA1 6 ILE A 740 LEU A 747 -1 N LYS A 745 O LEU A 788
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 GLY A 719 O VAL A 726
SHEET 1 AA2 2 VAL A 843 VAL A 845 0
SHEET 2 AA2 2 VAL A 851 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 CYS B 781 1 O ILE B 780 N ARG B 705
SHEET 3 AA3 6 GLN B 787 GLN B 791 -1 O ILE B 789 N GLY B 779
SHEET 4 AA3 6 ILE B 740 LEU B 747 -1 N LYS B 745 O LEU B 788
SHEET 5 AA3 6 GLY B 724 TRP B 731 -1 N TYR B 727 O ILE B 744
SHEET 6 AA3 6 PHE B 712 SER B 720 -1 N GLY B 719 O VAL B 726
SHEET 1 AA4 6 ARG D 705 ILE D 706 0
SHEET 2 AA4 6 GLY D 779 CYS D 781 1 O ILE D 780 N ARG D 705
SHEET 3 AA4 6 VAL D 786 GLN D 791 -1 O ILE D 789 N GLY D 779
SHEET 4 AA4 6 ILE D 740 LEU D 747 -1 N ALA D 743 O MET D 790
SHEET 5 AA4 6 THR D 725 TRP D 731 -1 N TYR D 727 O ILE D 744
SHEET 6 AA4 6 PHE D 712 SER D 720 -1 N LYS D 713 O LEU D 730
SHEET 1 AA5 3 GLY D 796 CYS D 797 0
SHEET 2 AA5 3 VAL D 843 VAL D 845 -1 O VAL D 845 N GLY D 796
SHEET 3 AA5 3 VAL D 851 ILE D 853 -1 O LYS D 852 N LEU D 844
SHEET 1 AA6 6 ARG E 705 ILE E 706 0
SHEET 2 AA6 6 GLY E 779 CYS E 781 1 O ILE E 780 N ARG E 705
SHEET 3 AA6 6 VAL E 786 GLN E 791 -1 O ILE E 789 N GLY E 779
SHEET 4 AA6 6 ILE E 740 LEU E 747 -1 N ALA E 743 O MET E 790
SHEET 5 AA6 6 GLY E 724 TRP E 731 -1 N TYR E 727 O ILE E 744
SHEET 6 AA6 6 PHE E 712 SER E 720 -1 N LYS E 713 O LEU E 730
SHEET 1 AA7 3 GLY E 796 CYS E 797 0
SHEET 2 AA7 3 VAL E 843 THR E 847 -1 O VAL E 845 N GLY E 796
SHEET 3 AA7 3 HIS E 850 ILE E 853 -1 O LYS E 852 N LEU E 844
SHEET 1 AA8 6 ARG F 705 ILE F 706 0
SHEET 2 AA8 6 GLY F 779 CYS F 781 1 O ILE F 780 N ARG F 705
SHEET 3 AA8 6 GLN F 787 GLN F 791 -1 O ILE F 789 N GLY F 779
SHEET 4 AA8 6 ILE F 740 LEU F 747 -1 N ALA F 743 O MET F 790
SHEET 5 AA8 6 GLY F 724 TRP F 731 -1 N TYR F 727 O ILE F 744
SHEET 6 AA8 6 PHE F 712 SER F 720 -1 N LYS F 716 O LYS F 728
SHEET 1 AA9 2 VAL F 843 VAL F 845 0
SHEET 2 AA9 2 VAL F 851 ILE F 853 -1 O LYS F 852 N LEU F 844
SHEET 1 AB1 6 ARG G 705 ILE G 706 0
SHEET 2 AB1 6 LEU G 777 CYS G 781 1 O ILE G 780 N ARG G 705
SHEET 3 AB1 6 GLN G 787 MET G 790 -1 O GLN G 787 N CYS G 781
SHEET 4 AB1 6 ILE G 740 LEU G 747 -1 N LYS G 745 O LEU G 788
SHEET 5 AB1 6 GLY G 724 TRP G 731 -1 N TYR G 727 O ILE G 744
SHEET 6 AB1 6 PHE G 712 SER G 720 -1 N GLY G 719 O VAL G 726
SHEET 1 AB2 2 VAL G 843 VAL G 845 0
SHEET 2 AB2 2 VAL G 851 ILE G 853 -1 O LYS G 852 N LEU G 844
SHEET 1 AB3 6 ARG H 705 ILE H 706 0
SHEET 2 AB3 6 GLY H 779 CYS H 781 1 O ILE H 780 N ARG H 705
SHEET 3 AB3 6 GLN H 787 MET H 790 -1 O GLN H 787 N CYS H 781
SHEET 4 AB3 6 ILE H 740 LEU H 747 -1 N ALA H 743 O MET H 790
SHEET 5 AB3 6 GLY H 724 TRP H 731 -1 N GLY H 729 O VAL H 742
SHEET 6 AB3 6 PHE H 712 SER H 720 -1 N LYS H 716 O LYS H 728
SHEET 1 AB4 2 LEU H 844 VAL H 845 0
SHEET 2 AB4 2 VAL H 851 LYS H 852 -1 O LYS H 852 N LEU H 844
SHEET 1 AB5 6 ARG C 705 ILE C 706 0
SHEET 2 AB5 6 GLY C 779 CYS C 781 1 O ILE C 780 N ARG C 705
SHEET 3 AB5 6 GLN C 787 GLN C 791 -1 O ILE C 789 N GLY C 779
SHEET 4 AB5 6 ILE C 740 LEU C 747 -1 N LYS C 745 O LEU C 788
SHEET 5 AB5 6 GLY C 724 TRP C 731 -1 N GLY C 729 O VAL C 742
SHEET 6 AB5 6 PHE C 712 SER C 720 -1 N LYS C 716 O LYS C 728
SHEET 1 AB6 2 VAL C 843 THR C 847 0
SHEET 2 AB6 2 HIS C 850 ILE C 853 -1 O LYS C 852 N LEU C 844
LINK SG CYS A 797 CAP 816 A1101 1555 1555 1.82
LINK SG CYS B 797 CAP 816 B1101 1555 1555 1.81
LINK SG CYS D 797 CAP 816 D1101 1555 1555 1.82
LINK SG CYS E 797 CAP 816 E1101 1555 1555 1.82
LINK SG CYS F 797 CAP 816 F1101 1555 1555 1.83
LINK SG CYS G 797 CAP 816 G1101 1555 1555 1.82
LINK SG CYS H 797 CAP 816 H1101 1555 1555 1.82
LINK SG CYS C 797 CAP 816 C1101 1555 1555 1.82
CISPEP 1 HIS B 988 LEU B 989 0 9.97
SITE 1 AC1 18 GLY A 719 VAL A 726 ALA A 743 LYS A 745
SITE 2 AC1 18 ARG A 776 LEU A 777 LEU A 788 MET A 790
SITE 3 AC1 18 GLN A 791 MET A 793 GLY A 796 CYS A 797
SITE 4 AC1 18 ASP A 800 ARG A 841 THR A 854 ASP A 855
SITE 5 AC1 18 LEU A 858 HOH A1219
SITE 1 AC2 4 GLU B 922 ILE B 926 GLU B 931 ASP G 974
SITE 1 AC3 2 GLU H 736 LYS H 737
SITE 1 AC4 1 MET H 945
SITE 1 AC5 1 MET H 945
SITE 1 AC6 20 GLY B 719 ALA B 743 LYS B 745 MET B 766
SITE 2 AC6 20 ARG B 776 LEU B 777 LEU B 788 MET B 790
SITE 3 AC6 20 GLN B 791 MET B 793 GLY B 796 LEU B 798
SITE 4 AC6 20 LEU B 799 ASP B 800 TYR B 801 ARG B 841
SITE 5 AC6 20 VAL B 843 THR B 854 ASP B 855 LEU B 858
SITE 1 AC7 19 GLY C 719 VAL C 726 ALA C 743 CYS C 775
SITE 2 AC7 19 ARG C 776 LEU C 777 LEU C 788 MET C 790
SITE 3 AC7 19 MET C 793 PHE C 795 GLY C 796 LEU C 798
SITE 4 AC7 19 LEU C 799 ASP C 800 TYR C 801 ARG C 841
SITE 5 AC7 19 VAL C 843 THR C 854 ASP C 855
SITE 1 AC8 20 LEU D 718 GLY D 719 VAL D 726 ALA D 743
SITE 2 AC8 20 LYS D 745 ARG D 776 LEU D 777 LEU D 788
SITE 3 AC8 20 MET D 790 GLN D 791 MET D 793 PHE D 795
SITE 4 AC8 20 GLY D 796 LEU D 798 LEU D 799 ASP D 800
SITE 5 AC8 20 TYR D 801 LEU D 844 THR D 854 ASP D 855
SITE 1 AC9 19 LEU E 718 GLY E 719 SER E 720 ALA E 743
SITE 2 AC9 19 LYS E 745 MET E 766 CYS E 775 LEU E 788
SITE 3 AC9 19 MET E 790 MET E 793 PHE E 795 GLY E 796
SITE 4 AC9 19 LEU E 798 LEU E 799 ASP E 800 TYR E 801
SITE 5 AC9 19 VAL E 843 THR E 854 ASP E 855
SITE 1 AD1 21 GLY F 719 VAL F 726 ALA F 743 LYS F 745
SITE 2 AD1 21 CYS F 775 ARG F 776 LEU F 777 LEU F 788
SITE 3 AD1 21 MET F 790 MET F 793 PHE F 795 GLY F 796
SITE 4 AD1 21 LEU F 798 LEU F 799 ASP F 800 TYR F 801
SITE 5 AD1 21 ARG F 841 THR F 854 ASP F 855 LEU F 858
SITE 6 AD1 21 HOH F1231
SITE 1 AD2 21 LEU G 718 GLY G 719 ALA G 743 LYS G 745
SITE 2 AD2 21 ARG G 776 LEU G 777 LEU G 788 MET G 790
SITE 3 AD2 21 GLN G 791 LEU G 792 MET G 793 GLY G 796
SITE 4 AD2 21 LEU G 798 LEU G 799 ASP G 800 TYR G 801
SITE 5 AD2 21 ARG G 841 VAL G 843 THR G 854 ASP G 855
SITE 6 AD2 21 PHE G 856
SITE 1 AD3 24 ARG E 962 LEU H 718 GLY H 719 ALA H 743
SITE 2 AD3 24 LYS H 745 MET H 766 ARG H 776 LEU H 777
SITE 3 AD3 24 LEU H 788 MET H 790 GLN H 791 LEU H 792
SITE 4 AD3 24 MET H 793 GLY H 796 LEU H 798 LEU H 799
SITE 5 AD3 24 ASP H 800 TYR H 801 ARG H 841 VAL H 843
SITE 6 AD3 24 THR H 854 ASP H 855 PHE H 856 LEU H 858
CRYST1 117.427 71.796 152.530 90.00 103.53 90.00 P 1 21 1 16
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 0.008516 0.000000 0.002049 0.00000
SCALE2 0.000000 0.013928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006743 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
