HEADER MUSCLE PROTEIN 26-AUG-98 1BR1
TITLE SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH
TITLE 2 MGADP.ALF4 BOUND AT THE ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: CHAINS A, C, E, G, MOTOR DOMAIN, CHAINS B, D, F, H,
COMPND 5 ESSENTIAL LIGHT;
COMPND 6 SYNONYM: MDE;
COMPND 7 EC: 3.6.1.32;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: MG, ADP, ALF(4);
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: MYOSIN;
COMPND 12 CHAIN: B, D, F, H;
COMPND 13 FRAGMENT: CHAINS A, C, E, G, MOTOR DOMAIN, CHAINS B, D, F, H,
COMPND 14 ESSENTIAL LIGHT;
COMPND 15 SYNONYM: MDE;
COMPND 16 EC: 3.6.1.32;
COMPND 17 ENGINEERED: YES;
COMPND 18 OTHER_DETAILS: 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;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 15 ORGANISM_COMMON: CHICKEN;
SOURCE 16 ORGANISM_TAXID: 9031;
SOURCE 17 CELL_LINE: SF9;
SOURCE 18 ORGAN: GIZZARD;
SOURCE 19 TISSUE: SMOOTH MUSCLE;
SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 21 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS
KEYWDS MUSCLE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.DOMINGUEZ,K.M.TRYBUS,C.COHEN
REVDAT 5 07-FEB-24 1BR1 1 REMARK LINK
REVDAT 4 24-FEB-09 1BR1 1 VERSN
REVDAT 3 30-SEP-03 1BR1 1 DBREF
REVDAT 2 08-JUN-99 1BR1 3 HET COMPND REMARK HETATM
REVDAT 2 2 3 DBREF SEQADV SCALE HEADER
REVDAT 2 3 3 TER SOURCE ATOM SEQRES
REVDAT 2 4 3 FORMUL JRNL HETSYN CONECT
REVDAT 1 09-SEP-98 1BR1 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. 3.50 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) : 3.50
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) (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 76805
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) : 0.227
REMARK 3 FREE R VALUE : 0.305
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 : 29992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.90
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) : 0.60
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
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 1BR1 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_1000172016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.905
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 : 79993
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
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 (%) : 91.7
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.800
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: SMOOTH MUSCLE MYOSIN MOTOR DOMAIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE 100MM HEPES PH
REMARK 280 7.2 2MM MGADP 2MM AL(NO3)3 8MM NAF PROTEIN CONCENTRATION: 10MG/
REMARK 280 ML TEMPERATURE: 4 DEGREES CENTIGRADE, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 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 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 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 CYS B 1
REMARK 465 ASP B 2
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 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 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 CYS D 1
REMARK 465 ASP D 2
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 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 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 CYS F 1
REMARK 465 ASP F 2
REMARK 465 LYS G 205
REMARK 465 ASP G 206
REMARK 465 THR G 207
REMARK 465 SER G 208
REMARK 465 ILE G 209
REMARK 465 THR G 210
REMARK 465 LYS G 452
REMARK 465 THR G 453
REMARK 465 LYS G 454
REMARK 465 ARG G 455
REMARK 465 GLN G 456
REMARK 465 GLY G 457
REMARK 465 ASP G 635
REMARK 465 GLN G 636
REMARK 465 MET G 637
REMARK 465 ALA G 638
REMARK 465 LYS G 639
REMARK 465 MET G 640
REMARK 465 THR G 641
REMARK 465 GLU G 642
REMARK 465 SER G 643
REMARK 465 SER G 644
REMARK 465 LEU G 645
REMARK 465 PRO G 646
REMARK 465 SER G 647
REMARK 465 ALA G 648
REMARK 465 SER G 649
REMARK 465 LYS G 650
REMARK 465 THR G 651
REMARK 465 LYS G 652
REMARK 465 LYS G 653
REMARK 465 GLY G 654
REMARK 465 MET G 655
REMARK 465 CYS H 1
REMARK 465 ASP H 2
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 O CYS F 84 N ASP F 87 1.99
REMARK 500 O TRP A 625 N ASP A 627 2.10
REMARK 500 O TYR E 663 N GLU E 665 2.17
REMARK 500 O TYR C 663 N GLU C 665 2.18
REMARK 500 O TRP G 625 N ASP G 627 2.19
REMARK 500 O TYR G 663 N GLU G 665 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE1 PHE E 19 OE2 GLU G 786 1556 1.59
REMARK 500 CD1 PHE E 19 OE2 GLU G 786 1556 1.66
REMARK 500 N ASP D 23 NH2 ARG G 371 1545 1.81
REMARK 500 N GLY D 22 CZ ARG G 371 1545 1.88
REMARK 500 CE1 PHE E 19 CD GLU G 786 1556 1.91
REMARK 500 NH1 ARG A 371 N GLY F 22 1544 1.91
REMARK 500 CA GLY D 22 NE ARG G 371 1545 1.96
REMARK 500 N GLY D 22 NH1 ARG G 371 1545 1.96
REMARK 500 C GLY D 22 NE ARG G 371 1545 2.07
REMARK 500 NE ARG A 371 CA GLY F 22 1544 2.09
REMARK 500 CG ASP D 23 NH2 ARG G 371 1545 2.11
REMARK 500 OG1 THR D 21 NH1 ARG G 371 1545 2.11
REMARK 500 NE ARG A 371 C GLY F 22 1544 2.13
REMARK 500 N GLY D 22 NE ARG G 371 1545 2.14
REMARK 500 CD1 PHE E 19 CD GLU G 786 1556 2.15
REMARK 500 NE ARG A 371 O GLY F 22 1544 2.18
REMARK 500 CZ ARG A 371 CA GLY F 22 1544 2.19
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 MET A 78 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 279 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 630 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 715 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 MET C 78 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG C 107 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 247 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 285 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 630 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG C 715 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 815 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 MET E 78 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG E 107 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG E 247 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG E 285 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG E 630 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG E 715 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG E 815 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 GLY F 22 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 PHE F 85 CA - C - N ANGL. DEV. = -15.8 DEGREES
REMARK 500 MET G 78 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG G 107 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 MET G 164 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG G 168 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG G 247 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG G 285 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG G 630 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG G 715 NE - CZ - NH2 ANGL. DEV. = 3.4 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 LYS A 4 170.73 -42.71
REMARK 500 ALA A 31 34.76 -71.22
REMARK 500 LYS A 32 -32.94 -33.04
REMARK 500 LYS A 33 7.14 -61.63
REMARK 500 PRO A 38 160.05 -31.19
REMARK 500 SER A 39 109.32 -176.62
REMARK 500 GLU A 40 10.52 -69.15
REMARK 500 LYS A 41 -11.23 -144.00
REMARK 500 GLU A 51 117.38 -164.75
REMARK 500 GLN A 62 21.15 -72.58
REMARK 500 GLU A 63 -77.74 -121.49
REMARK 500 LYS A 72 28.96 -70.20
REMARK 500 MET A 89 -35.89 -34.26
REMARK 500 ALA A 90 7.43 -60.55
REMARK 500 THR A 93 4.91 -68.21
REMARK 500 GLU A 106 -76.18 -55.79
REMARK 500 VAL A 123 69.62 -157.54
REMARK 500 TYR A 127 -0.46 78.87
REMARK 500 PRO A 131 70.53 -106.15
REMARK 500 LYS A 145 -168.06 -53.69
REMARK 500 GLU A 148 6.55 -61.12
REMARK 500 ARG A 168 80.37 43.87
REMARK 500 GLU A 169 96.54 -169.69
REMARK 500 ASP A 170 149.66 -28.32
REMARK 500 THR A 176 -151.88 -91.26
REMARK 500 ALA A 181 4.14 -53.73
REMARK 500 ASN A 186 -18.28 -49.38
REMARK 500 LYS A 202 38.40 -87.85
REMARK 500 SER A 214 107.11 -57.84
REMARK 500 PHE A 215 134.56 175.84
REMARK 500 ILE A 230 -61.97 -90.28
REMARK 500 ALA A 233 -82.25 -69.70
REMARK 500 VAL A 240 1.87 -56.94
REMARK 500 ASN A 242 115.08 -168.44
REMARK 500 ARG A 247 34.79 -90.82
REMARK 500 PHE A 248 132.22 176.97
REMARK 500 TYR A 270 -127.17 -125.02
REMARK 500 LEU A 271 78.84 -65.46
REMARK 500 GLU A 273 66.80 -61.04
REMARK 500 ARG A 276 -6.63 -41.53
REMARK 500 HIS A 288 -66.12 -17.10
REMARK 500 GLN A 300 -74.82 -55.36
REMARK 500 PHE A 332 -70.06 -52.10
REMARK 500 PHE A 344 109.45 -54.47
REMARK 500 GLU A 348 -13.20 -46.24
REMARK 500 ILE A 352 -10.88 -48.49
REMARK 500 VAL A 359 -5.28 -55.89
REMARK 500 LEU A 362 -3.68 -48.80
REMARK 500 ILE A 365 125.16 -37.94
REMARK 500 LYS A 369 159.24 -45.46
REMARK 500
REMARK 500 THIS ENTRY HAS 545 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 75.7
REMARK 620 3 HOH A 995 O 94.8 78.8
REMARK 620 4 ADP A 998 O2B 86.9 160.6 94.3
REMARK 620 5 ALF A 999 F2 152.2 97.2 57.5 94.2
REMARK 620 6 ALF A 999 F4 143.6 134.9 108.7 64.5 57.7
REMARK 620 7 ALF A 999 AL 160.7 122.5 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 SER A 245 OG
REMARK 620 2 ALF A 999 F1 141.3
REMARK 620 3 ALF A 999 F2 38.1 177.4
REMARK 620 4 ALF A 999 F3 53.9 88.4 90.5
REMARK 620 5 ALF A 999 F4 126.7 91.3 89.8 177.7
REMARK 620 6 HOH A 995 O 73.6 143.0 36.6 120.1 59.3
REMARK 620 7 ADP A 998 O1B 137.5 62.9 115.8 116.4 61.5 82.4
REMARK 620 8 ADP A 998 O2B 119.0 96.4 83.2 144.3 33.5 46.6 40.6
REMARK 620 9 ADP A 998 O3B 95.3 100.4 77.5 100.3 77.6 54.5 42.7 44.1
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 73.9
REMARK 620 3 HOH C 995 O 91.4 76.3
REMARK 620 4 ADP C 998 O2B 88.7 159.7 94.3
REMARK 620 5 ALF C 999 F2 148.8 95.6 57.4 94.2
REMARK 620 6 ALF C 999 F4 146.9 135.4 108.6 64.5 57.7
REMARK 620 7 ALF C 999 AL 161.5 121.8 83.7 74.0 31.7 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 GLY C 468 N
REMARK 620 2 ALF C 999 F1 35.6
REMARK 620 3 ALF C 999 F2 146.8 177.4
REMARK 620 4 ALF C 999 F3 94.8 88.3 90.5
REMARK 620 5 ALF C 999 F4 86.2 91.3 89.8 177.7
REMARK 620 6 HOH C 995 O 143.8 143.0 36.6 120.1 59.3
REMARK 620 7 ADP C 998 O3B 133.1 100.5 77.5 100.2 77.6 54.5
REMARK 620 8 ADP C 998 O2B 109.5 96.4 83.2 144.3 33.5 46.6 44.1
REMARK 620 9 ADP C 998 O1B 91.0 62.9 115.8 116.4 61.5 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 72.7
REMARK 620 3 HOH E 995 O 88.9 74.7
REMARK 620 4 ADP E 998 O2B 92.6 161.5 94.3
REMARK 620 5 ALF E 999 F2 146.0 92.1 57.4 94.2
REMARK 620 6 ALF E 999 F4 151.5 132.7 108.7 64.5 57.7
REMARK 620 7 ALF E 999 AL 164.2 118.3 83.7 74.0 31.7 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 E 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 468 N
REMARK 620 2 ALF E 999 F1 38.1
REMARK 620 3 ALF E 999 F2 144.3 177.4
REMARK 620 4 ALF E 999 F3 92.8 88.3 90.4
REMARK 620 5 ALF E 999 F4 88.3 91.4 89.8 177.8
REMARK 620 6 HOH E 995 O 144.9 143.0 36.6 120.1 59.3
REMARK 620 7 ADP E 998 O3B 136.4 100.5 77.5 100.3 77.6 54.5
REMARK 620 8 ADP E 998 O1B 94.4 62.9 115.8 116.4 61.6 82.4 42.7
REMARK 620 9 ADP E 998 O2B 112.6 96.5 83.2 144.3 33.6 46.6 44.1 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 G 997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 184 OG1
REMARK 620 2 SER G 246 OG 74.4
REMARK 620 3 HOH G 995 O 91.7 76.1
REMARK 620 4 ADP G 998 O2B 91.1 162.2 94.3
REMARK 620 5 ALF G 999 F2 148.9 93.1 57.4 94.3
REMARK 620 6 ALF G 999 F4 148.7 132.6 108.6 64.5 57.7
REMARK 620 7 ALF G 999 AL 164.0 118.9 83.7 74.0 31.7 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 G 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 468 N
REMARK 620 2 ALF G 999 F1 37.2
REMARK 620 3 ALF G 999 F2 145.2 177.5
REMARK 620 4 ALF G 999 F3 93.4 88.3 90.4
REMARK 620 5 ALF G 999 F4 87.7 91.3 89.8 177.7
REMARK 620 6 HOH G 995 O 144.6 143.1 36.6 120.1 59.3
REMARK 620 7 ADP G 998 O3B 135.2 100.5 77.5 100.3 77.6 54.5
REMARK 620 8 ADP G 998 O2B 111.6 96.5 83.2 144.3 33.5 46.6 44.1
REMARK 620 9 ADP G 998 O1B 93.2 62.9 115.8 116.4 61.5 82.4 42.7 40.6
REMARK 620 N 1 2 3 4 5 6 7 8
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 C 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF C 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF E 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF G 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 998
DBREF 1BR1 A 3 819 UNP P10587 MYH11_CHICK 2 818
DBREF 1BR1 B 1 150 UNP P02607 MLES_CHICK 1 150
DBREF 1BR1 C 3 819 UNP P10587 MYH11_CHICK 2 818
DBREF 1BR1 D 1 150 UNP P02607 MLES_CHICK 1 150
DBREF 1BR1 E 3 819 UNP P10587 MYH11_CHICK 2 818
DBREF 1BR1 F 1 150 UNP P02607 MLES_CHICK 1 150
DBREF 1BR1 G 3 819 UNP P10587 MYH11_CHICK 2 818
DBREF 1BR1 H 1 150 UNP P02607 MLES_CHICK 1 150
SEQRES 1 A 820 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 A 820 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 A 820 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 A 820 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 A 820 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 A 820 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 A 820 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 A 820 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 A 820 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 A 820 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 A 820 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 A 820 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 A 820 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 A 820 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 A 820 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 A 820 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 A 820 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 A 820 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 A 820 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 A 820 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 A 820 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 A 820 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 A 820 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 A 820 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 A 820 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 A 820 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 A 820 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 A 820 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 A 820 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 A 820 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 A 820 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 A 820 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 A 820 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 A 820 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 A 820 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 A 820 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 A 820 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 A 820 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 A 820 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 A 820 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 A 820 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 A 820 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 A 820 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 A 820 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 A 820 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 A 820 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 A 820 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 A 820 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 A 820 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 A 820 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 A 820 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 A 820 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 A 820 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 A 820 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 A 820 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 A 820 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 A 820 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 A 820 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 A 820 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 A 820 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 A 820 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP
SEQRES 62 A 820 VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU
SEQRES 63 A 820 ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY
SEQRES 64 A 820 SER
SEQRES 1 B 150 CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU
SEQRES 2 B 150 ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE
SEQRES 3 B 150 LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY
SEQRES 4 B 150 GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY
SEQRES 5 B 150 ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS
SEQRES 6 B 150 PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS
SEQRES 7 B 150 ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY
SEQRES 8 B 150 LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET
SEQRES 9 B 150 GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU
SEQRES 10 B 150 LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY
SEQRES 11 B 150 HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU
SEQRES 12 B 150 VAL ARG MET VAL LEU SER GLY
SEQRES 1 C 820 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 C 820 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 C 820 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 C 820 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 C 820 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 C 820 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 C 820 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 C 820 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 C 820 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 C 820 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 C 820 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 C 820 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 C 820 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 C 820 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 C 820 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 C 820 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 C 820 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 C 820 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 C 820 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 C 820 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 C 820 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 C 820 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 C 820 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 C 820 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 C 820 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 C 820 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 C 820 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 C 820 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 C 820 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 C 820 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 C 820 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 C 820 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 C 820 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 C 820 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 C 820 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 C 820 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 C 820 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 C 820 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 C 820 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 C 820 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 C 820 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 C 820 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 C 820 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 C 820 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 C 820 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 C 820 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 C 820 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 C 820 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 C 820 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 C 820 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 C 820 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 C 820 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 C 820 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 C 820 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 C 820 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 C 820 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 C 820 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 C 820 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 C 820 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 C 820 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 C 820 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP
SEQRES 62 C 820 VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU
SEQRES 63 C 820 ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY
SEQRES 64 C 820 SER
SEQRES 1 D 150 CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU
SEQRES 2 D 150 ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE
SEQRES 3 D 150 LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY
SEQRES 4 D 150 GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY
SEQRES 5 D 150 ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS
SEQRES 6 D 150 PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS
SEQRES 7 D 150 ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY
SEQRES 8 D 150 LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET
SEQRES 9 D 150 GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU
SEQRES 10 D 150 LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY
SEQRES 11 D 150 HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU
SEQRES 12 D 150 VAL ARG MET VAL LEU SER GLY
SEQRES 1 E 820 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 E 820 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 E 820 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 E 820 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 E 820 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 E 820 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 E 820 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 E 820 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 E 820 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 E 820 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 E 820 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 E 820 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 E 820 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 E 820 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 E 820 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 E 820 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 E 820 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 E 820 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 E 820 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 E 820 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 E 820 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 E 820 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 E 820 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 E 820 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 E 820 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 E 820 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 E 820 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 E 820 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 E 820 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 E 820 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 E 820 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 E 820 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 E 820 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 E 820 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 E 820 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 E 820 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 E 820 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 E 820 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 E 820 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 E 820 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 E 820 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 E 820 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 E 820 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 E 820 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 E 820 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 E 820 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 E 820 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 E 820 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 E 820 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 E 820 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 E 820 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 E 820 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 E 820 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 E 820 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 E 820 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 E 820 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 E 820 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 E 820 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 E 820 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 E 820 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 E 820 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP
SEQRES 62 E 820 VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU
SEQRES 63 E 820 ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY
SEQRES 64 E 820 SER
SEQRES 1 F 150 CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU
SEQRES 2 F 150 ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE
SEQRES 3 F 150 LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY
SEQRES 4 F 150 GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY
SEQRES 5 F 150 ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS
SEQRES 6 F 150 PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS
SEQRES 7 F 150 ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY
SEQRES 8 F 150 LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET
SEQRES 9 F 150 GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU
SEQRES 10 F 150 LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY
SEQRES 11 F 150 HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU
SEQRES 12 F 150 VAL ARG MET VAL LEU SER GLY
SEQRES 1 G 820 ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE
SEQRES 2 G 820 VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA
SEQRES 3 G 820 ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU
SEQRES 4 G 820 LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS
SEQRES 5 G 820 GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS
SEQRES 6 G 820 LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN
SEQRES 7 G 820 PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU
SEQRES 8 G 820 THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG
SEQRES 9 G 820 GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 G 820 LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO
SEQRES 11 G 820 ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS
SEQRES 12 G 820 LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA
SEQRES 13 G 820 ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP
SEQRES 14 G 820 GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 G 820 THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL
SEQRES 16 G 820 VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE
SEQRES 17 G 820 THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS
SEQRES 18 G 820 GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY
SEQRES 19 G 820 ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE
SEQRES 20 G 820 GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR
SEQRES 21 G 820 ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS
SEQRES 22 G 820 SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE
SEQRES 23 G 820 HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN
SEQRES 24 G 820 MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR
SEQRES 25 G 820 THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN
SEQRES 26 G 820 GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET
SEQRES 27 G 820 THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE
SEQRES 28 G 820 LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE
SEQRES 29 G 820 VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET
SEQRES 30 G 820 PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET
SEQRES 31 G 820 GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR
SEQRES 32 G 820 PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA
SEQRES 33 G 820 GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU
SEQRES 34 G 820 ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU
SEQRES 35 G 820 THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN
SEQRES 36 G 820 GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE
SEQRES 37 G 820 GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE
SEQRES 38 G 820 ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS
SEQRES 39 G 820 THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU
SEQRES 40 G 820 GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU
SEQRES 41 G 820 GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO
SEQRES 42 G 820 PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE
SEQRES 43 G 820 PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE
SEQRES 44 G 820 GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS
SEQRES 45 G 820 GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR
SEQRES 46 G 820 ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR
SEQRES 47 G 820 LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU
SEQRES 48 G 820 LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP
SEQRES 49 G 820 LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA
SEQRES 50 G 820 LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR
SEQRES 51 G 820 LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS
SEQRES 52 G 820 GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR
SEQRES 53 G 820 ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU
SEQRES 54 G 820 LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU
SEQRES 55 G 820 GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 56 G 820 CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU
SEQRES 57 G 820 PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE
SEQRES 58 G 820 PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU
SEQRES 59 G 820 MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG
SEQRES 60 G 820 ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU
SEQRES 61 G 820 ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP
SEQRES 62 G 820 VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU
SEQRES 63 G 820 ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY
SEQRES 64 G 820 SER
SEQRES 1 H 150 CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU
SEQRES 2 H 150 ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE
SEQRES 3 H 150 LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY
SEQRES 4 H 150 GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY
SEQRES 5 H 150 ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS
SEQRES 6 H 150 PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS
SEQRES 7 H 150 ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY
SEQRES 8 H 150 LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET
SEQRES 9 H 150 GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU
SEQRES 10 H 150 LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY
SEQRES 11 H 150 HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU
SEQRES 12 H 150 VAL ARG MET VAL LEU SER GLY
HET MG A 997 1
HET ALF A 999 5
HET ADP A 998 27
HET MG C 997 1
HET ALF C 999 5
HET ADP C 998 27
HET MG E 997 1
HET ALF E 999 5
HET ADP E 998 27
HET MG G 997 1
HET ALF G 999 5
HET ADP G 998 27
HETNAM MG MAGNESIUM ION
HETNAM ALF TETRAFLUOROALUMINATE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 9 MG 4(MG 2+)
FORMUL 10 ALF 4(AL F4 1-)
FORMUL 11 ADP 4(C10 H15 N5 O10 P2)
FORMUL 21 HOH *8(H2 O)
HELIX 1 1 GLU A 10 PHE A 12 5 3
HELIX 2 2 ALA A 25 SER A 30 1 6
HELIX 3 3 PRO A 81 PHE A 83 5 3
HELIX 4 4 SER A 99 SER A 110 1 12
HELIX 5 5 GLU A 135 TYR A 141 1 7
HELIX 6 6 ILE A 153 ASP A 167 1 15
HELIX 7 7 GLU A 185 VAL A 197 1 13
HELIX 8 8 LEU A 220 LEU A 231 1 12
HELIX 9 9 SER A 275 ALA A 277 5 3
HELIX 10 10 HIS A 288 GLY A 296 5 9
HELIX 11 11 GLU A 299 LEU A 305 1 7
HELIX 12 12 ASP A 328 MET A 342 1 15
HELIX 13 13 GLU A 346 GLY A 363 1 18
HELIX 14 14 THR A 382 LEU A 390 1 9
HELIX 15 15 VAL A 395 LEU A 403 1 9
HELIX 16 16 LYS A 420 ALA A 449 1 30
HELIX 17 17 PHE A 477 MET A 497 1 21
HELIX 18 18 ILE A 499 GLU A 508 1 10
HELIX 19 19 GLN A 522 GLU A 526 1 5
HELIX 20 20 VAL A 537 GLU A 543 1 7
HELIX 21 21 ASP A 552 GLU A 562 1 11
HELIX 22 22 TRP A 597 LYS A 600 1 4
HELIX 23 23 ASP A 607 ASN A 614 1 8
HELIX 24 24 LYS A 619 TRP A 625 1 7
HELIX 25 25 VAL A 659 ASN A 676 1 18
HELIX 26 26 ALA A 698 CYS A 707 1 10
HELIX 27 27 VAL A 710 GLN A 719 1 10
HELIX 28 28 PHE A 727 ARG A 733 1 7
HELIX 29 29 GLY A 749 LYS A 758 1 10
HELIX 30 30 VAL A 780 LYS A 791 1 12
HELIX 31 31 THR A 793 LEU A 819 1 27
HELIX 32 32 GLU B 5 GLN B 16 1 12
HELIX 33 33 CYS B 31 ALA B 37 1 7
HELIX 34 34 ASN B 44 LEU B 51 1 8
HELIX 35 35 SER B 56 MET B 59 5 4
HELIX 36 36 PHE B 66 ALA B 77 1 12
HELIX 37 37 PHE B 85 VAL B 94 1 10
HELIX 38 38 GLU B 107 VAL B 113 1 7
HELIX 39 39 GLU B 121 VAL B 128 1 8
HELIX 40 40 TYR B 140 LEU B 148 1 9
HELIX 41 41 GLU C 10 PHE C 12 5 3
HELIX 42 42 PRO C 23 SER C 30 1 8
HELIX 43 43 PRO C 81 PHE C 83 5 3
HELIX 44 44 SER C 99 SER C 110 1 12
HELIX 45 45 GLU C 135 TYR C 141 1 7
HELIX 46 46 ILE C 153 ASP C 167 1 15
HELIX 47 47 GLU C 185 VAL C 197 1 13
HELIX 48 48 LEU C 220 LEU C 231 1 12
HELIX 49 49 SER C 275 ALA C 277 5 3
HELIX 50 50 HIS C 288 GLY C 296 5 9
HELIX 51 51 GLU C 299 LEU C 305 1 7
HELIX 52 52 ASP C 328 MET C 342 1 15
HELIX 53 53 GLU C 346 GLY C 363 1 18
HELIX 54 54 THR C 382 LEU C 390 1 9
HELIX 55 55 VAL C 395 LEU C 403 1 9
HELIX 56 56 GLN C 422 ALA C 449 1 28
HELIX 57 57 PHE C 477 MET C 497 1 21
HELIX 58 58 ILE C 499 ARG C 507 1 9
HELIX 59 59 GLN C 522 GLU C 526 1 5
HELIX 60 60 VAL C 537 GLU C 543 1 7
HELIX 61 61 ASP C 552 GLU C 562 1 11
HELIX 62 62 TRP C 597 LYS C 600 1 4
HELIX 63 63 ASP C 607 ASN C 614 1 8
HELIX 64 64 LYS C 619 LEU C 624 1 6
HELIX 65 65 VAL C 659 ASN C 676 1 18
HELIX 66 66 ALA C 698 CYS C 707 1 10
HELIX 67 67 VAL C 710 GLN C 719 1 10
HELIX 68 68 PHE C 727 ARG C 733 1 7
HELIX 69 69 GLY C 749 LYS C 758 1 10
HELIX 70 70 VAL C 780 LYS C 791 1 12
HELIX 71 71 THR C 793 LEU C 819 1 27
HELIX 72 72 GLU D 5 GLN D 16 1 12
HELIX 73 73 CYS D 31 ALA D 37 1 7
HELIX 74 74 ASN D 44 LEU D 51 1 8
HELIX 75 75 SER D 56 MET D 59 5 4
HELIX 76 76 PHE D 66 ALA D 77 1 12
HELIX 77 77 PHE D 85 VAL D 94 1 10
HELIX 78 78 GLU D 107 VAL D 113 1 7
HELIX 79 79 GLU D 121 VAL D 128 1 8
HELIX 80 80 TYR D 140 LEU D 148 1 9
HELIX 81 81 GLU E 10 PHE E 12 5 3
HELIX 82 82 PRO E 23 SER E 30 1 8
HELIX 83 83 PRO E 81 PHE E 83 5 3
HELIX 84 84 SER E 99 SER E 110 1 12
HELIX 85 85 GLU E 135 TYR E 141 1 7
HELIX 86 86 ILE E 153 ASP E 167 1 15
HELIX 87 87 GLU E 185 VAL E 197 1 13
HELIX 88 88 LEU E 220 LEU E 231 1 12
HELIX 89 89 SER E 275 ALA E 277 5 3
HELIX 90 90 HIS E 288 GLY E 296 5 9
HELIX 91 91 GLU E 299 LEU E 305 1 7
HELIX 92 92 ASP E 328 MET E 342 1 15
HELIX 93 93 GLU E 346 GLY E 363 1 18
HELIX 94 94 THR E 382 LEU E 390 1 9
HELIX 95 95 VAL E 395 LEU E 403 1 9
HELIX 96 96 LYS E 420 VAL E 446 1 27
HELIX 97 97 PHE E 477 MET E 497 1 21
HELIX 98 98 ILE E 499 ARG E 507 1 9
HELIX 99 99 GLN E 522 GLU E 526 1 5
HELIX 100 100 VAL E 537 GLU E 543 1 7
HELIX 101 101 ASP E 552 GLU E 562 1 11
HELIX 102 102 TRP E 597 LYS E 600 1 4
HELIX 103 103 ASP E 607 ASN E 614 1 8
HELIX 104 104 LYS E 619 LEU E 624 1 6
HELIX 105 105 VAL E 659 ASN E 676 1 18
HELIX 106 106 ALA E 698 CYS E 707 1 10
HELIX 107 107 VAL E 710 GLN E 719 1 10
HELIX 108 108 PHE E 727 ARG E 733 1 7
HELIX 109 109 GLY E 749 LYS E 758 1 10
HELIX 110 110 VAL E 780 LYS E 791 1 12
HELIX 111 111 THR E 793 LEU E 819 1 27
HELIX 112 112 GLU F 5 GLN F 16 1 12
HELIX 113 113 CYS F 31 ALA F 37 1 7
HELIX 114 114 ASN F 44 LEU F 51 1 8
HELIX 115 115 SER F 56 MET F 59 5 4
HELIX 116 116 PHE F 66 ALA F 77 1 12
HELIX 117 117 TYR F 88 VAL F 94 1 7
HELIX 118 118 GLU F 107 VAL F 113 1 7
HELIX 119 119 GLU F 121 VAL F 128 1 8
HELIX 120 120 TYR F 140 LEU F 148 1 9
HELIX 121 121 GLU G 10 PHE G 12 5 3
HELIX 122 122 PRO G 23 SER G 30 1 8
HELIX 123 123 PRO G 81 PHE G 83 5 3
HELIX 124 124 SER G 99 SER G 110 1 12
HELIX 125 125 GLU G 135 TYR G 141 1 7
HELIX 126 126 ILE G 153 GLN G 166 1 14
HELIX 127 127 GLU G 185 VAL G 197 1 13
HELIX 128 128 LEU G 220 LEU G 231 1 12
HELIX 129 129 SER G 275 ALA G 277 5 3
HELIX 130 130 HIS G 288 GLY G 296 5 9
HELIX 131 131 GLU G 299 LEU G 305 1 7
HELIX 132 132 ASP G 328 MET G 342 1 15
HELIX 133 133 GLU G 346 GLY G 363 1 18
HELIX 134 134 THR G 382 LEU G 390 1 9
HELIX 135 135 VAL G 395 LEU G 403 1 9
HELIX 136 136 LYS G 420 ALA G 449 1 30
HELIX 137 137 PHE G 477 MET G 497 1 21
HELIX 138 138 ILE G 499 ARG G 507 1 9
HELIX 139 139 GLN G 522 GLU G 526 1 5
HELIX 140 140 VAL G 537 GLU G 543 1 7
HELIX 141 141 ASP G 552 GLU G 562 1 11
HELIX 142 142 TRP G 597 LYS G 600 1 4
HELIX 143 143 ASP G 607 ASN G 614 1 8
HELIX 144 144 LYS G 619 TRP G 625 1 7
HELIX 145 145 VAL G 659 ASN G 676 1 18
HELIX 146 146 ALA G 698 CYS G 707 1 10
HELIX 147 147 VAL G 710 GLN G 719 1 10
HELIX 148 148 PHE G 727 ARG G 733 1 7
HELIX 149 149 GLU G 735 LEU G 737 5 3
HELIX 150 150 GLY G 749 LYS G 758 1 10
HELIX 151 151 VAL G 780 LYS G 791 1 12
HELIX 152 152 THR G 793 LEU G 819 1 27
HELIX 153 153 GLU H 5 GLN H 16 1 12
HELIX 154 154 CYS H 31 ALA H 37 1 7
HELIX 155 155 ASN H 44 LEU H 51 1 8
HELIX 156 156 SER H 56 MET H 59 5 4
HELIX 157 157 PHE H 66 ALA H 77 1 12
HELIX 158 158 PHE H 85 PHE H 95 1 11
HELIX 159 159 GLU H 107 VAL H 113 1 7
HELIX 160 160 GLU H 121 VAL H 128 1 8
HELIX 161 161 TYR H 140 LEU H 148 1 9
SHEET 1 A 5 ILE A 75 LYS A 77 0
SHEET 2 A 5 LEU A 34 SER A 39 -1 N TRP A 36 O GLN A 76
SHEET 3 A 5 GLY A 43 LYS A 53 -1 N ALA A 47 O VAL A 35
SHEET 4 A 5 GLU A 56 LEU A 61 -1 N GLU A 60 O SER A 48
SHEET 5 A 5 LYS A 67 SER A 71 -1 N LEU A 70 O VAL A 57
SHEET 1 B 2 TYR A 114 SER A 117 0
SHEET 2 B 2 PHE A 120 VAL A 123 -1 N VAL A 122 O THR A 115
SHEET 1 C 5 ASN A 678 PHE A 681 0
SHEET 2 C 5 GLN A 171 LEU A 174 1 N SER A 172 O ASN A 678
SHEET 3 C 5 SER A 459 ASP A 465 1 N GLY A 462 O GLN A 171
SHEET 4 C 5 LYS A 250 PHE A 256 -1 N PHE A 256 O SER A 459
SHEET 5 C 5 ILE A 262 THR A 269 -1 N GLU A 268 O PHE A 251
SHEET 1 D 3 PHE A 569 LYS A 571 0
SHEET 2 D 3 GLU A 580 LEU A 584 -1 N CYS A 582 O GLN A 570
SHEET 3 D 3 LYS A 589 ASN A 593 -1 N TYR A 592 O PHE A 581
SHEET 1 E 2 ASN A 723 VAL A 726 0
SHEET 2 E 2 LYS A 773 PHE A 776 -1 N PHE A 776 O ASN A 723
SHEET 1 F 5 ILE C 75 LYS C 77 0
SHEET 2 F 5 LEU C 34 SER C 39 -1 N TRP C 36 O GLN C 76
SHEET 3 F 5 GLY C 43 LYS C 53 -1 N ALA C 47 O VAL C 35
SHEET 4 F 5 GLU C 56 LEU C 61 -1 N GLU C 60 O SER C 48
SHEET 5 F 5 LYS C 67 SER C 71 -1 N LEU C 70 O VAL C 57
SHEET 1 G 2 TYR C 114 SER C 117 0
SHEET 2 G 2 PHE C 120 VAL C 123 -1 N VAL C 122 O THR C 115
SHEET 1 H 5 ASN C 678 PHE C 681 0
SHEET 2 H 5 GLN C 171 LEU C 174 1 N SER C 172 O ASN C 678
SHEET 3 H 5 SER C 459 ASP C 465 1 N GLY C 462 O GLN C 171
SHEET 4 H 5 LYS C 250 PHE C 256 -1 N PHE C 256 O SER C 459
SHEET 5 H 5 ILE C 262 THR C 269 -1 N GLU C 268 O PHE C 251
SHEET 1 I 3 PHE C 569 LYS C 571 0
SHEET 2 I 3 GLU C 580 LEU C 584 -1 N CYS C 582 O GLN C 570
SHEET 3 I 3 LYS C 589 ASN C 593 -1 N TYR C 592 O PHE C 581
SHEET 1 J 3 ASN C 723 VAL C 726 0
SHEET 2 J 3 LYS C 773 PHE C 776 -1 N PHE C 776 O ASN C 723
SHEET 3 J 3 TYR C 767 ILE C 769 -1 N ARG C 768 O PHE C 775
SHEET 1 K 5 ILE E 75 LYS E 77 0
SHEET 2 K 5 LEU E 34 SER E 39 -1 N TRP E 36 O GLN E 76
SHEET 3 K 5 GLY E 43 LYS E 53 -1 N ALA E 47 O VAL E 35
SHEET 4 K 5 GLU E 56 LEU E 61 -1 N GLU E 60 O SER E 48
SHEET 5 K 5 LYS E 67 SER E 71 -1 N LEU E 70 O VAL E 57
SHEET 1 L 2 TYR E 114 SER E 117 0
SHEET 2 L 2 PHE E 120 VAL E 123 -1 N VAL E 122 O THR E 115
SHEET 1 M 5 ASN E 678 PHE E 681 0
SHEET 2 M 5 GLN E 171 LEU E 174 1 N SER E 172 O ASN E 678
SHEET 3 M 5 SER E 459 ASP E 465 1 N GLY E 462 O GLN E 171
SHEET 4 M 5 LYS E 250 PHE E 256 -1 N PHE E 256 O SER E 459
SHEET 5 M 5 ILE E 262 THR E 269 -1 N GLU E 268 O PHE E 251
SHEET 1 N 3 PHE E 569 LYS E 571 0
SHEET 2 N 3 GLU E 580 LEU E 584 -1 N CYS E 582 O GLN E 570
SHEET 3 N 3 LYS E 589 ASN E 593 -1 N TYR E 592 O PHE E 581
SHEET 1 O 3 ASN E 723 VAL E 726 0
SHEET 2 O 3 LYS E 773 PHE E 776 -1 N PHE E 776 O ASN E 723
SHEET 3 O 3 TYR E 767 ILE E 769 -1 N ARG E 768 O PHE E 775
SHEET 1 P 5 ILE G 75 LYS G 77 0
SHEET 2 P 5 LEU G 34 SER G 39 -1 N TRP G 36 O GLN G 76
SHEET 3 P 5 GLY G 43 LYS G 53 -1 N ALA G 47 O VAL G 35
SHEET 4 P 5 GLU G 56 LEU G 61 -1 N GLU G 60 O SER G 48
SHEET 5 P 5 LYS G 67 SER G 71 -1 N LEU G 70 O VAL G 57
SHEET 1 Q 2 TYR G 114 SER G 117 0
SHEET 2 Q 2 PHE G 120 VAL G 123 -1 N VAL G 122 O THR G 115
SHEET 1 R 5 ASN G 678 PHE G 681 0
SHEET 2 R 5 GLN G 171 LEU G 174 1 N SER G 172 O ASN G 678
SHEET 3 R 5 SER G 459 ASP G 465 1 N GLY G 462 O GLN G 171
SHEET 4 R 5 LYS G 250 PHE G 256 -1 N PHE G 256 O SER G 459
SHEET 5 R 5 ILE G 262 THR G 269 -1 N GLU G 268 O PHE G 251
SHEET 1 S 3 PHE G 569 LYS G 571 0
SHEET 2 S 3 GLU G 580 LEU G 584 -1 N CYS G 582 O GLN G 570
SHEET 3 S 3 LYS G 589 ASN G 593 -1 N TYR G 592 O PHE G 581
SHEET 1 T 3 ASN G 723 VAL G 726 0
SHEET 2 T 3 LYS G 773 PHE G 776 -1 N PHE G 776 O ASN G 723
SHEET 3 T 3 TYR G 767 ILE G 769 -1 N ARG G 768 O PHE G 775
LINK OG1 THR A 184 MG MG A 997 1555 1555 2.16
LINK OG SER A 245 AL ALF A 999 1555 1555 3.67
LINK OG SER A 246 MG MG A 997 1555 1555 2.58
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 O1B ADP A 998 AL ALF A 999 1555 1555 3.59
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 OG1 THR C 184 MG MG C 997 1555 1555 2.17
LINK OG SER C 246 MG MG C 997 1555 1555 2.60
LINK N GLY C 468 AL ALF C 999 1555 1555 3.69
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 2.08
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 O2B ADP C 998 AL ALF C 999 1555 1555 3.48
LINK O1B ADP C 998 AL ALF C 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 2.73
LINK N GLY E 468 AL ALF E 999 1555 1555 3.63
LINK O HOH E 995 MG MG E 997 1555 1555 1.84
LINK O HOH E 995 AL ALF E 999 1555 1555 3.71
LINK MG MG E 997 O2B ADP E 998 1555 1555 2.04
LINK MG MG E 997 F2 ALF E 999 1555 1555 2.96
LINK MG MG E 997 F4 ALF E 999 1555 1555 2.08
LINK MG MG E 997 AL ALF E 999 1555 1555 3.43
LINK O3B ADP E 998 AL ALF E 999 1555 1555 2.08
LINK O1B ADP E 998 AL ALF E 999 1555 1555 3.59
LINK O2B ADP E 998 AL ALF E 999 1555 1555 3.48
LINK OG1 THR G 184 MG MG G 997 1555 1555 2.07
LINK OG SER G 246 MG MG G 997 1555 1555 2.66
LINK N GLY G 468 AL ALF G 999 1555 1555 3.71
LINK O HOH G 995 MG MG G 997 1555 1555 1.84
LINK O HOH G 995 AL ALF G 999 1555 1555 3.71
LINK MG MG G 997 O2B ADP G 998 1555 1555 2.04
LINK MG MG G 997 F2 ALF G 999 1555 1555 2.96
LINK MG MG G 997 F4 ALF G 999 1555 1555 2.09
LINK MG MG G 997 AL ALF G 999 1555 1555 3.43
LINK O3B ADP G 998 AL ALF G 999 1555 1555 2.08
LINK O2B ADP G 998 AL ALF G 999 1555 1555 3.48
LINK O1B ADP G 998 AL ALF G 999 1555 1555 3.59
SITE 1 AC1 5 THR A 184 SER A 246 HOH A 995 ADP A 998
SITE 2 AC1 5 ALF A 999
SITE 1 AC2 9 SER A 179 GLY A 180 LYS A 183 SER A 245
SITE 2 AC2 9 SER A 246 GLY A 468 HOH A 995 MG A 997
SITE 3 AC2 9 ADP A 998
SITE 1 AC3 5 THR C 184 SER C 246 HOH C 995 ADP C 998
SITE 2 AC3 5 ALF C 999
SITE 1 AC4 9 SER C 179 LYS C 183 SER C 245 SER C 246
SITE 2 AC4 9 ALA C 467 GLY C 468 HOH C 995 MG C 997
SITE 3 AC4 9 ADP C 998
SITE 1 AC5 5 THR E 184 SER E 246 HOH E 995 ADP E 998
SITE 2 AC5 5 ALF E 999
SITE 1 AC6 10 SER E 179 GLY E 180 LYS E 183 SER E 245
SITE 2 AC6 10 SER E 246 ALA E 467 GLY E 468 HOH E 995
SITE 3 AC6 10 MG E 997 ADP E 998
SITE 1 AC7 5 THR G 184 SER G 246 HOH G 995 ADP G 998
SITE 2 AC7 5 ALF G 999
SITE 1 AC8 9 SER G 179 GLY G 180 LYS G 183 SER G 245
SITE 2 AC8 9 SER G 246 GLY G 468 HOH G 995 MG G 997
SITE 3 AC8 9 ADP G 998
SITE 1 AC9 15 ASN A 125 PRO A 126 TYR A 127 TYR A 133
SITE 2 AC9 15 GLY A 180 ALA A 181 GLY A 182 LYS A 183
SITE 3 AC9 15 THR A 184 GLU A 185 ASN A 242 HOH A 995
SITE 4 AC9 15 HOH A 996 MG A 997 ALF A 999
SITE 1 BC1 15 ASN C 125 PRO C 126 TYR C 127 TYR C 133
SITE 2 BC1 15 GLY C 180 ALA C 181 GLY C 182 LYS C 183
SITE 3 BC1 15 THR C 184 GLU C 185 ASN C 242 HOH C 995
SITE 4 BC1 15 HOH C 996 MG C 997 ALF C 999
SITE 1 BC2 15 ASN E 125 PRO E 126 TYR E 127 TYR E 133
SITE 2 BC2 15 GLY E 180 ALA E 181 GLY E 182 LYS E 183
SITE 3 BC2 15 THR E 184 GLU E 185 ASN E 242 HOH E 995
SITE 4 BC2 15 HOH E 996 MG E 997 ALF E 999
SITE 1 BC3 15 ASN G 125 PRO G 126 TYR G 127 TYR G 133
SITE 2 BC3 15 GLY G 180 ALA G 181 GLY G 182 LYS G 183
SITE 3 BC3 15 THR G 184 GLU G 185 ASN G 242 HOH G 995
SITE 4 BC3 15 HOH G 996 MG G 997 ALF G 999
CRYST1 95.320 144.660 147.290 111.21 106.10 92.58 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010491 0.000473 0.003489 0.00000
SCALE2 0.000000 0.006920 0.002930 0.00000
SCALE3 0.000000 0.000000 0.007674 0.00000
MTRIX1 1 0.636300 0.759920 0.132790 74.91910 1
MTRIX2 1 0.765970 -0.642820 0.008300 36.46862 1
MTRIX3 1 0.091670 0.096430 -0.991110 57.02822 1
MTRIX1 2 0.707040 0.668210 0.231470 -16.38862 1
MTRIX2 2 -0.687720 0.725960 0.004980 -10.04698 1
MTRIX3 2 -0.164710 -0.162710 0.972830 82.88082 1
MTRIX1 3 0.996000 0.082670 -0.033900 45.17225 1
MTRIX2 3 0.085230 -0.992920 0.082690 81.93243 1
MTRIX3 3 -0.026830 -0.085250 -0.996000 9.46068 1
MTRIX1 4 0.618640 0.774410 0.132600 74.12373 1
MTRIX2 4 0.779830 -0.625780 0.016390 36.34917 1
MTRIX3 4 0.095670 0.093260 -0.991030 57.19003 1
MTRIX1 5 0.678740 0.687340 0.258610 -17.56703 1
MTRIX2 5 -0.712770 0.701370 0.006610 -9.98185 1
MTRIX3 5 -0.176840 -0.188820 0.965960 83.36942 1
MTRIX1 6 0.999380 0.023850 0.025980 46.73965 1
MTRIX2 6 0.019120 -0.985410 0.169090 80.05285 1
MTRIX3 6 0.029640 -0.168490 -0.985260 13.21120 1
(ATOM LINES ARE NOT SHOWN.)
END