HEADER MUSCLE PROTEIN 26-AUG-98 1BR2
TITLE SMOOTH MUSCLE MYOSIN MOTOR DOMAIN COMPLEXED WITH MGADP.ALF4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: MOTOR DOMAIN;
COMPND 5 EC: 3.6.1.32;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: LIGANDS MG, ADP, ALF(4)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELL_LINE: SF9;
SOURCE 6 ORGAN: GIZZARD;
SOURCE 7 TISSUE: SMOOTH MUSCLE;
SOURCE 8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS
KEYWDS MUSCLE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.DOMINGUEZ,K.M.TRYBUS,C.COHEN
REVDAT 5 09-AUG-23 1BR2 1 REMARK LINK
REVDAT 4 24-FEB-09 1BR2 1 VERSN
REVDAT 3 30-SEP-03 1BR2 1 DBREF
REVDAT 2 08-JUN-99 1BR2 3 HET COMPND REMARK HETATM
REVDAT 2 2 3 DBREF SEQADV HEADER TER
REVDAT 2 3 3 ATOM SOURCE FORMUL JRNL
REVDAT 2 4 3 HETSYN CONECT
REVDAT 1 09-SEP-98 1BR2 0
JRNL AUTH R.DOMINGUEZ,Y.FREYZON,K.M.TRYBUS,C.COHEN
JRNL TITL CRYSTAL STRUCTURE OF A VERTEBRATE SMOOTH MUSCLE MYOSIN MOTOR
JRNL TITL 2 DOMAIN AND ITS COMPLEX WITH THE ESSENTIAL LIGHT CHAIN:
JRNL TITL 3 VISUALIZATION OF THE PRE-POWER STROKE STATE.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 94 559 1998
JRNL REFN ISSN 0092-8674
JRNL PMID 9741621
JRNL DOI 10.1016/S0092-8674(00)81598-6
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 0.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.1
REMARK 3 NUMBER OF REFLECTIONS : 96444
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 SET) : 0.232
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 31620
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.50
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.600
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172017.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JAN-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99071
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.7
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1MND
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG8000 100MM IMIDAZOLE PH 6.8
REMARK 280 150MM CACL2 2MM MGADP 2MM AL(NO3)3 8MM NAF PROTEIN CONCENTRATION:
REMARK 280 10MG/ML TEMPERATURE: 4 DEGREES CENTIGRADE, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 ALA A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 4
REMARK 465 PRO A 5
REMARK 465 LEU A 6
REMARK 465 SER A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 GLU A 10
REMARK 465 LYS A 11
REMARK 465 PHE A 12
REMARK 465 LEU A 13
REMARK 465 PHE A 14
REMARK 465 VAL A 15
REMARK 465 ASP A 16
REMARK 465 LYS A 17
REMARK 465 ASN A 18
REMARK 465 PHE A 19
REMARK 465 VAL A 20
REMARK 465 ASN A 21
REMARK 465 ASN A 22
REMARK 465 PRO A 23
REMARK 465 LEU A 24
REMARK 465 ALA A 25
REMARK 465 GLN A 26
REMARK 465 ALA A 27
REMARK 465 ASP A 28
REMARK 465 TRP A 29
REMARK 465 SER A 30
REMARK 465 ALA A 31
REMARK 465 LYS A 32
REMARK 465 LYS A 33
REMARK 465 LYS A 50
REMARK 465 GLU A 51
REMARK 465 GLU A 52
REMARK 465 LYS A 53
REMARK 465 GLY A 54
REMARK 465 ASP A 55
REMARK 465 SER A 200
REMARK 465 HIS A 201
REMARK 465 LYS A 202
REMARK 465 GLY A 203
REMARK 465 LYS A 204
REMARK 465 LYS A 205
REMARK 465 ASP A 206
REMARK 465 THR A 207
REMARK 465 SER A 208
REMARK 465 ILE A 209
REMARK 465 THR A 210
REMARK 465 GLN A 211
REMARK 465 GLY A 212
REMARK 465 PRO A 213
REMARK 465 SER A 214
REMARK 465 PHE A 215
REMARK 465 SER A 216
REMARK 465 TYR A 217
REMARK 465 ARG A 371
REMARK 465 ASN A 372
REMARK 465 THR A 373
REMARK 465 ASP A 374
REMARK 465 ARG A 406
REMARK 465 ILE A 407
REMARK 465 LYS A 408
REMARK 465 VAL A 409
REMARK 465 GLY A 410
REMARK 465 ARG A 411
REMARK 465 ASP A 412
REMARK 465 VAL A 413
REMARK 465 VAL A 414
REMARK 465 GLN A 415
REMARK 465 LYS A 452
REMARK 465 THR A 453
REMARK 465 LYS A 454
REMARK 465 ARG A 455
REMARK 465 GLN A 456
REMARK 465 GLY A 457
REMARK 465 TRP A 546
REMARK 465 PHE A 547
REMARK 465 PRO A 548
REMARK 465 LYS A 549
REMARK 465 LYS A 573
REMARK 465 GLN A 574
REMARK 465 LEU A 575
REMARK 465 LYS A 576
REMARK 465 ASP A 577
REMARK 465 ASP A 627
REMARK 465 VAL A 628
REMARK 465 ASP A 629
REMARK 465 ARG A 630
REMARK 465 ILE A 631
REMARK 465 VAL A 632
REMARK 465 GLY A 633
REMARK 465 LEU A 634
REMARK 465 ASP A 635
REMARK 465 GLN A 636
REMARK 465 MET A 637
REMARK 465 ALA A 638
REMARK 465 LYS A 639
REMARK 465 MET A 640
REMARK 465 THR A 641
REMARK 465 GLU A 642
REMARK 465 SER A 643
REMARK 465 SER A 644
REMARK 465 LEU A 645
REMARK 465 PRO A 646
REMARK 465 SER A 647
REMARK 465 ALA A 648
REMARK 465 SER A 649
REMARK 465 LYS A 650
REMARK 465 THR A 651
REMARK 465 LYS A 652
REMARK 465 LYS A 653
REMARK 465 GLY A 654
REMARK 465 MET A 655
REMARK 465 PHE A 656
REMARK 465 LEU A 790
REMARK 465 LYS A 791
REMARK 465 ILE A 792
REMARK 465 ALA B 2
REMARK 465 GLN B 3
REMARK 465 LYS B 4
REMARK 465 PRO B 5
REMARK 465 LEU B 6
REMARK 465 SER B 7
REMARK 465 ASP B 8
REMARK 465 ASP B 9
REMARK 465 GLU B 10
REMARK 465 LYS B 11
REMARK 465 PHE B 12
REMARK 465 LEU B 13
REMARK 465 PHE B 14
REMARK 465 VAL B 15
REMARK 465 ASP B 16
REMARK 465 LYS B 17
REMARK 465 ASN B 18
REMARK 465 PHE B 19
REMARK 465 VAL B 20
REMARK 465 ASN B 21
REMARK 465 ASN B 22
REMARK 465 PRO B 23
REMARK 465 LEU B 24
REMARK 465 ALA B 25
REMARK 465 GLN B 26
REMARK 465 ALA B 27
REMARK 465 ASP B 28
REMARK 465 TRP B 29
REMARK 465 SER B 30
REMARK 465 ALA B 31
REMARK 465 LYS B 32
REMARK 465 LYS B 33
REMARK 465 LYS B 50
REMARK 465 GLU B 51
REMARK 465 GLU B 52
REMARK 465 LYS B 53
REMARK 465 GLY B 54
REMARK 465 ASP B 55
REMARK 465 SER B 200
REMARK 465 HIS B 201
REMARK 465 LYS B 202
REMARK 465 GLY B 203
REMARK 465 LYS B 204
REMARK 465 LYS B 205
REMARK 465 ASP B 206
REMARK 465 THR B 207
REMARK 465 SER B 208
REMARK 465 ILE B 209
REMARK 465 THR B 210
REMARK 465 GLN B 211
REMARK 465 GLY B 212
REMARK 465 PRO B 213
REMARK 465 SER B 214
REMARK 465 PHE B 215
REMARK 465 SER B 216
REMARK 465 TYR B 217
REMARK 465 ARG B 371
REMARK 465 ASN B 372
REMARK 465 THR B 373
REMARK 465 ASP B 374
REMARK 465 ARG B 406
REMARK 465 ILE B 407
REMARK 465 LYS B 408
REMARK 465 VAL B 409
REMARK 465 GLY B 410
REMARK 465 ARG B 411
REMARK 465 ASP B 412
REMARK 465 VAL B 413
REMARK 465 VAL B 414
REMARK 465 GLN B 415
REMARK 465 LYS B 452
REMARK 465 THR B 453
REMARK 465 LYS B 454
REMARK 465 ARG B 455
REMARK 465 GLN B 456
REMARK 465 GLY B 457
REMARK 465 TRP B 546
REMARK 465 PHE B 547
REMARK 465 PRO B 548
REMARK 465 LYS B 549
REMARK 465 LYS B 573
REMARK 465 GLN B 574
REMARK 465 LEU B 575
REMARK 465 LYS B 576
REMARK 465 ASP B 577
REMARK 465 ASP B 627
REMARK 465 VAL B 628
REMARK 465 ASP B 629
REMARK 465 ARG B 630
REMARK 465 ILE B 631
REMARK 465 VAL B 632
REMARK 465 GLY B 633
REMARK 465 LEU B 634
REMARK 465 ASP B 635
REMARK 465 GLN B 636
REMARK 465 MET B 637
REMARK 465 ALA B 638
REMARK 465 LYS B 639
REMARK 465 MET B 640
REMARK 465 THR B 641
REMARK 465 GLU B 642
REMARK 465 SER B 643
REMARK 465 SER B 644
REMARK 465 LEU B 645
REMARK 465 PRO B 646
REMARK 465 SER B 647
REMARK 465 ALA B 648
REMARK 465 SER B 649
REMARK 465 LYS B 650
REMARK 465 THR B 651
REMARK 465 LYS B 652
REMARK 465 LYS B 653
REMARK 465 GLY B 654
REMARK 465 MET B 655
REMARK 465 PHE B 656
REMARK 465 LEU B 790
REMARK 465 LYS B 791
REMARK 465 ILE B 792
REMARK 465 ALA C 2
REMARK 465 GLN C 3
REMARK 465 LYS C 4
REMARK 465 PRO C 5
REMARK 465 LEU C 6
REMARK 465 SER C 7
REMARK 465 ASP C 8
REMARK 465 ASP C 9
REMARK 465 GLU C 10
REMARK 465 LYS C 11
REMARK 465 PHE C 12
REMARK 465 LEU C 13
REMARK 465 PHE C 14
REMARK 465 VAL C 15
REMARK 465 ASP C 16
REMARK 465 LYS C 17
REMARK 465 ASN C 18
REMARK 465 PHE C 19
REMARK 465 VAL C 20
REMARK 465 ASN C 21
REMARK 465 ASN C 22
REMARK 465 PRO C 23
REMARK 465 LEU C 24
REMARK 465 ALA C 25
REMARK 465 GLN C 26
REMARK 465 ALA C 27
REMARK 465 ASP C 28
REMARK 465 TRP C 29
REMARK 465 SER C 30
REMARK 465 ALA C 31
REMARK 465 LYS C 32
REMARK 465 LYS C 33
REMARK 465 LYS C 50
REMARK 465 GLU C 51
REMARK 465 GLU C 52
REMARK 465 LYS C 53
REMARK 465 GLY C 54
REMARK 465 ASP C 55
REMARK 465 SER C 200
REMARK 465 HIS C 201
REMARK 465 LYS C 202
REMARK 465 GLY C 203
REMARK 465 LYS C 204
REMARK 465 LYS C 205
REMARK 465 ASP C 206
REMARK 465 THR C 207
REMARK 465 SER C 208
REMARK 465 ILE C 209
REMARK 465 THR C 210
REMARK 465 GLN C 211
REMARK 465 GLY C 212
REMARK 465 PRO C 213
REMARK 465 SER C 214
REMARK 465 PHE C 215
REMARK 465 SER C 216
REMARK 465 TYR C 217
REMARK 465 ARG C 371
REMARK 465 ASN C 372
REMARK 465 THR C 373
REMARK 465 ASP C 374
REMARK 465 ARG C 406
REMARK 465 ILE C 407
REMARK 465 LYS C 408
REMARK 465 VAL C 409
REMARK 465 GLY C 410
REMARK 465 ARG C 411
REMARK 465 ASP C 412
REMARK 465 VAL C 413
REMARK 465 VAL C 414
REMARK 465 GLN C 415
REMARK 465 LYS C 452
REMARK 465 THR C 453
REMARK 465 LYS C 454
REMARK 465 ARG C 455
REMARK 465 GLN C 456
REMARK 465 GLY C 457
REMARK 465 TRP C 546
REMARK 465 PHE C 547
REMARK 465 PRO C 548
REMARK 465 LYS C 549
REMARK 465 LYS C 573
REMARK 465 GLN C 574
REMARK 465 LEU C 575
REMARK 465 LYS C 576
REMARK 465 ASP C 577
REMARK 465 ASP C 627
REMARK 465 VAL C 628
REMARK 465 ASP C 629
REMARK 465 ARG C 630
REMARK 465 ILE C 631
REMARK 465 VAL C 632
REMARK 465 GLY C 633
REMARK 465 LEU C 634
REMARK 465 ASP C 635
REMARK 465 GLN C 636
REMARK 465 MET C 637
REMARK 465 ALA C 638
REMARK 465 LYS C 639
REMARK 465 MET C 640
REMARK 465 THR C 641
REMARK 465 GLU C 642
REMARK 465 SER C 643
REMARK 465 SER C 644
REMARK 465 LEU C 645
REMARK 465 PRO C 646
REMARK 465 SER C 647
REMARK 465 ALA C 648
REMARK 465 SER C 649
REMARK 465 LYS C 650
REMARK 465 THR C 651
REMARK 465 LYS C 652
REMARK 465 LYS C 653
REMARK 465 GLY C 654
REMARK 465 MET C 655
REMARK 465 PHE C 656
REMARK 465 LEU C 790
REMARK 465 LYS C 791
REMARK 465 ILE C 792
REMARK 465 ALA D 2
REMARK 465 GLN D 3
REMARK 465 LYS D 4
REMARK 465 PRO D 5
REMARK 465 LEU D 6
REMARK 465 SER D 7
REMARK 465 ASP D 8
REMARK 465 ASP D 9
REMARK 465 GLU D 10
REMARK 465 LYS D 11
REMARK 465 PHE D 12
REMARK 465 LEU D 13
REMARK 465 PHE D 14
REMARK 465 VAL D 15
REMARK 465 ASP D 16
REMARK 465 LYS D 17
REMARK 465 ASN D 18
REMARK 465 PHE D 19
REMARK 465 VAL D 20
REMARK 465 ASN D 21
REMARK 465 ASN D 22
REMARK 465 PRO D 23
REMARK 465 LEU D 24
REMARK 465 ALA D 25
REMARK 465 GLN D 26
REMARK 465 ALA D 27
REMARK 465 ASP D 28
REMARK 465 TRP D 29
REMARK 465 SER D 30
REMARK 465 ALA D 31
REMARK 465 LYS D 32
REMARK 465 LYS D 33
REMARK 465 LYS D 50
REMARK 465 GLU D 51
REMARK 465 GLU D 52
REMARK 465 LYS D 53
REMARK 465 GLY D 54
REMARK 465 ASP D 55
REMARK 465 SER D 200
REMARK 465 HIS D 201
REMARK 465 LYS D 202
REMARK 465 GLY D 203
REMARK 465 LYS D 204
REMARK 465 LYS D 205
REMARK 465 ASP D 206
REMARK 465 THR D 207
REMARK 465 SER D 208
REMARK 465 ILE D 209
REMARK 465 THR D 210
REMARK 465 GLN D 211
REMARK 465 GLY D 212
REMARK 465 PRO D 213
REMARK 465 SER D 214
REMARK 465 PHE D 215
REMARK 465 SER D 216
REMARK 465 TYR D 217
REMARK 465 ARG D 371
REMARK 465 ASN D 372
REMARK 465 THR D 373
REMARK 465 ASP D 374
REMARK 465 ARG D 406
REMARK 465 ILE D 407
REMARK 465 LYS D 408
REMARK 465 VAL D 409
REMARK 465 GLY D 410
REMARK 465 ARG D 411
REMARK 465 ASP D 412
REMARK 465 VAL D 413
REMARK 465 VAL D 414
REMARK 465 GLN D 415
REMARK 465 LYS D 452
REMARK 465 THR D 453
REMARK 465 LYS D 454
REMARK 465 ARG D 455
REMARK 465 GLN D 456
REMARK 465 GLY D 457
REMARK 465 TRP D 546
REMARK 465 PHE D 547
REMARK 465 PRO D 548
REMARK 465 LYS D 549
REMARK 465 LYS D 573
REMARK 465 GLN D 574
REMARK 465 LEU D 575
REMARK 465 LYS D 576
REMARK 465 ASP D 577
REMARK 465 ASP D 627
REMARK 465 VAL D 628
REMARK 465 ASP D 629
REMARK 465 ARG D 630
REMARK 465 ILE D 631
REMARK 465 VAL D 632
REMARK 465 GLY D 633
REMARK 465 LEU D 634
REMARK 465 ASP D 635
REMARK 465 GLN D 636
REMARK 465 MET D 637
REMARK 465 ALA D 638
REMARK 465 LYS D 639
REMARK 465 MET D 640
REMARK 465 THR D 641
REMARK 465 GLU D 642
REMARK 465 SER D 643
REMARK 465 SER D 644
REMARK 465 LEU D 645
REMARK 465 PRO D 646
REMARK 465 SER D 647
REMARK 465 ALA D 648
REMARK 465 SER D 649
REMARK 465 LYS D 650
REMARK 465 THR D 651
REMARK 465 LYS D 652
REMARK 465 LYS D 653
REMARK 465 GLY D 654
REMARK 465 MET D 655
REMARK 465 PHE D 656
REMARK 465 LEU D 790
REMARK 465 LYS D 791
REMARK 465 ILE D 792
REMARK 465 ALA E 2
REMARK 465 GLN E 3
REMARK 465 LYS E 4
REMARK 465 PRO E 5
REMARK 465 LEU E 6
REMARK 465 SER E 7
REMARK 465 ASP E 8
REMARK 465 ASP E 9
REMARK 465 GLU E 10
REMARK 465 LYS E 11
REMARK 465 PHE E 12
REMARK 465 LEU E 13
REMARK 465 PHE E 14
REMARK 465 VAL E 15
REMARK 465 ASP E 16
REMARK 465 LYS E 17
REMARK 465 ASN E 18
REMARK 465 PHE E 19
REMARK 465 VAL E 20
REMARK 465 ASN E 21
REMARK 465 ASN E 22
REMARK 465 PRO E 23
REMARK 465 LEU E 24
REMARK 465 ALA E 25
REMARK 465 GLN E 26
REMARK 465 ALA E 27
REMARK 465 ASP E 28
REMARK 465 TRP E 29
REMARK 465 SER E 30
REMARK 465 ALA E 31
REMARK 465 LYS E 32
REMARK 465 LYS E 33
REMARK 465 LYS E 50
REMARK 465 GLU E 51
REMARK 465 GLU E 52
REMARK 465 LYS E 53
REMARK 465 GLY E 54
REMARK 465 ASP E 55
REMARK 465 SER E 200
REMARK 465 HIS E 201
REMARK 465 LYS E 202
REMARK 465 GLY E 203
REMARK 465 LYS E 204
REMARK 465 LYS E 205
REMARK 465 ASP E 206
REMARK 465 THR E 207
REMARK 465 SER E 208
REMARK 465 ILE E 209
REMARK 465 THR E 210
REMARK 465 GLN E 211
REMARK 465 GLY E 212
REMARK 465 PRO E 213
REMARK 465 SER E 214
REMARK 465 PHE E 215
REMARK 465 SER E 216
REMARK 465 TYR E 217
REMARK 465 ARG E 371
REMARK 465 ASN E 372
REMARK 465 THR E 373
REMARK 465 ASP E 374
REMARK 465 ARG E 406
REMARK 465 ILE E 407
REMARK 465 LYS E 408
REMARK 465 VAL E 409
REMARK 465 GLY E 410
REMARK 465 ARG E 411
REMARK 465 ASP E 412
REMARK 465 VAL E 413
REMARK 465 VAL E 414
REMARK 465 GLN E 415
REMARK 465 LYS E 452
REMARK 465 THR E 453
REMARK 465 LYS E 454
REMARK 465 ARG E 455
REMARK 465 GLN E 456
REMARK 465 GLY E 457
REMARK 465 TRP E 546
REMARK 465 PHE E 547
REMARK 465 PRO E 548
REMARK 465 LYS E 549
REMARK 465 LYS E 573
REMARK 465 GLN E 574
REMARK 465 LEU E 575
REMARK 465 LYS E 576
REMARK 465 ASP E 577
REMARK 465 ASP E 627
REMARK 465 VAL E 628
REMARK 465 ASP E 629
REMARK 465 ARG E 630
REMARK 465 ILE E 631
REMARK 465 VAL E 632
REMARK 465 GLY E 633
REMARK 465 LEU E 634
REMARK 465 ASP E 635
REMARK 465 GLN E 636
REMARK 465 MET E 637
REMARK 465 ALA E 638
REMARK 465 LYS E 639
REMARK 465 MET E 640
REMARK 465 THR E 641
REMARK 465 GLU E 642
REMARK 465 SER E 643
REMARK 465 SER E 644
REMARK 465 LEU E 645
REMARK 465 PRO E 646
REMARK 465 SER E 647
REMARK 465 ALA E 648
REMARK 465 SER E 649
REMARK 465 LYS E 650
REMARK 465 THR E 651
REMARK 465 LYS E 652
REMARK 465 LYS E 653
REMARK 465 GLY E 654
REMARK 465 MET E 655
REMARK 465 PHE E 656
REMARK 465 LEU E 790
REMARK 465 LYS E 791
REMARK 465 ILE E 792
REMARK 465 ALA F 2
REMARK 465 GLN F 3
REMARK 465 LYS F 4
REMARK 465 PRO F 5
REMARK 465 LEU F 6
REMARK 465 SER F 7
REMARK 465 ASP F 8
REMARK 465 ASP F 9
REMARK 465 GLU F 10
REMARK 465 LYS F 11
REMARK 465 PHE F 12
REMARK 465 LEU F 13
REMARK 465 PHE F 14
REMARK 465 VAL F 15
REMARK 465 ASP F 16
REMARK 465 LYS F 17
REMARK 465 ASN F 18
REMARK 465 PHE F 19
REMARK 465 VAL F 20
REMARK 465 ASN F 21
REMARK 465 ASN F 22
REMARK 465 PRO F 23
REMARK 465 LEU F 24
REMARK 465 ALA F 25
REMARK 465 GLN F 26
REMARK 465 ALA F 27
REMARK 465 ASP F 28
REMARK 465 TRP F 29
REMARK 465 SER F 30
REMARK 465 ALA F 31
REMARK 465 LYS F 32
REMARK 465 LYS F 33
REMARK 465 LYS F 50
REMARK 465 GLU F 51
REMARK 465 GLU F 52
REMARK 465 LYS F 53
REMARK 465 GLY F 54
REMARK 465 ASP F 55
REMARK 465 SER F 200
REMARK 465 HIS F 201
REMARK 465 LYS F 202
REMARK 465 GLY F 203
REMARK 465 LYS F 204
REMARK 465 LYS F 205
REMARK 465 ASP F 206
REMARK 465 THR F 207
REMARK 465 SER F 208
REMARK 465 ILE F 209
REMARK 465 THR F 210
REMARK 465 GLN F 211
REMARK 465 GLY F 212
REMARK 465 PRO F 213
REMARK 465 SER F 214
REMARK 465 PHE F 215
REMARK 465 SER F 216
REMARK 465 TYR F 217
REMARK 465 ARG F 371
REMARK 465 ASN F 372
REMARK 465 THR F 373
REMARK 465 ASP F 374
REMARK 465 ARG F 406
REMARK 465 ILE F 407
REMARK 465 LYS F 408
REMARK 465 VAL F 409
REMARK 465 GLY F 410
REMARK 465 ARG F 411
REMARK 465 ASP F 412
REMARK 465 VAL F 413
REMARK 465 VAL F 414
REMARK 465 GLN F 415
REMARK 465 LYS F 452
REMARK 465 THR F 453
REMARK 465 LYS F 454
REMARK 465 ARG F 455
REMARK 465 GLN F 456
REMARK 465 GLY F 457
REMARK 465 TRP F 546
REMARK 465 PHE F 547
REMARK 465 PRO F 548
REMARK 465 LYS F 549
REMARK 465 LYS F 573
REMARK 465 GLN F 574
REMARK 465 LEU F 575
REMARK 465 LYS F 576
REMARK 465 ASP F 577
REMARK 465 ASP F 627
REMARK 465 VAL F 628
REMARK 465 ASP F 629
REMARK 465 ARG F 630
REMARK 465 ILE F 631
REMARK 465 VAL F 632
REMARK 465 GLY F 633
REMARK 465 LEU F 634
REMARK 465 ASP F 635
REMARK 465 GLN F 636
REMARK 465 MET F 637
REMARK 465 ALA F 638
REMARK 465 LYS F 639
REMARK 465 MET F 640
REMARK 465 THR F 641
REMARK 465 GLU F 642
REMARK 465 SER F 643
REMARK 465 SER F 644
REMARK 465 LEU F 645
REMARK 465 PRO F 646
REMARK 465 SER F 647
REMARK 465 ALA F 648
REMARK 465 SER F 649
REMARK 465 LYS F 650
REMARK 465 THR F 651
REMARK 465 LYS F 652
REMARK 465 LYS F 653
REMARK 465 GLY F 654
REMARK 465 MET F 655
REMARK 465 PHE F 656
REMARK 465 LEU F 790
REMARK 465 LYS F 791
REMARK 465 ILE F 792
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 GLU A 56 CG CD OE1 OE2
REMARK 470 GLU A 60 CG CD OE1 OE2
REMARK 470 GLN A 62 CG CD OE1 NE2
REMARK 470 GLU A 63 CG CD OE1 OE2
REMARK 470 ASN A 64 CG OD1 ND2
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 VAL A 68 CG1 CG2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 ASP A 73 CG OD1 OD2
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 GLU A 221 CG CD OE1 OE2
REMARK 470 LYS A 222 CG CD CE NZ
REMARK 470 TYR A 261 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 300 CG CD OE1 NE2
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 LYS A 369 CG CD CE NZ
REMARK 470 GLU A 370 CG CD OE1 OE2
REMARK 470 GLN A 375 CG CD OE1 NE2
REMARK 470 LYS A 416 CG CD CE NZ
REMARK 470 GLU A 421 CG CD OE1 OE2
REMARK 470 GLU A 543 CG CD OE1 OE2
REMARK 470 THR A 551 OG1 CG2
REMARK 470 GLU A 557 CG CD OE1 OE2
REMARK 470 LYS A 558 CG CD CE NZ
REMARK 470 LYS A 571 CG CD CE NZ
REMARK 470 LYS A 578 CG CD CE NZ
REMARK 470 LYS A 619 CG CD CE NZ
REMARK 470 LYS A 626 CG CD CE NZ
REMARK 470 ARG A 657 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 665 CG CD OE1 OE2
REMARK 470 GLU A 703 CG CD OE1 OE2
REMARK 470 ILE A 736 CG1 CG2 CD1
REMARK 470 LYS A 744 CG CD CE NZ
REMARK 470 LYS A 758 CG CD CE NZ
REMARK 470 GLU A 787 CG CD OE1 OE2
REMARK 470 ASP A 789 CG OD1 OD2
REMARK 470 GLU B 56 CG CD OE1 OE2
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 GLN B 62 CG CD OE1 NE2
REMARK 470 GLU B 63 CG CD OE1 OE2
REMARK 470 ASN B 64 CG OD1 ND2
REMARK 470 LYS B 66 CG CD CE NZ
REMARK 470 VAL B 68 CG1 CG2
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 ASP B 73 CG OD1 OD2
REMARK 470 GLU B 219 CG CD OE1 OE2
REMARK 470 GLU B 221 CG CD OE1 OE2
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 TYR B 261 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 300 CG CD OE1 NE2
REMARK 470 LYS B 368 CG CD CE NZ
REMARK 470 LYS B 369 CG CD CE NZ
REMARK 470 GLU B 370 CG CD OE1 OE2
REMARK 470 GLN B 375 CG CD OE1 NE2
REMARK 470 LYS B 416 CG CD CE NZ
REMARK 470 GLU B 421 CG CD OE1 OE2
REMARK 470 GLU B 543 CG CD OE1 OE2
REMARK 470 THR B 551 OG1 CG2
REMARK 470 GLU B 557 CG CD OE1 OE2
REMARK 470 LYS B 558 CG CD CE NZ
REMARK 470 LYS B 571 CG CD CE NZ
REMARK 470 LYS B 578 CG CD CE NZ
REMARK 470 LYS B 619 CG CD CE NZ
REMARK 470 LYS B 626 CG CD CE NZ
REMARK 470 ARG B 657 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 665 CG CD OE1 OE2
REMARK 470 GLU B 703 CG CD OE1 OE2
REMARK 470 ILE B 736 CG1 CG2 CD1
REMARK 470 LYS B 744 CG CD CE NZ
REMARK 470 LYS B 758 CG CD CE NZ
REMARK 470 GLU B 787 CG CD OE1 OE2
REMARK 470 ASP B 789 CG OD1 OD2
REMARK 470 GLU C 56 CG CD OE1 OE2
REMARK 470 GLU C 60 CG CD OE1 OE2
REMARK 470 GLN C 62 CG CD OE1 NE2
REMARK 470 GLU C 63 CG CD OE1 OE2
REMARK 470 ASN C 64 CG OD1 ND2
REMARK 470 LYS C 66 CG CD CE NZ
REMARK 470 VAL C 68 CG1 CG2
REMARK 470 LYS C 72 CG CD CE NZ
REMARK 470 ASP C 73 CG OD1 OD2
REMARK 470 GLU C 219 CG CD OE1 OE2
REMARK 470 GLU C 221 CG CD OE1 OE2
REMARK 470 LYS C 222 CG CD CE NZ
REMARK 470 TYR C 261 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN C 300 CG CD OE1 NE2
REMARK 470 LYS C 368 CG CD CE NZ
REMARK 470 LYS C 369 CG CD CE NZ
REMARK 470 GLU C 370 CG CD OE1 OE2
REMARK 470 GLN C 375 CG CD OE1 NE2
REMARK 470 LYS C 416 CG CD CE NZ
REMARK 470 GLU C 421 CG CD OE1 OE2
REMARK 470 GLU C 543 CG CD OE1 OE2
REMARK 470 THR C 551 OG1 CG2
REMARK 470 GLU C 557 CG CD OE1 OE2
REMARK 470 LYS C 558 CG CD CE NZ
REMARK 470 LYS C 571 CG CD CE NZ
REMARK 470 LYS C 578 CG CD CE NZ
REMARK 470 LYS C 619 CG CD CE NZ
REMARK 470 LYS C 626 CG CD CE NZ
REMARK 470 ARG C 657 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 665 CG CD OE1 OE2
REMARK 470 GLU C 703 CG CD OE1 OE2
REMARK 470 ILE C 736 CG1 CG2 CD1
REMARK 470 LYS C 744 CG CD CE NZ
REMARK 470 LYS C 758 CG CD CE NZ
REMARK 470 GLU C 787 CG CD OE1 OE2
REMARK 470 ASP C 789 CG OD1 OD2
REMARK 470 GLU D 56 CG CD OE1 OE2
REMARK 470 GLU D 60 CG CD OE1 OE2
REMARK 470 GLN D 62 CG CD OE1 NE2
REMARK 470 GLU D 63 CG CD OE1 OE2
REMARK 470 ASN D 64 CG OD1 ND2
REMARK 470 LYS D 66 CG CD CE NZ
REMARK 470 VAL D 68 CG1 CG2
REMARK 470 LYS D 72 CG CD CE NZ
REMARK 470 ASP D 73 CG OD1 OD2
REMARK 470 GLU D 219 CG CD OE1 OE2
REMARK 470 GLU D 221 CG CD OE1 OE2
REMARK 470 LYS D 222 CG CD CE NZ
REMARK 470 TYR D 261 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN D 300 CG CD OE1 NE2
REMARK 470 LYS D 368 CG CD CE NZ
REMARK 470 LYS D 369 CG CD CE NZ
REMARK 470 GLU D 370 CG CD OE1 OE2
REMARK 470 GLN D 375 CG CD OE1 NE2
REMARK 470 LYS D 416 CG CD CE NZ
REMARK 470 GLU D 421 CG CD OE1 OE2
REMARK 470 GLU D 543 CG CD OE1 OE2
REMARK 470 THR D 551 OG1 CG2
REMARK 470 GLU D 557 CG CD OE1 OE2
REMARK 470 LYS D 558 CG CD CE NZ
REMARK 470 LYS D 571 CG CD CE NZ
REMARK 470 LYS D 578 CG CD CE NZ
REMARK 470 LYS D 619 CG CD CE NZ
REMARK 470 LYS D 626 CG CD CE NZ
REMARK 470 ARG D 657 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 665 CG CD OE1 OE2
REMARK 470 GLU D 703 CG CD OE1 OE2
REMARK 470 ILE D 736 CG1 CG2 CD1
REMARK 470 LYS D 744 CG CD CE NZ
REMARK 470 LYS D 758 CG CD CE NZ
REMARK 470 GLU D 787 CG CD OE1 OE2
REMARK 470 ASP D 789 CG OD1 OD2
REMARK 470 GLU E 56 CG CD OE1 OE2
REMARK 470 GLU E 60 CG CD OE1 OE2
REMARK 470 GLN E 62 CG CD OE1 NE2
REMARK 470 GLU E 63 CG CD OE1 OE2
REMARK 470 ASN E 64 CG OD1 ND2
REMARK 470 LYS E 66 CG CD CE NZ
REMARK 470 VAL E 68 CG1 CG2
REMARK 470 LYS E 72 CG CD CE NZ
REMARK 470 ASP E 73 CG OD1 OD2
REMARK 470 GLU E 219 CG CD OE1 OE2
REMARK 470 GLU E 221 CG CD OE1 OE2
REMARK 470 LYS E 222 CG CD CE NZ
REMARK 470 TYR E 261 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN E 300 CG CD OE1 NE2
REMARK 470 LYS E 368 CG CD CE NZ
REMARK 470 LYS E 369 CG CD CE NZ
REMARK 470 GLU E 370 CG CD OE1 OE2
REMARK 470 GLN E 375 CG CD OE1 NE2
REMARK 470 LYS E 416 CG CD CE NZ
REMARK 470 GLU E 421 CG CD OE1 OE2
REMARK 470 GLU E 543 CG CD OE1 OE2
REMARK 470 THR E 551 OG1 CG2
REMARK 470 GLU E 557 CG CD OE1 OE2
REMARK 470 LYS E 558 CG CD CE NZ
REMARK 470 LYS E 571 CG CD CE NZ
REMARK 470 LYS E 578 CG CD CE NZ
REMARK 470 LYS E 619 CG CD CE NZ
REMARK 470 LYS E 626 CG CD CE NZ
REMARK 470 ARG E 657 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 665 CG CD OE1 OE2
REMARK 470 GLU E 703 CG CD OE1 OE2
REMARK 470 ILE E 736 CG1 CG2 CD1
REMARK 470 LYS E 744 CG CD CE NZ
REMARK 470 LYS E 758 CG CD CE NZ
REMARK 470 GLU E 787 CG CD OE1 OE2
REMARK 470 ASP E 789 CG OD1 OD2
REMARK 470 GLU F 56 CG CD OE1 OE2
REMARK 470 GLU F 60 CG CD OE1 OE2
REMARK 470 GLN F 62 CG CD OE1 NE2
REMARK 470 GLU F 63 CG CD OE1 OE2
REMARK 470 ASN F 64 CG OD1 ND2
REMARK 470 LYS F 66 CG CD CE NZ
REMARK 470 VAL F 68 CG1 CG2
REMARK 470 LYS F 72 CG CD CE NZ
REMARK 470 ASP F 73 CG OD1 OD2
REMARK 470 GLU F 219 CG CD OE1 OE2
REMARK 470 GLU F 221 CG CD OE1 OE2
REMARK 470 LYS F 222 CG CD CE NZ
REMARK 470 TYR F 261 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN F 300 CG CD OE1 NE2
REMARK 470 LYS F 368 CG CD CE NZ
REMARK 470 LYS F 369 CG CD CE NZ
REMARK 470 GLU F 370 CG CD OE1 OE2
REMARK 470 GLN F 375 CG CD OE1 NE2
REMARK 470 LYS F 416 CG CD CE NZ
REMARK 470 GLU F 421 CG CD OE1 OE2
REMARK 470 GLU F 543 CG CD OE1 OE2
REMARK 470 THR F 551 OG1 CG2
REMARK 470 GLU F 557 CG CD OE1 OE2
REMARK 470 LYS F 558 CG CD CE NZ
REMARK 470 LYS F 571 CG CD CE NZ
REMARK 470 LYS F 578 CG CD CE NZ
REMARK 470 LYS F 619 CG CD CE NZ
REMARK 470 LYS F 626 CG CD CE NZ
REMARK 470 ARG F 657 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 665 CG CD OE1 OE2
REMARK 470 GLU F 703 CG CD OE1 OE2
REMARK 470 ILE F 736 CG1 CG2 CD1
REMARK 470 LYS F 744 CG CD CE NZ
REMARK 470 LYS F 758 CG CD CE NZ
REMARK 470 GLU F 787 CG CD OE1 OE2
REMARK 470 ASP F 789 CG OD1 OD2
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 184 OG1
REMARK 620 2 SER A 246 OG 93.7
REMARK 620 3 HOH A 995 O 100.6 80.9
REMARK 620 4 ADP A 998 O2B 90.5 174.1 94.3
REMARK 620 5 ALF A 999 F2 157.8 80.4 57.5 94.2
REMARK 620 6 ALF A 999 F4 142.3 113.7 108.7 64.6 57.6
REMARK 620 7 ALF A 999 AL 164.2 102.0 83.7 74.0 31.6 26.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ALF A 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 995 O
REMARK 620 2 ALF A 999 F1 143.0
REMARK 620 3 ALF A 999 F2 36.6 177.6
REMARK 620 4 ALF A 999 F3 120.2 88.4 90.6
REMARK 620 5 ALF A 999 F4 59.3 91.3 89.7 177.9
REMARK 620 6 ADP A 998 O2B 46.6 96.4 83.2 144.4 33.6
REMARK 620 7 ADP A 998 O3B 54.5 100.6 77.5 100.4 77.7 44.1
REMARK 620 8 ADP A 998 O1B 82.4 62.9 115.8 116.5 61.6 40.6 42.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 184 OG1
REMARK 620 2 SER B 246 OG 88.1
REMARK 620 3 HOH B 995 O 98.8 80.8
REMARK 620 4 ADP B 998 O2B 90.9 174.8 94.2
REMARK 620 5 ALF B 999 F2 156.0 84.6 57.5 94.2
REMARK 620 6 ALF B 999 F4 143.8 118.6 108.7 64.5 57.7
REMARK 620 7 ALF B 999 AL 164.9 107.0 83.7 74.0 31.6 26.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ALF B 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 468 N
REMARK 620 2 ALF B 999 F1 34.8
REMARK 620 3 ALF B 999 F2 147.5 177.5
REMARK 620 4 ALF B 999 F3 91.3 88.4 90.5
REMARK 620 5 ALF B 999 F4 89.6 91.3 89.8 177.9
REMARK 620 6 HOH B 995 O 147.1 143.0 36.6 120.2 59.3
REMARK 620 7 ADP B 998 O1B 92.1 62.8 115.8 116.5 61.6 82.4
REMARK 620 8 ADP B 998 O2B 112.4 96.4 83.2 144.4 33.6 46.6 40.6
REMARK 620 9 ADP B 998 O3B 133.8 100.5 77.5 100.4 77.6 54.5 42.7 44.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 184 OG1
REMARK 620 2 SER C 246 OG 92.2
REMARK 620 3 HOH C 995 O 104.1 84.3
REMARK 620 4 ADP C 998 O2B 89.9 177.7 94.4
REMARK 620 5 ALF C 999 F2 161.4 83.4 57.5 94.2
REMARK 620 6 ALF C 999 F4 139.4 114.1 108.7 64.6 57.6
REMARK 620 7 ALF C 999 AL 162.8 104.0 83.7 74.0 31.6 26.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ALF C 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 995 O
REMARK 620 2 ALF C 999 F1 143.0
REMARK 620 3 ALF C 999 F2 36.6 177.6
REMARK 620 4 ALF C 999 F3 120.2 88.4 90.5
REMARK 620 5 ALF C 999 F4 59.3 91.3 89.7 177.9
REMARK 620 6 ADP C 998 O3B 54.5 100.5 77.5 100.3 77.7
REMARK 620 7 ADP C 998 O1B 82.4 62.8 115.8 116.5 61.6 42.7
REMARK 620 8 ADP C 998 O2B 46.6 96.4 83.2 144.4 33.6 44.1 40.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 184 OG1
REMARK 620 2 SER D 246 OG 89.6
REMARK 620 3 HOH D 995 O 98.2 79.4
REMARK 620 4 ADP D 998 O2B 90.4 173.6 94.3
REMARK 620 5 ALF D 999 F2 155.5 83.2 57.5 94.2
REMARK 620 6 ALF D 999 F4 143.9 118.2 108.7 64.5 57.6
REMARK 620 7 ALF D 999 AL 164.4 105.9 83.8 74.0 31.6 26.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ALF D 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY D 468 N
REMARK 620 2 ALF D 999 F1 34.5
REMARK 620 3 ALF D 999 F2 147.7 177.6
REMARK 620 4 ALF D 999 F3 90.7 88.4 90.5
REMARK 620 5 ALF D 999 F4 90.2 91.3 89.7 177.9
REMARK 620 6 HOH D 995 O 147.7 143.0 36.7 120.2 59.3
REMARK 620 7 ADP D 998 O3B 133.7 100.5 77.5 100.4 77.7 54.5
REMARK 620 8 ADP D 998 O2B 112.8 96.4 83.2 144.4 33.6 46.6 44.1
REMARK 620 9 ADP D 998 O1B 92.2 62.8 115.8 116.5 61.6 82.4 42.7 40.6
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 184 OG1
REMARK 620 2 SER E 246 OG 93.4
REMARK 620 3 HOH E 995 O 94.3 79.4
REMARK 620 4 ADP E 998 O2B 87.2 165.8 86.4
REMARK 620 5 ALF E 999 F4 147.9 113.6 107.0 70.9
REMARK 620 6 ALF E 999 F2 153.5 82.0 59.2 91.1 53.4
REMARK 620 7 ALF E 999 AL 162.3 103.3 83.5 75.1 24.5 29.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ALF E 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP E 998 O2B
REMARK 620 2 ALF E 999 F1 95.5
REMARK 620 3 ALF E 999 F2 82.7 177.4
REMARK 620 4 ALF E 999 F3 139.1 90.3 89.8
REMARK 620 5 ALF E 999 F4 39.8 89.7 90.1 178.9
REMARK 620 6 ADP E 998 O3B 42.3 97.6 79.7 96.8 82.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 184 OG1
REMARK 620 2 SER F 246 OG 93.7
REMARK 620 3 HOH F 995 O 95.5 79.3
REMARK 620 4 ADP F 998 O2B 86.9 165.9 86.7
REMARK 620 5 ALF F 999 F2 154.7 81.1 59.2 92.3
REMARK 620 6 ALF F 999 F4 147.4 113.9 106.1 70.6 53.1
REMARK 620 7 ALF F 999 AL 162.4 103.2 83.1 75.6 29.7 24.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ALF F 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY F 468 N
REMARK 620 2 ALF F 999 F1 34.7
REMARK 620 3 ALF F 999 F2 147.5 177.7
REMARK 620 4 ALF F 999 F3 92.8 90.2 90.0
REMARK 620 5 ALF F 999 F4 87.9 89.8 90.0 178.6
REMARK 620 6 ADP F 998 O3B 131.3 97.8 79.9 99.0 79.6
REMARK 620 7 ADP F 998 O2B 113.4 95.2 83.2 140.3 38.3 41.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF C 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF D 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF E 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF F 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP F 998
DBREF 1BR2 A 3 792 UNP P10587 MYH11_CHICK 2 791
DBREF 1BR2 B 3 792 UNP P10587 MYH11_CHICK 2 791
DBREF 1BR2 C 3 792 UNP P10587 MYH11_CHICK 2 791
DBREF 1BR2 D 3 792 UNP P10587 MYH11_CHICK 2 791
DBREF 1BR2 E 3 792 UNP P10587 MYH11_CHICK 2 791
DBREF 1BR2 F 3 792 UNP P10587 MYH11_CHICK 2 791
SEQRES 1 A 791 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 A 791 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 A 791 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 A 791 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 A 791 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 A 791 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 A 791 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 A 791 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 A 791 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 A 791 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 A 791 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 A 791 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 A 791 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 A 791 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 A 791 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 A 791 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 A 791 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 A 791 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 A 791 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 A 791 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 A 791 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 A 791 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 A 791 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 A 791 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 A 791 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 A 791 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 A 791 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 A 791 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 A 791 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 A 791 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 A 791 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 A 791 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 A 791 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 A 791 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 A 791 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 A 791 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 A 791 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 A 791 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 A 791 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 A 791 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 A 791 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 A 791 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 A 791 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 A 791 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 A 791 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 A 791 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 A 791 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 A 791 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 A 791 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 A 791 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 A 791 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 A 791 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 A 791 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 A 791 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 A 791 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 A 791 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 A 791 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 A 791 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 A 791 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 A 791 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 A 791 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE
SEQRES 1 B 791 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 B 791 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 B 791 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 B 791 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 B 791 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 B 791 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 B 791 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 B 791 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 B 791 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 B 791 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 B 791 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 B 791 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 B 791 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 B 791 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 B 791 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 B 791 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 B 791 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 B 791 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 B 791 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 B 791 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 B 791 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 B 791 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 B 791 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 B 791 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 B 791 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 B 791 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 B 791 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 B 791 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 B 791 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 B 791 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 B 791 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 B 791 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 B 791 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 B 791 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 B 791 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 B 791 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 B 791 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 B 791 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 B 791 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 B 791 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 B 791 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 B 791 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 B 791 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 B 791 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 B 791 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 B 791 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 B 791 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 B 791 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 B 791 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 B 791 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 B 791 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 B 791 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 B 791 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 B 791 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 B 791 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 B 791 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 B 791 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 B 791 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 B 791 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 B 791 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 B 791 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE
SEQRES 1 C 791 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 C 791 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 C 791 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 C 791 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 C 791 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 C 791 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 C 791 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 C 791 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 C 791 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 C 791 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 C 791 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 C 791 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 C 791 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 C 791 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 C 791 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 C 791 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 C 791 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 C 791 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 C 791 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 C 791 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 C 791 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 C 791 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 C 791 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 C 791 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 C 791 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 C 791 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 C 791 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 C 791 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 C 791 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 C 791 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 C 791 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 C 791 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 C 791 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 C 791 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 C 791 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 C 791 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 C 791 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 C 791 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 C 791 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 C 791 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 C 791 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 C 791 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 C 791 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 C 791 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 C 791 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 C 791 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 C 791 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 C 791 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 C 791 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 C 791 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 C 791 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 C 791 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 C 791 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 C 791 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 C 791 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 C 791 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 C 791 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 C 791 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 C 791 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 C 791 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 C 791 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE
SEQRES 1 D 791 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 D 791 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 D 791 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 D 791 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 D 791 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 D 791 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 D 791 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 D 791 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 D 791 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 D 791 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 D 791 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 D 791 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 D 791 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 D 791 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 D 791 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 D 791 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 D 791 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 D 791 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 D 791 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 D 791 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 D 791 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 D 791 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 D 791 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 D 791 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 D 791 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 D 791 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 D 791 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 D 791 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 D 791 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 D 791 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 D 791 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 D 791 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 D 791 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 D 791 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 D 791 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 D 791 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 D 791 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 D 791 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 D 791 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 D 791 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 D 791 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 D 791 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 D 791 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 D 791 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 D 791 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 D 791 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 D 791 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 D 791 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 D 791 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 D 791 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 D 791 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 D 791 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 D 791 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 D 791 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 D 791 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 D 791 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 D 791 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 D 791 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 D 791 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 D 791 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 D 791 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE
SEQRES 1 E 791 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 E 791 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 E 791 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 E 791 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 E 791 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 E 791 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 E 791 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 E 791 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 E 791 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 E 791 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 E 791 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 E 791 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 E 791 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 E 791 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 E 791 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 E 791 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 E 791 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 E 791 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 E 791 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 E 791 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 E 791 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 E 791 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 E 791 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 E 791 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 E 791 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 E 791 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 E 791 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 E 791 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 E 791 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 E 791 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 E 791 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 E 791 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 E 791 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 E 791 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 E 791 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 E 791 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 E 791 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 E 791 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 E 791 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 E 791 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 E 791 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 E 791 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 E 791 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 E 791 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 E 791 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 E 791 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 E 791 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 E 791 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 E 791 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 E 791 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 E 791 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 E 791 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 E 791 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 E 791 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 E 791 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 E 791 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 E 791 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 E 791 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 E 791 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 E 791 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 E 791 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE
SEQRES 1 F 791 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 F 791 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 F 791 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 F 791 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 F 791 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 F 791 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 F 791 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 F 791 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 F 791 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 F 791 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 F 791 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 F 791 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 F 791 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 F 791 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 F 791 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 F 791 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 F 791 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 F 791 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 F 791 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 F 791 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 F 791 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 F 791 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 F 791 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 F 791 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 F 791 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 F 791 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 F 791 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 F 791 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 F 791 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 F 791 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 F 791 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 F 791 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 F 791 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 F 791 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 F 791 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 F 791 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 F 791 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 F 791 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 F 791 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 F 791 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 F 791 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 F 791 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 F 791 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 F 791 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 F 791 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 F 791 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 F 791 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 F 791 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 F 791 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 F 791 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 F 791 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 F 791 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 F 791 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 F 791 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 F 791 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 F 791 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 F 791 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 F 791 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 F 791 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 F 791 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 F 791 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE
HET MG A 997 1
HET ALF A 999 5
HET ADP A 998 27
HET MG B 997 1
HET ALF B 999 5
HET ADP B 998 27
HET MG C 997 1
HET ALF C 999 5
HET ADP C 998 27
HET MG D 997 1
HET ALF D 999 5
HET ADP D 998 27
HET MG E 997 1
HET ALF E 999 5
HET ADP E 998 27
HET MG F 997 1
HET ALF F 999 5
HET ADP F 998 27
HETNAM MG MAGNESIUM ION
HETNAM ALF TETRAFLUOROALUMINATE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 7 MG 6(MG 2+)
FORMUL 8 ALF 6(AL F4 1-)
FORMUL 9 ADP 6(C10 H15 N5 O10 P2)
FORMUL 25 HOH *12(H2 O)
HELIX 1 1 PRO A 81 PHE A 83 5 3
HELIX 2 2 GLU A 97 PHE A 109 1 13
HELIX 3 3 GLU A 135 MET A 140 1 6
HELIX 4 4 ARG A 146 GLU A 148 5 3
HELIX 5 5 ILE A 153 ASP A 167 1 15
HELIX 6 6 LYS A 183 ALA A 198 1 16
HELIX 7 7 GLU A 219 GLY A 235 1 17
HELIX 8 8 LYS A 274 ALA A 277 5 4
HELIX 9 9 HIS A 288 GLY A 296 1 9
HELIX 10 10 GLU A 299 ARG A 302 1 4
HELIX 11 11 ASP A 328 MET A 342 1 15
HELIX 12 12 GLU A 346 ASN A 364 1 19
HELIX 13 13 THR A 382 MET A 391 1 10
HELIX 14 14 VAL A 395 LEU A 403 1 9
HELIX 15 15 LYS A 420 LEU A 450 1 31
HELIX 16 16 PHE A 477 GLU A 508 1 32
HELIX 17 17 GLN A 522 GLU A 529 1 8
HELIX 18 18 VAL A 537 GLU A 544 1 8
HELIX 19 19 ASP A 552 GLU A 562 1 11
HELIX 20 20 TRP A 597 MET A 602 1 6
HELIX 21 21 ASP A 607 GLN A 615 1 9
HELIX 22 22 LYS A 619 LEU A 624 1 6
HELIX 23 23 VAL A 659 ASN A 676 1 18
HELIX 24 24 ALA A 698 CYS A 707 1 10
HELIX 25 25 VAL A 710 GLN A 719 1 10
HELIX 26 26 PHE A 727 ALA A 738 1 12
HELIX 27 27 GLY A 749 LEU A 760 1 12
HELIX 28 28 PRO A 764 LEU A 766 5 3
HELIX 29 29 VAL A 780 GLU A 787 1 8
HELIX 30 30 PRO B 81 PHE B 83 5 3
HELIX 31 31 GLU B 97 PHE B 109 1 13
HELIX 32 32 GLU B 135 MET B 140 1 6
HELIX 33 33 ARG B 146 GLU B 148 5 3
HELIX 34 34 ILE B 153 ASP B 167 1 15
HELIX 35 35 LYS B 183 ALA B 198 1 16
HELIX 36 36 GLU B 219 LEU B 224 1 6
HELIX 37 37 ALA B 227 GLY B 235 1 9
HELIX 38 38 LYS B 274 ALA B 277 5 4
HELIX 39 39 HIS B 288 GLY B 296 1 9
HELIX 40 40 GLU B 299 ARG B 302 1 4
HELIX 41 41 ASP B 328 MET B 342 1 15
HELIX 42 42 GLU B 346 ASN B 364 1 19
HELIX 43 43 THR B 382 MET B 391 1 10
HELIX 44 44 VAL B 395 LEU B 403 1 9
HELIX 45 45 LYS B 420 LEU B 450 1 31
HELIX 46 46 PHE B 477 GLU B 508 1 32
HELIX 47 47 GLN B 522 GLU B 529 1 8
HELIX 48 48 VAL B 537 GLU B 544 1 8
HELIX 49 49 ASP B 552 GLU B 562 1 11
HELIX 50 50 TRP B 597 MET B 602 1 6
HELIX 51 51 ASP B 607 GLN B 615 1 9
HELIX 52 52 LYS B 619 LEU B 624 1 6
HELIX 53 53 VAL B 659 ASN B 676 1 18
HELIX 54 54 ALA B 698 CYS B 707 1 10
HELIX 55 55 VAL B 710 GLN B 719 1 10
HELIX 56 56 PHE B 727 ALA B 738 1 12
HELIX 57 57 GLY B 749 LEU B 760 1 12
HELIX 58 58 PRO B 764 LEU B 766 5 3
HELIX 59 59 VAL B 780 GLU B 787 1 8
HELIX 60 60 PRO C 81 PHE C 83 5 3
HELIX 61 61 GLU C 97 PHE C 109 1 13
HELIX 62 62 GLU C 135 MET C 140 1 6
HELIX 63 63 ARG C 146 GLU C 148 5 3
HELIX 64 64 ILE C 153 ASP C 167 1 15
HELIX 65 65 LYS C 183 ALA C 198 1 16
HELIX 66 66 GLU C 219 LEU C 224 1 6
HELIX 67 67 ALA C 227 GLY C 235 1 9
HELIX 68 68 LYS C 274 ALA C 277 5 4
HELIX 69 69 HIS C 288 GLY C 296 1 9
HELIX 70 70 GLU C 299 ARG C 302 1 4
HELIX 71 71 ASP C 328 MET C 342 1 15
HELIX 72 72 GLU C 346 ASN C 364 1 19
HELIX 73 73 THR C 382 MET C 391 1 10
HELIX 74 74 VAL C 395 LEU C 403 1 9
HELIX 75 75 LYS C 420 LEU C 450 1 31
HELIX 76 76 PHE C 477 GLU C 508 1 32
HELIX 77 77 GLN C 522 GLU C 529 1 8
HELIX 78 78 VAL C 537 GLU C 544 1 8
HELIX 79 79 ASP C 552 GLU C 562 1 11
HELIX 80 80 TRP C 597 MET C 602 1 6
HELIX 81 81 ASP C 607 GLN C 615 1 9
HELIX 82 82 LYS C 619 LEU C 624 1 6
HELIX 83 83 VAL C 659 ASN C 676 1 18
HELIX 84 84 ALA C 698 CYS C 707 1 10
HELIX 85 85 VAL C 710 GLN C 719 1 10
HELIX 86 86 PHE C 727 ALA C 738 1 12
HELIX 87 87 GLY C 749 LEU C 760 1 12
HELIX 88 88 PRO C 764 LEU C 766 5 3
HELIX 89 89 VAL C 780 GLU C 787 1 8
HELIX 90 90 PRO D 81 PHE D 83 5 3
HELIX 91 91 GLU D 97 PHE D 109 1 13
HELIX 92 92 GLU D 135 MET D 140 1 6
HELIX 93 93 ARG D 146 GLU D 148 5 3
HELIX 94 94 ILE D 153 ASP D 167 1 15
HELIX 95 95 LYS D 183 ALA D 198 1 16
HELIX 96 96 GLU D 219 GLY D 235 1 17
HELIX 97 97 LYS D 274 ALA D 277 5 4
HELIX 98 98 HIS D 288 GLY D 296 1 9
HELIX 99 99 GLU D 299 ARG D 302 1 4
HELIX 100 100 ASP D 328 MET D 342 1 15
HELIX 101 101 GLU D 346 ASN D 364 1 19
HELIX 102 102 THR D 382 MET D 391 1 10
HELIX 103 103 VAL D 395 LEU D 403 1 9
HELIX 104 104 LYS D 420 LEU D 450 1 31
HELIX 105 105 PHE D 477 GLU D 508 1 32
HELIX 106 106 GLN D 522 GLU D 529 1 8
HELIX 107 107 VAL D 537 GLU D 544 1 8
HELIX 108 108 ASP D 552 GLU D 562 1 11
HELIX 109 109 TRP D 597 MET D 602 1 6
HELIX 110 110 ASP D 607 GLN D 615 1 9
HELIX 111 111 LYS D 619 LEU D 624 1 6
HELIX 112 112 VAL D 659 ASN D 676 1 18
HELIX 113 113 ALA D 698 CYS D 707 1 10
HELIX 114 114 VAL D 710 GLN D 719 1 10
HELIX 115 115 PHE D 727 ALA D 738 1 12
HELIX 116 116 GLY D 749 LEU D 760 1 12
HELIX 117 117 PRO D 764 LEU D 766 5 3
HELIX 118 118 VAL D 780 GLU D 787 1 8
HELIX 119 119 PRO E 81 PHE E 83 5 3
HELIX 120 120 GLU E 97 PHE E 109 1 13
HELIX 121 121 GLU E 135 MET E 140 1 6
HELIX 122 122 ARG E 146 GLU E 148 5 3
HELIX 123 123 ILE E 153 ASP E 167 1 15
HELIX 124 124 LYS E 183 ALA E 198 1 16
HELIX 125 125 GLU E 219 LEU E 224 1 6
HELIX 126 126 ALA E 227 GLY E 235 1 9
HELIX 127 127 LYS E 274 ALA E 277 5 4
HELIX 128 128 HIS E 288 GLY E 296 1 9
HELIX 129 129 GLU E 299 ARG E 302 1 4
HELIX 130 130 ASP E 328 MET E 342 1 15
HELIX 131 131 GLU E 346 ASN E 364 1 19
HELIX 132 132 THR E 382 MET E 391 1 10
HELIX 133 133 VAL E 395 LEU E 403 1 9
HELIX 134 134 LYS E 420 LEU E 450 1 31
HELIX 135 135 PHE E 477 GLU E 508 1 32
HELIX 136 136 GLN E 522 GLU E 529 1 8
HELIX 137 137 VAL E 537 GLU E 544 1 8
HELIX 138 138 ASP E 552 GLU E 562 1 11
HELIX 139 139 TRP E 597 MET E 602 1 6
HELIX 140 140 ASP E 607 GLN E 615 1 9
HELIX 141 141 LYS E 619 LEU E 624 1 6
HELIX 142 142 VAL E 659 ASN E 676 1 18
HELIX 143 143 ALA E 698 CYS E 707 1 10
HELIX 144 144 VAL E 710 GLN E 719 1 10
HELIX 145 145 PHE E 727 ALA E 738 1 12
HELIX 146 146 GLY E 749 LEU E 760 1 12
HELIX 147 147 PRO E 764 LEU E 766 5 3
HELIX 148 148 VAL E 780 GLU E 787 1 8
HELIX 149 149 PRO F 81 PHE F 83 5 3
HELIX 150 150 GLU F 97 PHE F 109 1 13
HELIX 151 151 GLU F 135 MET F 140 1 6
HELIX 152 152 ARG F 146 GLU F 148 5 3
HELIX 153 153 ILE F 153 ASP F 167 1 15
HELIX 154 154 LYS F 183 ALA F 198 1 16
HELIX 155 155 GLU F 219 LEU F 224 1 6
HELIX 156 156 ALA F 227 GLY F 235 1 9
HELIX 157 157 LYS F 274 ALA F 277 5 4
HELIX 158 158 HIS F 288 GLY F 296 1 9
HELIX 159 159 GLU F 299 ARG F 302 1 4
HELIX 160 160 ASP F 328 MET F 342 1 15
HELIX 161 161 GLU F 346 ASN F 364 1 19
HELIX 162 162 THR F 382 MET F 391 1 10
HELIX 163 163 VAL F 395 LEU F 403 1 9
HELIX 164 164 LYS F 420 LEU F 450 1 31
HELIX 165 165 PHE F 477 GLU F 508 1 32
HELIX 166 166 GLN F 522 GLU F 529 1 8
HELIX 167 167 VAL F 537 GLU F 544 1 8
HELIX 168 168 ASP F 552 GLU F 562 1 11
HELIX 169 169 TRP F 597 MET F 602 1 6
HELIX 170 170 ASP F 607 GLN F 615 1 9
HELIX 171 171 LYS F 619 LEU F 624 1 6
HELIX 172 172 VAL F 659 ASN F 676 1 18
HELIX 173 173 ALA F 698 CYS F 707 1 10
HELIX 174 174 VAL F 710 GLN F 719 1 10
HELIX 175 175 PHE F 727 ALA F 738 1 12
HELIX 176 176 GLY F 749 LEU F 760 1 12
HELIX 177 177 PRO F 764 LEU F 766 5 3
HELIX 178 178 VAL F 780 GLU F 787 1 8
SHEET 1 A 2 VAL A 35 PRO A 38 0
SHEET 2 A 2 PHE A 44 ALA A 47 -1 N ALA A 47 O VAL A 35
SHEET 1 B 2 VAL A 57 GLU A 60 0
SHEET 2 B 2 LYS A 67 LEU A 70 -1 N LEU A 70 O VAL A 57
SHEET 1 C 7 TYR A 114 TYR A 116 0
SHEET 2 C 7 CYS A 121 ILE A 124 -1 N VAL A 122 O THR A 115
SHEET 3 C 7 ASN A 678 ILE A 685 1 N ARG A 683 O CYS A 121
SHEET 4 C 7 GLN A 171 THR A 176 1 N SER A 172 O ASN A 678
SHEET 5 C 7 SER A 459 ASP A 465 1 N GLY A 462 O GLN A 171
SHEET 6 C 7 GLY A 249 PHE A 256 -1 N PHE A 256 O SER A 459
SHEET 7 C 7 ILE A 262 TYR A 270 -1 N TYR A 270 O GLY A 249
SHEET 1 D 3 PHE A 569 LYS A 571 0
SHEET 2 D 3 GLU A 580 HIS A 585 -1 N CYS A 582 O GLN A 570
SHEET 3 D 3 GLY A 588 ASN A 593 -1 N TYR A 592 O PHE A 581
SHEET 1 E 3 ASN A 723 VAL A 726 0
SHEET 2 E 3 LYS A 773 PHE A 776 -1 N PHE A 776 O ASN A 723
SHEET 3 E 3 TYR A 767 ILE A 769 -1 N ARG A 768 O PHE A 775
SHEET 1 F 2 VAL B 35 PRO B 38 0
SHEET 2 F 2 PHE B 44 ALA B 47 -1 N ALA B 47 O VAL B 35
SHEET 1 G 2 VAL B 57 GLU B 60 0
SHEET 2 G 2 LYS B 67 LEU B 70 -1 N LEU B 70 O VAL B 57
SHEET 1 H 7 TYR B 114 TYR B 116 0
SHEET 2 H 7 CYS B 121 ILE B 124 -1 N VAL B 122 O THR B 115
SHEET 3 H 7 ASN B 678 ILE B 685 1 N ARG B 683 O CYS B 121
SHEET 4 H 7 GLN B 171 THR B 176 1 N SER B 172 O ASN B 678
SHEET 5 H 7 SER B 459 ASP B 465 1 N GLY B 462 O GLN B 171
SHEET 6 H 7 GLY B 249 PHE B 256 -1 N PHE B 256 O SER B 459
SHEET 7 H 7 ILE B 262 TYR B 270 -1 N TYR B 270 O GLY B 249
SHEET 1 I 3 PHE B 569 LYS B 571 0
SHEET 2 I 3 GLU B 580 HIS B 585 -1 N CYS B 582 O GLN B 570
SHEET 3 I 3 GLY B 588 ASN B 593 -1 N TYR B 592 O PHE B 581
SHEET 1 J 3 ASN B 723 VAL B 726 0
SHEET 2 J 3 LYS B 773 PHE B 776 -1 N PHE B 776 O ASN B 723
SHEET 3 J 3 TYR B 767 ILE B 769 -1 N ARG B 768 O PHE B 775
SHEET 1 K 2 VAL C 35 PRO C 38 0
SHEET 2 K 2 PHE C 44 ALA C 47 -1 N ALA C 47 O VAL C 35
SHEET 1 L 2 VAL C 57 GLU C 60 0
SHEET 2 L 2 LYS C 67 LEU C 70 -1 N LEU C 70 O VAL C 57
SHEET 1 M 7 TYR C 114 TYR C 116 0
SHEET 2 M 7 CYS C 121 ILE C 124 -1 N VAL C 122 O THR C 115
SHEET 3 M 7 ASN C 678 ILE C 685 1 N ARG C 683 O CYS C 121
SHEET 4 M 7 GLN C 171 THR C 176 1 N SER C 172 O ASN C 678
SHEET 5 M 7 SER C 459 ASP C 465 1 N GLY C 462 O GLN C 171
SHEET 6 M 7 GLY C 249 PHE C 256 -1 N PHE C 256 O SER C 459
SHEET 7 M 7 ILE C 262 TYR C 270 -1 N TYR C 270 O GLY C 249
SHEET 1 N 3 PHE C 569 LYS C 571 0
SHEET 2 N 3 GLU C 580 HIS C 585 -1 N CYS C 582 O GLN C 570
SHEET 3 N 3 GLY C 588 ASN C 593 -1 N TYR C 592 O PHE C 581
SHEET 1 O 3 ASN C 723 VAL C 726 0
SHEET 2 O 3 LYS C 773 PHE C 776 -1 N PHE C 776 O ASN C 723
SHEET 3 O 3 TYR C 767 ILE C 769 -1 N ARG C 768 O PHE C 775
SHEET 1 P 2 VAL D 35 PRO D 38 0
SHEET 2 P 2 PHE D 44 ALA D 47 -1 N ALA D 47 O VAL D 35
SHEET 1 Q 2 VAL D 57 GLU D 60 0
SHEET 2 Q 2 LYS D 67 LEU D 70 -1 N LEU D 70 O VAL D 57
SHEET 1 R 7 TYR D 114 TYR D 116 0
SHEET 2 R 7 CYS D 121 ILE D 124 -1 N VAL D 122 O THR D 115
SHEET 3 R 7 ASN D 678 ILE D 685 1 N ARG D 683 O CYS D 121
SHEET 4 R 7 GLN D 171 THR D 176 1 N SER D 172 O ASN D 678
SHEET 5 R 7 SER D 459 ASP D 465 1 N GLY D 462 O GLN D 171
SHEET 6 R 7 GLY D 249 PHE D 256 -1 N PHE D 256 O SER D 459
SHEET 7 R 7 ILE D 262 TYR D 270 -1 N TYR D 270 O GLY D 249
SHEET 1 S 3 PHE D 569 LYS D 571 0
SHEET 2 S 3 GLU D 580 HIS D 585 -1 N CYS D 582 O GLN D 570
SHEET 3 S 3 GLY D 588 ASN D 593 -1 N TYR D 592 O PHE D 581
SHEET 1 T 3 ASN D 723 VAL D 726 0
SHEET 2 T 3 LYS D 773 PHE D 776 -1 N PHE D 776 O ASN D 723
SHEET 3 T 3 TYR D 767 ILE D 769 -1 N ARG D 768 O PHE D 775
SHEET 1 U 3 PHE E 44 ALA E 47 0
SHEET 2 U 3 VAL E 35 PRO E 38 -1 N VAL E 37 O GLU E 45
SHEET 3 U 3 ILE E 75 LYS E 77 -1 N GLN E 76 O TRP E 36
SHEET 1 V 2 VAL E 57 GLU E 60 0
SHEET 2 V 2 LYS E 67 LEU E 70 -1 N LEU E 70 O VAL E 57
SHEET 1 W 7 TYR E 114 TYR E 116 0
SHEET 2 W 7 CYS E 121 ILE E 124 -1 N VAL E 122 O THR E 115
SHEET 3 W 7 ASN E 678 ILE E 685 1 N ARG E 683 O CYS E 121
SHEET 4 W 7 GLN E 171 THR E 176 1 N SER E 172 O ASN E 678
SHEET 5 W 7 SER E 459 ASP E 465 1 N GLY E 462 O GLN E 171
SHEET 6 W 7 GLY E 249 PHE E 256 -1 N PHE E 256 O SER E 459
SHEET 7 W 7 ILE E 262 TYR E 270 -1 N TYR E 270 O GLY E 249
SHEET 1 X 3 PHE E 569 LYS E 571 0
SHEET 2 X 3 GLU E 580 HIS E 585 -1 N CYS E 582 O GLN E 570
SHEET 3 X 3 GLY E 588 ASN E 593 -1 N TYR E 592 O PHE E 581
SHEET 1 Y 3 ASN E 723 VAL E 726 0
SHEET 2 Y 3 LYS E 773 PHE E 776 -1 N PHE E 776 O ASN E 723
SHEET 3 Y 3 TYR E 767 ILE E 769 -1 N ARG E 768 O PHE E 775
SHEET 1 Z 2 VAL F 35 PRO F 38 0
SHEET 2 Z 2 PHE F 44 ALA F 47 -1 N ALA F 47 O VAL F 35
SHEET 1 AA 2 VAL F 57 GLU F 60 0
SHEET 2 AA 2 LYS F 67 LEU F 70 -1 N LEU F 70 O VAL F 57
SHEET 1 AB 7 TYR F 114 TYR F 116 0
SHEET 2 AB 7 CYS F 121 ILE F 124 -1 N VAL F 122 O THR F 115
SHEET 3 AB 7 ASN F 678 ILE F 685 1 N ARG F 683 O CYS F 121
SHEET 4 AB 7 GLN F 171 THR F 176 1 N SER F 172 O ASN F 678
SHEET 5 AB 7 SER F 459 ASP F 465 1 N GLY F 462 O GLN F 171
SHEET 6 AB 7 GLY F 249 PHE F 256 -1 N PHE F 256 O SER F 459
SHEET 7 AB 7 ILE F 262 TYR F 270 -1 N TYR F 270 O GLY F 249
SHEET 1 AC 3 PHE F 569 LYS F 571 0
SHEET 2 AC 3 GLU F 580 HIS F 585 -1 N CYS F 582 O GLN F 570
SHEET 3 AC 3 GLY F 588 ASN F 593 -1 N TYR F 592 O PHE F 581
SHEET 1 AD 3 ASN F 723 VAL F 726 0
SHEET 2 AD 3 LYS F 773 PHE F 776 -1 N PHE F 776 O ASN F 723
SHEET 3 AD 3 TYR F 767 ILE F 769 -1 N ARG F 768 O PHE F 775
LINK OG1 THR A 184 MG MG A 997 1555 1555 2.01
LINK OG SER A 246 MG MG A 997 1555 1555 2.39
LINK O HOH A 995 MG MG A 997 1555 1555 1.84
LINK O HOH A 995 AL ALF A 999 1555 1555 3.71
LINK MG MG A 997 O2B ADP A 998 1555 1555 2.04
LINK MG MG A 997 F2 ALF A 999 1555 1555 2.96
LINK MG MG A 997 F4 ALF A 999 1555 1555 2.09
LINK MG MG A 997 AL ALF A 999 1555 1555 3.43
LINK O2B ADP A 998 AL ALF A 999 1555 1555 3.48
LINK O3B ADP A 998 AL ALF A 999 1555 1555 2.08
LINK O1B ADP A 998 AL ALF A 999 1555 1555 3.59
LINK OG1 THR B 184 MG MG B 997 1555 1555 2.18
LINK OG SER B 246 MG MG B 997 1555 1555 2.47
LINK N GLY B 468 AL ALF B 999 1555 1555 3.69
LINK O HOH B 995 MG MG B 997 1555 1555 1.84
LINK O HOH B 995 AL ALF B 999 1555 1555 3.71
LINK MG MG B 997 O2B ADP B 998 1555 1555 2.04
LINK MG MG B 997 F2 ALF B 999 1555 1555 2.96
LINK MG MG B 997 F4 ALF B 999 1555 1555 2.09
LINK MG MG B 997 AL ALF B 999 1555 1555 3.43
LINK O1B ADP B 998 AL ALF B 999 1555 1555 3.59
LINK O2B ADP B 998 AL ALF B 999 1555 1555 3.48
LINK O3B ADP B 998 AL ALF B 999 1555 1555 2.08
LINK OG1 THR C 184 MG MG C 997 1555 1555 2.07
LINK OG SER C 246 MG MG C 997 1555 1555 2.39
LINK O HOH C 995 MG MG C 997 1555 1555 1.84
LINK O HOH C 995 AL ALF C 999 1555 1555 3.71
LINK MG MG C 997 O2B ADP C 998 1555 1555 2.04
LINK MG MG C 997 F2 ALF C 999 1555 1555 2.96
LINK MG MG C 997 F4 ALF C 999 1555 1555 2.09
LINK MG MG C 997 AL ALF C 999 1555 1555 3.43
LINK O3B ADP C 998 AL ALF C 999 1555 1555 2.08
LINK O1B ADP C 998 AL ALF C 999 1555 1555 3.59
LINK O2B ADP C 998 AL ALF C 999 1555 1555 3.48
LINK OG1 THR D 184 MG MG D 997 1555 1555 2.15
LINK OG SER D 246 MG MG D 997 1555 1555 2.40
LINK N GLY D 468 AL ALF D 999 1555 1555 3.66
LINK O HOH D 995 MG MG D 997 1555 1555 1.84
LINK O HOH D 995 AL ALF D 999 1555 1555 3.71
LINK MG MG D 997 O2B ADP D 998 1555 1555 2.04
LINK MG MG D 997 F2 ALF D 999 1555 1555 2.96
LINK MG MG D 997 F4 ALF D 999 1555 1555 2.09
LINK MG MG D 997 AL ALF D 999 1555 1555 3.43
LINK O3B ADP D 998 AL ALF D 999 1555 1555 2.08
LINK O2B ADP D 998 AL ALF D 999 1555 1555 3.48
LINK O1B ADP D 998 AL ALF D 999 1555 1555 3.59
LINK OG1 THR E 184 MG MG E 997 1555 1555 2.08
LINK OG SER E 246 MG MG E 997 1555 1555 2.37
LINK O HOH E 995 MG MG E 997 1555 1555 2.06
LINK MG MG E 997 O2B ADP E 998 1555 1555 2.24
LINK MG MG E 997 F4 ALF E 999 1555 1555 2.18
LINK MG MG E 997 F2 ALF E 999 1555 1555 3.10
LINK MG MG E 997 AL ALF E 999 1555 1555 3.54
LINK O2B ADP E 998 AL ALF E 999 1555 1555 3.67
LINK O3B ADP E 998 AL ALF E 999 1555 1555 2.56
LINK OG1 THR F 184 MG MG F 997 1555 1555 2.07
LINK OG SER F 246 MG MG F 997 1555 1555 2.35
LINK N GLY F 468 AL ALF F 999 1555 1555 3.70
LINK O HOH F 995 MG MG F 997 1555 1555 2.07
LINK MG MG F 997 O2B ADP F 998 1555 1555 2.19
LINK MG MG F 997 F2 ALF F 999 1555 1555 3.12
LINK MG MG F 997 F4 ALF F 999 1555 1555 2.18
LINK MG MG F 997 AL ALF F 999 1555 1555 3.55
LINK O3B ADP F 998 AL ALF F 999 1555 1555 2.53
LINK O2B ADP F 998 AL ALF F 999 1555 1555 3.68
SITE 1 AC1 6 THR A 184 SER A 246 ASP A 465 HOH A 995
SITE 2 AC1 6 ADP A 998 ALF A 999
SITE 1 AC2 10 SER A 179 LYS A 183 SER A 245 SER A 246
SITE 2 AC2 10 ASP A 465 ILE A 466 GLY A 468 HOH A 995
SITE 3 AC2 10 MG A 997 ADP A 998
SITE 1 AC3 6 THR B 184 SER B 246 ASP B 465 HOH B 995
SITE 2 AC3 6 ADP B 998 ALF B 999
SITE 1 AC4 11 SER B 179 LYS B 183 SER B 245 SER B 246
SITE 2 AC4 11 ASP B 465 ILE B 466 ALA B 467 GLY B 468
SITE 3 AC4 11 HOH B 995 MG B 997 ADP B 998
SITE 1 AC5 6 THR C 184 SER C 246 ASP C 465 HOH C 995
SITE 2 AC5 6 ADP C 998 ALF C 999
SITE 1 AC6 10 SER C 179 LYS C 183 ASN C 242 SER C 245
SITE 2 AC6 10 SER C 246 ASP C 465 GLY C 468 HOH C 995
SITE 3 AC6 10 MG C 997 ADP C 998
SITE 1 AC7 6 THR D 184 SER D 246 ASP D 465 HOH D 995
SITE 2 AC7 6 ADP D 998 ALF D 999
SITE 1 AC8 11 SER D 179 LYS D 183 SER D 245 SER D 246
SITE 2 AC8 11 ASP D 465 ILE D 466 ALA D 467 GLY D 468
SITE 3 AC8 11 HOH D 995 MG D 997 ADP D 998
SITE 1 AC9 6 THR E 184 SER E 246 ASP E 465 HOH E 995
SITE 2 AC9 6 ADP E 998 ALF E 999
SITE 1 BC1 11 SER E 179 LYS E 183 SER E 245 SER E 246
SITE 2 BC1 11 ASP E 465 ILE E 466 ALA E 467 GLY E 468
SITE 3 BC1 11 HOH E 995 MG E 997 ADP E 998
SITE 1 BC2 6 THR F 184 SER F 246 ASP F 465 HOH F 995
SITE 2 BC2 6 ADP F 998 ALF F 999
SITE 1 BC3 10 SER F 179 LYS F 183 SER F 245 SER F 246
SITE 2 BC3 10 ILE F 466 ALA F 467 GLY F 468 HOH F 995
SITE 3 BC3 10 MG F 997 ADP F 998
SITE 1 BC4 16 ILE A 113 ASN A 125 PRO A 126 TYR A 127
SITE 2 BC4 16 LYS A 128 TYR A 133 GLY A 180 GLY A 182
SITE 3 BC4 16 LYS A 183 THR A 184 GLU A 185 ASN A 242
SITE 4 BC4 16 HOH A 995 HOH A 996 MG A 997 ALF A 999
SITE 1 BC5 15 ILE B 113 ASN B 125 PRO B 126 TYR B 127
SITE 2 BC5 15 TYR B 133 GLY B 180 GLY B 182 LYS B 183
SITE 3 BC5 15 THR B 184 GLU B 185 ASN B 242 HOH B 995
SITE 4 BC5 15 HOH B 996 MG B 997 ALF B 999
SITE 1 BC6 16 ILE C 113 ASN C 125 PRO C 126 TYR C 127
SITE 2 BC6 16 LYS C 128 TYR C 133 GLY C 180 GLY C 182
SITE 3 BC6 16 LYS C 183 THR C 184 GLU C 185 ASN C 242
SITE 4 BC6 16 HOH C 995 HOH C 996 MG C 997 ALF C 999
SITE 1 BC7 15 ILE D 113 ASN D 125 PRO D 126 TYR D 127
SITE 2 BC7 15 TYR D 133 GLY D 180 GLY D 182 LYS D 183
SITE 3 BC7 15 THR D 184 GLU D 185 ASN D 242 HOH D 995
SITE 4 BC7 15 HOH D 996 MG D 997 ALF D 999
SITE 1 BC8 16 ILE E 113 ASN E 125 PRO E 126 TYR E 127
SITE 2 BC8 16 LYS E 128 TYR E 133 GLY E 180 GLY E 182
SITE 3 BC8 16 LYS E 183 THR E 184 GLU E 185 ASN E 242
SITE 4 BC8 16 HOH E 995 HOH E 996 MG E 997 ALF E 999
SITE 1 BC9 16 ILE F 113 ASN F 125 PRO F 126 TYR F 127
SITE 2 BC9 16 LYS F 128 TYR F 133 GLY F 180 GLY F 182
SITE 3 BC9 16 LYS F 183 THR F 184 GLU F 185 ASN F 242
SITE 4 BC9 16 HOH F 995 HOH F 996 MG F 997 ALF F 999
CRYST1 134.010 107.670 188.310 90.00 90.66 90.00 P 1 2 1 12
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 0.007462 0.000000 0.000086 0.00000
SCALE2 0.000000 0.009288 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005311 0.00000
MTRIX1 1 -0.997600 0.068650 -0.008880 129.05473 1
MTRIX2 1 0.068990 0.996590 -0.045290 51.34279 1
MTRIX3 1 0.005740 -0.045800 -0.998930 98.17990 1
MTRIX1 2 -0.990670 0.100100 -0.092510 84.21188 1
MTRIX2 2 0.015660 -0.590600 -0.806810 79.82545 1
MTRIX3 2 -0.135400 -0.800730 0.583520 108.69299 1
MTRIX1 3 -0.984290 0.144620 -0.101310 37.79606 1
MTRIX2 3 -0.154260 -0.425080 0.891910 24.29972 1
MTRIX3 3 0.085920 0.893530 0.440710 -17.58553 1
MTRIX1 4 0.977350 -0.191640 0.089780 98.94315 1
MTRIX2 4 -0.163700 -0.415750 0.894630 77.70154 1
MTRIX3 4 -0.134120 -0.889060 -0.437700 110.75905 1
MTRIX1 5 0.996900 -0.052800 0.058360 44.46971 1
MTRIX2 5 0.016980 -0.579820 -0.814570 133.12106 1
MTRIX3 5 0.076850 0.813030 -0.577130 -10.85735 1
(ATOM LINES ARE NOT SHOWN.)
END
