HEADER STRUCTURAL PROTEIN 04-JAN-18 6C1H
TITLE HIGH-RESOLUTION CRYO-EM STRUCTURES OF ACTIN-BOUND MYOSIN STATES REVEAL
TITLE 2 THE MECHANISM OF MYOSIN FORCE SENSING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 SYNONYM: ALPHA-ACTIN-1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: UNCONVENTIONAL MYOSIN-IB;
COMPND 7 CHAIN: P;
COMPND 8 SYNONYM: MYOSIN I ALPHA,MMIA,MYOSIN HEAVY CHAIN MYR 1;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: CALMODULIN;
COMPND 11 CHAIN: R
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 7 ORGANISM_COMMON: RAT;
SOURCE 8 ORGANISM_TAXID: 10116;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 11 ORGANISM_TAXID: 32644
KEYWDS MECHANOCHEMISTRY, MECHANOBIOLOGY, STRUCTURAL BIOLOGY, CYTOSKELETON,
KEYWDS 2 MOLECULAR MOTOR, MYOSIN-I, STRUCTURAL PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.MENTES,A.HUEHN,X.LIU,A.ZWOLAK,R.DOMINGUEZ,H.SHUMAN,E.M.OSTAP,
AUTHOR 2 C.V.SINDELAR
REVDAT 5 13-MAR-24 6C1H 1 REMARK
REVDAT 4 08-JAN-20 6C1H 1 REMARK
REVDAT 3 28-FEB-18 6C1H 1 JRNL
REVDAT 2 07-FEB-18 6C1H 1 JRNL
REVDAT 1 31-JAN-18 6C1H 0
JRNL AUTH A.MENTES,A.HUEHN,X.LIU,A.ZWOLAK,R.DOMINGUEZ,H.SHUMAN,
JRNL AUTH 2 E.M.OSTAP,C.V.SINDELAR
JRNL TITL HIGH-RESOLUTION CRYO-EM STRUCTURES OF ACTIN-BOUND MYOSIN
JRNL TITL 2 STATES REVEAL THE MECHANISM OF MYOSIN FORCE SENSING.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 1292 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29358376
JRNL DOI 10.1073/PNAS.1718316115
REMARK 2
REMARK 2 RESOLUTION. 3.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.900
REMARK 3 NUMBER OF PARTICLES : 62000
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: RESOLUTION ESTIMATED BY POST-PROCESSING IN RELION
REMARK 3 USING A MASK WITH SOFT EDGES THAT INCLUDED ONLY THE CENTRAL
REMARK 3 SUBUNIT.
REMARK 4
REMARK 4 6C1H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1000231939.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : HELICAL
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : HELICAL ARRAY
REMARK 245 PARTICLE TYPE : HELICAL
REMARK 245 NAME OF SAMPLE : COMPLEX OF ACTIN, MYOSIN-1B,
REMARK 245 AND CALMODULIN WITH ADP
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, P, R
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 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 TYR P 638 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR P 638 OH
REMARK 470 GLU P 639 CB CG CD OE1 OE2
REMARK 470 PRO P 640 CB CG CD
REMARK 470 CYS P 641 CB SG
REMARK 470 LEU P 642 CB CG CD1 CD2
REMARK 470 GLU P 643 CB CG CD OE1 OE2
REMARK 470 ARG P 644 CB CG CD NE CZ NH1 NH2
REMARK 470 TYR P 645 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR P 645 OH
REMARK 470 LYS P 646 CB CG CD CE NZ
REMARK 470 MET P 647 CB CG SD CE
REMARK 470 LEU P 648 CB CG CD1 CD2
REMARK 470 CYS P 649 CB SG
REMARK 470 LYS P 650 CB CG CD CE NZ
REMARK 470 GLN P 651 CB CG CD OE1 NE2
REMARK 470 THR P 652 CB OG1 CG2
REMARK 470 TRP P 653 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP P 653 CZ2 CZ3 CH2
REMARK 470 PRO P 654 CB CG CD
REMARK 470 HIS P 655 CB CG ND1 CD2 CE1 NE2
REMARK 470 TRP P 656 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP P 656 CZ2 CZ3 CH2
REMARK 470 LYS P 657 CB CG CD CE NZ
REMARK 470 PRO P 659 CB CG CD
REMARK 470 ALA P 660 CB
REMARK 470 ARG P 661 CB CG CD NE CZ NH1 NH2
REMARK 470 SER P 662 CB OG
REMARK 470 VAL P 664 CB CG1 CG2
REMARK 470 GLU P 665 CB CG CD OE1 OE2
REMARK 470 VAL P 666 CB CG1 CG2
REMARK 470 LEU P 667 CB CG CD1 CD2
REMARK 470 PHE P 668 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN P 669 CB CG OD1 ND2
REMARK 470 GLU P 670 CB CG CD OE1 OE2
REMARK 470 LEU P 671 CB CG CD1 CD2
REMARK 470 GLU P 672 CB CG CD OE1 OE2
REMARK 470 ILE P 673 CB CG1 CG2 CD1
REMARK 470 PRO P 674 CB CG CD
REMARK 470 VAL P 675 CB CG1 CG2
REMARK 470 GLU P 676 CB CG CD OE1 OE2
REMARK 470 GLU P 677 CB CG CD OE1 OE2
REMARK 470 TYR P 678 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR P 678 OH
REMARK 470 ARG P 700 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS P 701 CB CG CD CE NZ
REMARK 470 GLN P 702 CB CG CD OE1 NE2
REMARK 470 ARG P 703 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU P 704 CB CG CD1 CD2
REMARK 470 GLU P 705 CB CG CD OE1 OE2
REMARK 470 ASP P 706 CB CG OD1 OD2
REMARK 470 LEU P 707 CB CG CD1 CD2
REMARK 470 ALA P 708 CB
REMARK 470 THR P 709 CB OG1 CG2
REMARK 470 LEU P 710 CB CG CD1 CD2
REMARK 470 ILE P 711 CB CG1 CG2 CD1
REMARK 470 GLN P 712 CB CG CD OE1 NE2
REMARK 470 LYS P 713 CB CG CD CE NZ
REMARK 470 ILE P 714 CB CG1 CG2 CD1
REMARK 470 TYR P 715 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR P 715 OH
REMARK 470 ARG P 716 CB CG CD NE CZ NH1 NH2
REMARK 470 TRP P 718 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP P 718 CZ2 CZ3 CH2
REMARK 470 LYS P 719 CB CG CD CE NZ
REMARK 470 CYS P 720 CB SG
REMARK 470 ARG P 721 CB CG CD NE CZ NH1 NH2
REMARK 470 THR P 722 CB OG1 CG2
REMARK 470 HIS P 723 CB CG ND1 CD2 CE1 NE2
REMARK 470 PHE P 724 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU P 725 CB CG CD1 CD2
REMARK 470 LEU P 726 CB CG CD1 CD2
REMARK 470 MET P 727 CB CG SD CE
REMARK 470 LYS P 728 CB CG CD CE NZ
REMARK 470 LEU P 730 CB CG CD1 CD2
REMARK 470 ASN P 731 CB CG OD1 ND2
REMARK 470 ASP P 732 CB CG OD1 OD2
REMARK 470 ILE P 733 CB CG1 CG2 CD1
REMARK 470 PHE P 734 O CB CG CD1 CD2 CE1 CE2
REMARK 470 PHE P 734 CZ
REMARK 470 ALA R 1 CB
REMARK 470 ASP R 2 CB CG OD1 OD2
REMARK 470 GLN R 3 CB CG CD OE1 NE2
REMARK 470 LEU R 4 CB CG CD1 CD2
REMARK 470 THR R 5 CB OG1 CG2
REMARK 470 GLU R 6 CB CG CD OE1 OE2
REMARK 470 GLU R 7 CB CG CD OE1 OE2
REMARK 470 GLN R 8 CB CG CD OE1 NE2
REMARK 470 ILE R 9 CB CG1 CG2 CD1
REMARK 470 ALA R 10 CB
REMARK 470 GLU R 11 CB CG CD OE1 OE2
REMARK 470 PHE R 12 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS R 13 CB CG CD CE NZ
REMARK 470 GLU R 14 CB CG CD OE1 OE2
REMARK 470 ALA R 15 CB
REMARK 470 PHE R 16 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER R 17 CB OG
REMARK 470 LEU R 18 CB CG CD1 CD2
REMARK 470 PHE R 19 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP R 20 CB CG OD1 OD2
REMARK 470 LYS R 21 CB CG CD CE NZ
REMARK 470 ASP R 22 CB CG OD1 OD2
REMARK 470 ASP R 24 CB CG OD1 OD2
REMARK 470 THR R 26 CB OG1 CG2
REMARK 470 ILE R 27 CB CG1 CG2 CD1
REMARK 470 THR R 28 CB OG1 CG2
REMARK 470 THR R 29 CB OG1 CG2
REMARK 470 LYS R 30 CB CG CD CE NZ
REMARK 470 GLU R 31 CB CG CD OE1 OE2
REMARK 470 LEU R 32 CB CG CD1 CD2
REMARK 470 THR R 34 CB OG1 CG2
REMARK 470 VAL R 35 CB CG1 CG2
REMARK 470 MET R 36 CB CG SD CE
REMARK 470 ARG R 37 CB CG CD NE CZ NH1 NH2
REMARK 470 SER R 38 CB OG
REMARK 470 LEU R 39 CB CG CD1 CD2
REMARK 470 GLN R 41 CB CG CD OE1 NE2
REMARK 470 ASN R 42 CB CG OD1 ND2
REMARK 470 PRO R 43 CB CG CD
REMARK 470 THR R 44 CB OG1 CG2
REMARK 470 GLU R 45 CB CG CD OE1 OE2
REMARK 470 ALA R 46 CB
REMARK 470 GLU R 47 CB CG CD OE1 OE2
REMARK 470 LEU R 48 CB CG CD1 CD2
REMARK 470 GLN R 49 CB CG CD OE1 NE2
REMARK 470 ASP R 50 CB CG OD1 OD2
REMARK 470 MET R 51 CB CG SD CE
REMARK 470 ILE R 52 CB CG1 CG2 CD1
REMARK 470 ASN R 53 CB CG OD1 ND2
REMARK 470 GLU R 54 CB CG CD OE1 OE2
REMARK 470 VAL R 55 CB CG1 CG2
REMARK 470 ASP R 56 CB CG OD1 OD2
REMARK 470 ALA R 57 CB
REMARK 470 ASP R 58 CB CG OD1 OD2
REMARK 470 ASN R 60 CB CG OD1 ND2
REMARK 470 THR R 62 CB OG1 CG2
REMARK 470 ILE R 63 CB CG1 CG2 CD1
REMARK 470 ASP R 64 CB CG OD1 OD2
REMARK 470 PHE R 65 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO R 66 CB CG CD
REMARK 470 GLU R 67 CB CG CD OE1 OE2
REMARK 470 PHE R 68 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU R 69 CB CG CD1 CD2
REMARK 470 THR R 70 CB OG1 CG2
REMARK 470 MET R 71 CB CG SD CE
REMARK 470 MET R 72 CB CG SD CE
REMARK 470 ALA R 73 CB
REMARK 470 ARG R 74 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS R 75 CB CG CD CE NZ
REMARK 470 MET R 76 CB CG SD CE
REMARK 470 LYS R 77 CB CG CD CE NZ
REMARK 470 ASP R 78 CB CG OD1 OD2
REMARK 470 THR R 79 CB OG1 CG2
REMARK 470 ASP R 80 CB CG OD1 OD2
REMARK 470 SER R 81 CB OG
REMARK 470 GLU R 82 CB CG CD OE1 OE2
REMARK 470 GLU R 83 CB CG CD OE1 OE2
REMARK 470 GLU R 84 CB CG CD OE1 OE2
REMARK 470 ILE R 85 CB CG1 CG2 CD1
REMARK 470 ARG R 86 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU R 87 CB CG CD OE1 OE2
REMARK 470 ALA R 88 CB
REMARK 470 PHE R 89 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG R 90 CB CG CD NE CZ NH1 NH2
REMARK 470 VAL R 91 CB CG1 CG2
REMARK 470 PHE R 92 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP R 93 CB CG OD1 OD2
REMARK 470 LYS R 94 CB CG CD CE NZ
REMARK 470 ASP R 95 CB CG OD1 OD2
REMARK 470 ASN R 97 CB CG OD1 ND2
REMARK 470 TYR R 99 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR R 99 OH
REMARK 470 ILE R 100 CB CG1 CG2 CD1
REMARK 470 SER R 101 CB OG
REMARK 470 ALA R 102 CB
REMARK 470 ALA R 103 CB
REMARK 470 GLU R 104 CB CG CD OE1 OE2
REMARK 470 LEU R 105 CB CG CD1 CD2
REMARK 470 ARG R 106 CB CG CD NE CZ NH1 NH2
REMARK 470 HIS R 107 CB CG ND1 CD2 CE1 NE2
REMARK 470 VAL R 108 CB CG1 CG2
REMARK 470 MET R 109 CB CG SD CE
REMARK 470 THR R 110 CB OG1 CG2
REMARK 470 ASN R 111 CB CG OD1 ND2
REMARK 470 LEU R 112 CB CG CD1 CD2
REMARK 470 GLU R 114 CB CG CD OE1 OE2
REMARK 470 LYS R 115 CB CG CD CE NZ
REMARK 470 LEU R 116 CB CG CD1 CD2
REMARK 470 THR R 117 CB OG1 CG2
REMARK 470 ASP R 118 CB CG OD1 OD2
REMARK 470 GLU R 119 CB CG CD OE1 OE2
REMARK 470 GLU R 120 CB CG CD OE1 OE2
REMARK 470 VAL R 121 CB CG1 CG2
REMARK 470 ASP R 122 CB CG OD1 OD2
REMARK 470 GLU R 123 CB CG CD OE1 OE2
REMARK 470 MET R 124 CB CG SD CE
REMARK 470 ILE R 125 CB CG1 CG2 CD1
REMARK 470 ARG R 126 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU R 127 CB CG CD OE1 OE2
REMARK 470 ALA R 128 CB
REMARK 470 ASP R 129 CB CG OD1 OD2
REMARK 470 ILE R 130 CB CG1 CG2 CD1
REMARK 470 ASP R 131 CB CG OD1 OD2
REMARK 470 ASP R 133 CB CG OD1 OD2
REMARK 470 GLN R 135 CB CG CD OE1 NE2
REMARK 470 VAL R 136 CB CG1 CG2
REMARK 470 ASN R 137 CB CG OD1 ND2
REMARK 470 TYR R 138 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR R 138 OH
REMARK 470 GLU R 139 CB CG CD OE1 OE2
REMARK 470 GLU R 140 CB CG CD OE1 OE2
REMARK 470 PHE R 141 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL R 142 CB CG1 CG2
REMARK 470 GLN R 143 CB CG CD OE1 NE2
REMARK 470 MET R 144 CB CG SD CE
REMARK 470 MET R 145 CB CG SD CE
REMARK 470 THR R 146 CB OG1 CG2
REMARK 470 ALA R 147 CB
REMARK 470 LYS R 148 O CB CG CD CE NZ
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 CD2 LEU P 142 CE MET P 170 1.61
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 SER A 14 -15.43 -144.00
REMARK 500 ASP A 51 49.92 -92.02
REMARK 500 ARG A 95 65.69 60.19
REMARK 500 ALA A 220 73.06 57.82
REMARK 500 ASP A 244 68.13 61.04
REMARK 500 ASP A 288 31.73 -94.32
REMARK 500 LYS A 336 -11.64 75.24
REMARK 500 GLN A 360 -10.81 75.20
REMARK 500 SER B 14 -15.38 -144.00
REMARK 500 ASP B 51 49.91 -92.05
REMARK 500 ARG B 95 65.61 60.28
REMARK 500 ALA B 220 73.07 57.83
REMARK 500 ASP B 244 68.10 61.09
REMARK 500 ASP B 288 31.85 -94.31
REMARK 500 LYS B 336 -11.67 75.23
REMARK 500 GLN B 360 -10.80 75.16
REMARK 500 SER C 14 -15.37 -144.06
REMARK 500 ASP C 51 49.91 -92.03
REMARK 500 ARG C 95 65.66 60.22
REMARK 500 ALA C 220 73.14 57.73
REMARK 500 ASP C 244 68.07 60.98
REMARK 500 ASP C 288 31.80 -94.35
REMARK 500 LYS C 336 -11.59 75.19
REMARK 500 GLN C 360 -10.81 75.17
REMARK 500 SER D 14 -15.37 -143.99
REMARK 500 ASP D 51 49.91 -92.02
REMARK 500 ARG D 95 65.68 60.26
REMARK 500 ALA D 220 73.13 57.72
REMARK 500 ASP D 244 68.15 61.02
REMARK 500 ASP D 288 31.74 -94.35
REMARK 500 LYS D 336 -11.67 75.17
REMARK 500 GLN D 360 -10.84 75.22
REMARK 500 SER E 14 -15.35 -144.00
REMARK 500 ASP E 51 49.88 -92.02
REMARK 500 ARG E 95 65.68 60.23
REMARK 500 ALA E 220 73.10 57.79
REMARK 500 ASP E 244 68.13 61.02
REMARK 500 ASP E 288 31.78 -94.32
REMARK 500 LYS E 336 -11.64 75.16
REMARK 500 GLN E 360 -10.84 75.21
REMARK 500 ASN P 563 -74.69 -65.11
REMARK 500 LEU P 564 -166.59 170.18
REMARK 500 ARG P 566 83.02 -152.95
REMARK 500 TRP P 656 -51.69 -121.19
REMARK 500 PRO P 690 2.69 -63.24
REMARK 500 LEU R 4 80.79 60.33
REMARK 500 ASN R 42 75.89 58.84
REMARK 500 LYS R 115 70.92 59.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN P 563 LEU P 564 133.51
REMARK 500 LEU P 564 LYS P 565 143.63
REMARK 500 PRO P 568 THR P 569 34.89
REMARK 500 ASN P 591 TYR P 592 -149.40
REMARK 500 ARG P 629 ALA P 630 -137.41
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 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 401 O1B
REMARK 620 2 ADP A 401 O3B 58.1
REMARK 620 3 ADP A 401 O1A 85.9 78.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 401 O1B
REMARK 620 2 ADP B 401 O3B 55.7
REMARK 620 3 ADP B 401 O1A 83.0 77.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP C 401 O1B
REMARK 620 2 ADP C 401 O3B 56.3
REMARK 620 3 ADP C 401 O1A 82.9 77.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP D 401 O1B
REMARK 620 2 ADP D 401 O3B 53.9
REMARK 620 3 ADP D 401 O1A 87.6 71.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP E 401 O1B
REMARK 620 2 ADP E 401 O3B 63.1
REMARK 620 3 ADP E 401 O1A 92.4 77.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7331 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-7329 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-7330 RELATED DB: EMDB
DBREF 6C1H A 1 375 UNP P68135 ACTS_RABIT 3 377
DBREF 6C1H B 1 375 UNP P68135 ACTS_RABIT 3 377
DBREF 6C1H C 1 375 UNP P68135 ACTS_RABIT 3 377
DBREF 6C1H D 1 375 UNP P68135 ACTS_RABIT 3 377
DBREF 6C1H E 1 375 UNP P68135 ACTS_RABIT 3 377
DBREF 6C1H P 6 728 UNP Q05096 MYO1B_RAT 6 728
DBREF 6C1H R 1 148 PDB 6C1H 6C1H 1 148
SEQADV 6C1H GLY P 729 UNP Q05096 EXPRESSION TAG
SEQADV 6C1H LEU P 730 UNP Q05096 EXPRESSION TAG
SEQADV 6C1H ASN P 731 UNP Q05096 EXPRESSION TAG
SEQADV 6C1H ASP P 732 UNP Q05096 EXPRESSION TAG
SEQADV 6C1H ILE P 733 UNP Q05096 EXPRESSION TAG
SEQADV 6C1H PHE P 734 UNP Q05096 EXPRESSION TAG
SEQRES 1 A 375 ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY
SEQRES 2 A 375 SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA
SEQRES 3 A 375 PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG
SEQRES 4 A 375 HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER
SEQRES 5 A 375 TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU
SEQRES 6 A 375 THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE THR ASN
SEQRES 7 A 375 TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR
SEQRES 8 A 375 ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU
SEQRES 9 A 375 LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU
SEQRES 10 A 375 LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO
SEQRES 11 A 375 ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR
SEQRES 12 A 375 ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY
SEQRES 13 A 375 ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR
SEQRES 14 A 375 ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY
SEQRES 15 A 375 ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU
SEQRES 16 A 375 ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE
SEQRES 17 A 375 VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU
SEQRES 18 A 375 ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER
SEQRES 19 A 375 SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL
SEQRES 20 A 375 ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR
SEQRES 21 A 375 LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY
SEQRES 22 A 375 ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP
SEQRES 23 A 375 ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET
SEQRES 24 A 375 SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG
SEQRES 25 A 375 MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET
SEQRES 26 A 375 LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER
SEQRES 27 A 375 VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR
SEQRES 28 A 375 PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU
SEQRES 29 A 375 ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 B 375 ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY
SEQRES 2 B 375 SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA
SEQRES 3 B 375 PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG
SEQRES 4 B 375 HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER
SEQRES 5 B 375 TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU
SEQRES 6 B 375 THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE THR ASN
SEQRES 7 B 375 TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR
SEQRES 8 B 375 ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU
SEQRES 9 B 375 LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU
SEQRES 10 B 375 LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO
SEQRES 11 B 375 ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR
SEQRES 12 B 375 ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY
SEQRES 13 B 375 ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR
SEQRES 14 B 375 ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY
SEQRES 15 B 375 ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU
SEQRES 16 B 375 ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE
SEQRES 17 B 375 VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU
SEQRES 18 B 375 ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER
SEQRES 19 B 375 SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL
SEQRES 20 B 375 ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR
SEQRES 21 B 375 LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY
SEQRES 22 B 375 ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP
SEQRES 23 B 375 ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET
SEQRES 24 B 375 SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG
SEQRES 25 B 375 MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET
SEQRES 26 B 375 LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER
SEQRES 27 B 375 VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR
SEQRES 28 B 375 PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU
SEQRES 29 B 375 ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 C 375 ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY
SEQRES 2 C 375 SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA
SEQRES 3 C 375 PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG
SEQRES 4 C 375 HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER
SEQRES 5 C 375 TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU
SEQRES 6 C 375 THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE THR ASN
SEQRES 7 C 375 TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR
SEQRES 8 C 375 ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU
SEQRES 9 C 375 LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU
SEQRES 10 C 375 LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO
SEQRES 11 C 375 ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR
SEQRES 12 C 375 ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY
SEQRES 13 C 375 ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR
SEQRES 14 C 375 ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY
SEQRES 15 C 375 ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU
SEQRES 16 C 375 ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE
SEQRES 17 C 375 VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU
SEQRES 18 C 375 ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER
SEQRES 19 C 375 SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL
SEQRES 20 C 375 ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR
SEQRES 21 C 375 LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY
SEQRES 22 C 375 ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP
SEQRES 23 C 375 ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET
SEQRES 24 C 375 SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG
SEQRES 25 C 375 MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET
SEQRES 26 C 375 LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER
SEQRES 27 C 375 VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR
SEQRES 28 C 375 PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU
SEQRES 29 C 375 ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 D 375 ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY
SEQRES 2 D 375 SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA
SEQRES 3 D 375 PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG
SEQRES 4 D 375 HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER
SEQRES 5 D 375 TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU
SEQRES 6 D 375 THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE THR ASN
SEQRES 7 D 375 TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR
SEQRES 8 D 375 ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU
SEQRES 9 D 375 LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU
SEQRES 10 D 375 LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO
SEQRES 11 D 375 ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR
SEQRES 12 D 375 ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY
SEQRES 13 D 375 ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR
SEQRES 14 D 375 ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY
SEQRES 15 D 375 ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU
SEQRES 16 D 375 ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE
SEQRES 17 D 375 VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU
SEQRES 18 D 375 ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER
SEQRES 19 D 375 SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL
SEQRES 20 D 375 ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR
SEQRES 21 D 375 LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY
SEQRES 22 D 375 ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP
SEQRES 23 D 375 ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET
SEQRES 24 D 375 SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG
SEQRES 25 D 375 MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET
SEQRES 26 D 375 LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER
SEQRES 27 D 375 VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR
SEQRES 28 D 375 PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU
SEQRES 29 D 375 ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 E 375 ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY
SEQRES 2 E 375 SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA
SEQRES 3 E 375 PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG
SEQRES 4 E 375 HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER
SEQRES 5 E 375 TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU
SEQRES 6 E 375 THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE THR ASN
SEQRES 7 E 375 TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR
SEQRES 8 E 375 ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU
SEQRES 9 E 375 LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU
SEQRES 10 E 375 LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO
SEQRES 11 E 375 ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR
SEQRES 12 E 375 ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY
SEQRES 13 E 375 ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR
SEQRES 14 E 375 ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY
SEQRES 15 E 375 ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU
SEQRES 16 E 375 ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE
SEQRES 17 E 375 VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU
SEQRES 18 E 375 ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER
SEQRES 19 E 375 SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL
SEQRES 20 E 375 ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR
SEQRES 21 E 375 LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY
SEQRES 22 E 375 ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP
SEQRES 23 E 375 ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET
SEQRES 24 E 375 SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG
SEQRES 25 E 375 MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET
SEQRES 26 E 375 LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER
SEQRES 27 E 375 VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR
SEQRES 28 E 375 PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU
SEQRES 29 E 375 ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 P 729 VAL LYS SER SER LEU LEU ASP ASN MET ILE GLY VAL GLY
SEQRES 2 P 729 ASP THR VAL LEU LEU GLU PRO LEU ASN GLU GLU THR PHE
SEQRES 3 P 729 ILE ASP ASN LEU LYS LYS ARG PHE ASP HIS ASN GLU ILE
SEQRES 4 P 729 TYR THR TYR ILE GLY SER VAL VAL ILE SER VAL ASN PRO
SEQRES 5 P 729 TYR ARG SER LEU PRO ILE TYR SER PRO GLU LYS VAL GLU
SEQRES 6 P 729 ASP TYR ARG ASN ARG ASN PHE TYR GLU LEU SER PRO HIS
SEQRES 7 P 729 ILE PHE ALA LEU SER ASP GLU ALA TYR ARG SER LEU ARG
SEQRES 8 P 729 ASP GLN ASP LYS ASP GLN CYS ILE LEU ILE THR GLY GLU
SEQRES 9 P 729 SER GLY ALA GLY LYS THR GLU ALA SER LYS LEU VAL MET
SEQRES 10 P 729 SER TYR VAL ALA ALA VAL CYS GLY LYS GLY ALA GLU VAL
SEQRES 11 P 729 ASN GLN VAL LYS GLU GLN LEU LEU GLN SER THR PRO VAL
SEQRES 12 P 729 LEU GLU ALA PHE GLY ASN ALA LYS THR VAL ARG ASN ASP
SEQRES 13 P 729 ASN SER SER ARG PHE GLY LYS TYR MET ASP ILE GLU PHE
SEQRES 14 P 729 ASP PHE LYS GLY ASP PRO LEU GLY GLY VAL ILE SER ASN
SEQRES 15 P 729 TYR LEU LEU GLU LYS SER ARG VAL VAL LYS GLN PRO ARG
SEQRES 16 P 729 GLY GLU ARG ASN PHE HIS VAL PHE TYR GLN LEU LEU SER
SEQRES 17 P 729 GLY ALA SER GLU GLU LEU LEU HIS LYS LEU LYS LEU GLU
SEQRES 18 P 729 ARG ASP PHE SER ARG TYR ASN TYR LEU SER LEU ASP SER
SEQRES 19 P 729 ALA LYS VAL ASN GLY VAL ASP ASP ALA ALA ASN PHE ARG
SEQRES 20 P 729 THR VAL ARG ASN ALA MET GLN ILE VAL GLY PHE SER ASP
SEQRES 21 P 729 PRO GLU ALA GLU SER VAL LEU GLU VAL VAL ALA ALA VAL
SEQRES 22 P 729 LEU LYS LEU GLY ASN ILE GLU PHE LYS PRO GLU SER ARG
SEQRES 23 P 729 MET ASN GLY LEU ASP GLU SER LYS ILE LYS ASP LYS ASN
SEQRES 24 P 729 GLU LEU LYS GLU ILE CYS GLU LEU THR SER ILE ASP GLN
SEQRES 25 P 729 VAL VAL LEU GLU ARG ALA PHE SER PHE ARG THR VAL GLU
SEQRES 26 P 729 ALA LYS GLN GLU LYS VAL SER THR THR LEU ASN VAL ALA
SEQRES 27 P 729 GLN ALA TYR TYR ALA ARG ASP ALA LEU ALA LYS ASN LEU
SEQRES 28 P 729 TYR SER ARG LEU PHE SER TRP LEU VAL ASN ARG ILE ASN
SEQRES 29 P 729 GLU SER ILE LYS ALA GLN THR LYS VAL ARG LYS LYS VAL
SEQRES 30 P 729 MET GLY VAL LEU ASP ILE TYR GLY PHE GLU ILE PHE GLU
SEQRES 31 P 729 ASP ASN SER PHE GLU GLN PHE ILE ILE ASN TYR CYS ASN
SEQRES 32 P 729 GLU LYS LEU GLN GLN ILE PHE ILE GLU LEU THR LEU LYS
SEQRES 33 P 729 GLU GLU GLN GLU GLU TYR ILE ARG GLU ASP ILE GLU TRP
SEQRES 34 P 729 THR HIS ILE ASP TYR PHE ASN ASN ALA ILE ILE CYS ASP
SEQRES 35 P 729 LEU ILE GLU ASN ASN THR ASN GLY ILE LEU ALA MET LEU
SEQRES 36 P 729 ASP GLU GLU CYS LEU ARG PRO GLY THR VAL THR ASP GLU
SEQRES 37 P 729 THR PHE LEU GLU LYS LEU ASN GLN VAL CYS ALA THR HIS
SEQRES 38 P 729 GLN HIS PHE GLU SER ARG MET SER LYS CYS SER ARG PHE
SEQRES 39 P 729 LEU ASN ASP THR THR LEU PRO HIS SER CYS PHE ARG ILE
SEQRES 40 P 729 GLN HIS TYR ALA GLY LYS VAL LEU TYR GLN VAL GLU GLY
SEQRES 41 P 729 PHE VAL ASP LYS ASN ASN ASP LEU LEU TYR ARG ASP LEU
SEQRES 42 P 729 SER GLN ALA MET TRP LYS ALA GLY HIS ALA LEU ILE LYS
SEQRES 43 P 729 SER LEU PHE PRO GLU GLY ASN PRO ALA LYS VAL ASN LEU
SEQRES 44 P 729 LYS ARG PRO PRO THR ALA GLY SER GLN PHE LYS ALA SER
SEQRES 45 P 729 VAL ALA THR LEU MET LYS ASN LEU GLN THR LYS ASN PRO
SEQRES 46 P 729 ASN TYR ILE ARG CYS ILE LYS PRO ASN ASP LYS LYS ALA
SEQRES 47 P 729 ALA HIS ILE PHE SER GLU SER LEU VAL CYS HIS GLN ILE
SEQRES 48 P 729 ARG TYR LEU GLY LEU LEU GLU ASN VAL ARG VAL ARG ARG
SEQRES 49 P 729 ALA GLY TYR ALA PHE ARG GLN ALA TYR GLU PRO CYS LEU
SEQRES 50 P 729 GLU ARG TYR LYS MET LEU CYS LYS GLN THR TRP PRO HIS
SEQRES 51 P 729 TRP LYS GLY PRO ALA ARG SER GLY VAL GLU VAL LEU PHE
SEQRES 52 P 729 ASN GLU LEU GLU ILE PRO VAL GLU GLU TYR SER PHE GLY
SEQRES 53 P 729 ARG SER LYS ILE PHE ILE ARG ASN PRO ARG THR LEU PHE
SEQRES 54 P 729 GLN LEU GLU ASP LEU ARG LYS GLN ARG LEU GLU ASP LEU
SEQRES 55 P 729 ALA THR LEU ILE GLN LYS ILE TYR ARG GLY TRP LYS CYS
SEQRES 56 P 729 ARG THR HIS PHE LEU LEU MET LYS GLY LEU ASN ASP ILE
SEQRES 57 P 729 PHE
SEQRES 1 R 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 R 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 R 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 R 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 R 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 R 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 R 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 R 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 R 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 R 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 R 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 R 148 MET MET THR ALA LYS
HET ADP A 401 27
HET MG A 402 1
HET ADP B 401 27
HET MG B 402 1
HET ADP C 401 27
HET MG C 402 1
HET ADP D 401 27
HET MG D 402 1
HET ADP E 401 27
HET MG E 402 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 8 ADP 5(C10 H15 N5 O10 P2)
FORMUL 9 MG 5(MG 2+)
HELIX 1 AA1 GLY A 55 LYS A 61 1 7
HELIX 2 AA2 ARG A 62 LEU A 65 5 4
HELIX 3 AA3 ASN A 78 ASN A 92 1 15
HELIX 4 AA4 ALA A 97 HIS A 101 5 5
HELIX 5 AA5 PRO A 112 THR A 126 1 15
HELIX 6 AA6 GLN A 137 ALA A 144 1 8
HELIX 7 AA7 PRO A 172 ILE A 175 5 4
HELIX 8 AA8 ALA A 181 GLY A 197 1 17
HELIX 9 AA9 THR A 202 LEU A 216 1 15
HELIX 10 AB1 ASP A 222 SER A 233 1 12
HELIX 11 AB2 GLY A 251 ARG A 254 5 4
HELIX 12 AB3 PHE A 255 GLN A 263 1 9
HELIX 13 AB4 GLY A 273 LYS A 284 1 12
HELIX 14 AB5 ASP A 286 ASP A 288 5 3
HELIX 15 AB6 ILE A 289 ALA A 295 1 7
HELIX 16 AB7 GLY A 308 ALA A 321 1 14
HELIX 17 AB8 TYR A 337 SER A 348 1 12
HELIX 18 AB9 LEU A 349 MET A 355 5 7
HELIX 19 AC1 GLU A 361 GLY A 366 1 6
HELIX 20 AC2 ILE A 369 CYS A 374 1 6
HELIX 21 AC3 GLY B 55 LYS B 61 1 7
HELIX 22 AC4 ARG B 62 LEU B 65 5 4
HELIX 23 AC5 ASN B 78 ASN B 92 1 15
HELIX 24 AC6 ALA B 97 HIS B 101 5 5
HELIX 25 AC7 PRO B 112 THR B 126 1 15
HELIX 26 AC8 GLN B 137 ALA B 144 1 8
HELIX 27 AC9 PRO B 172 ILE B 175 5 4
HELIX 28 AD1 ALA B 181 GLY B 197 1 17
HELIX 29 AD2 THR B 202 LEU B 216 1 15
HELIX 30 AD3 ASP B 222 SER B 233 1 12
HELIX 31 AD4 GLY B 251 ARG B 254 5 4
HELIX 32 AD5 PHE B 255 GLN B 263 1 9
HELIX 33 AD6 GLY B 273 LYS B 284 1 12
HELIX 34 AD7 ASP B 286 ASP B 288 5 3
HELIX 35 AD8 ILE B 289 ALA B 295 1 7
HELIX 36 AD9 GLY B 308 ALA B 321 1 14
HELIX 37 AE1 TYR B 337 SER B 348 1 12
HELIX 38 AE2 LEU B 349 MET B 355 5 7
HELIX 39 AE3 GLU B 361 GLY B 366 1 6
HELIX 40 AE4 ILE B 369 CYS B 374 1 6
HELIX 41 AE5 GLY C 55 LYS C 61 1 7
HELIX 42 AE6 ARG C 62 LEU C 65 5 4
HELIX 43 AE7 ASN C 78 ASN C 92 1 15
HELIX 44 AE8 ALA C 97 HIS C 101 5 5
HELIX 45 AE9 PRO C 112 THR C 126 1 15
HELIX 46 AF1 GLN C 137 ALA C 144 1 8
HELIX 47 AF2 PRO C 172 ILE C 175 5 4
HELIX 48 AF3 ALA C 181 GLY C 197 1 17
HELIX 49 AF4 THR C 202 LEU C 216 1 15
HELIX 50 AF5 ASP C 222 SER C 233 1 12
HELIX 51 AF6 GLY C 251 ARG C 254 5 4
HELIX 52 AF7 PHE C 255 GLN C 263 1 9
HELIX 53 AF8 GLY C 273 LYS C 284 1 12
HELIX 54 AF9 ASP C 286 ASP C 288 5 3
HELIX 55 AG1 ILE C 289 ALA C 295 1 7
HELIX 56 AG2 GLY C 308 ALA C 321 1 14
HELIX 57 AG3 TYR C 337 SER C 348 1 12
HELIX 58 AG4 LEU C 349 MET C 355 5 7
HELIX 59 AG5 GLU C 361 GLY C 366 1 6
HELIX 60 AG6 ILE C 369 CYS C 374 1 6
HELIX 61 AG7 GLY D 55 LYS D 61 1 7
HELIX 62 AG8 ARG D 62 LEU D 65 5 4
HELIX 63 AG9 ASN D 78 ASN D 92 1 15
HELIX 64 AH1 ALA D 97 HIS D 101 5 5
HELIX 65 AH2 PRO D 112 THR D 126 1 15
HELIX 66 AH3 GLN D 137 ALA D 144 1 8
HELIX 67 AH4 PRO D 172 ILE D 175 5 4
HELIX 68 AH5 ALA D 181 GLY D 197 1 17
HELIX 69 AH6 THR D 202 LEU D 216 1 15
HELIX 70 AH7 ASP D 222 SER D 233 1 12
HELIX 71 AH8 GLY D 251 ARG D 254 5 4
HELIX 72 AH9 PHE D 255 GLN D 263 1 9
HELIX 73 AI1 GLY D 273 LYS D 284 1 12
HELIX 74 AI2 ASP D 286 ASP D 288 5 3
HELIX 75 AI3 ILE D 289 ALA D 295 1 7
HELIX 76 AI4 GLY D 308 ALA D 321 1 14
HELIX 77 AI5 TYR D 337 SER D 348 1 12
HELIX 78 AI6 LEU D 349 MET D 355 5 7
HELIX 79 AI7 GLU D 361 GLY D 366 1 6
HELIX 80 AI8 ILE D 369 CYS D 374 1 6
HELIX 81 AI9 GLY E 55 LYS E 61 1 7
HELIX 82 AJ1 ARG E 62 LEU E 65 5 4
HELIX 83 AJ2 ASN E 78 ASN E 92 1 15
HELIX 84 AJ3 ALA E 97 HIS E 101 5 5
HELIX 85 AJ4 PRO E 112 THR E 126 1 15
HELIX 86 AJ5 GLN E 137 ALA E 144 1 8
HELIX 87 AJ6 PRO E 172 ILE E 175 5 4
HELIX 88 AJ7 ALA E 181 GLY E 197 1 17
HELIX 89 AJ8 THR E 202 LEU E 216 1 15
HELIX 90 AJ9 ASP E 222 SER E 233 1 12
HELIX 91 AK1 GLY E 251 ARG E 254 5 4
HELIX 92 AK2 PHE E 255 GLN E 263 1 9
HELIX 93 AK3 GLY E 273 LYS E 284 1 12
HELIX 94 AK4 ASP E 286 ASP E 288 5 3
HELIX 95 AK5 ILE E 289 ALA E 295 1 7
HELIX 96 AK6 GLY E 308 ALA E 321 1 14
HELIX 97 AK7 TYR E 337 SER E 348 1 12
HELIX 98 AK8 LEU E 349 MET E 355 5 7
HELIX 99 AK9 GLU E 361 GLY E 366 1 6
HELIX 100 AL1 ILE E 369 CYS E 374 1 6
HELIX 101 AL2 ASP P 19 LEU P 23 5 5
HELIX 102 AL3 ASN P 27 HIS P 41 1 15
HELIX 103 AL4 LEU P 61 TYR P 64 5 4
HELIX 104 AL5 SER P 65 ARG P 73 1 9
HELIX 105 AL6 ILE P 84 ASP P 97 1 14
HELIX 106 AL7 GLY P 113 CYS P 129 1 17
HELIX 107 AL8 LYS P 131 GLY P 153 1 23
HELIX 108 AL9 LYS P 192 LYS P 197 1 6
HELIX 109 AM1 PHE P 205 ALA P 215 1 11
HELIX 110 AM2 SER P 216 LEU P 223 1 8
HELIX 111 AM3 ASP P 228 TYR P 232 5 5
HELIX 112 AM4 ASP P 246 GLY P 262 1 17
HELIX 113 AM5 SER P 264 LEU P 281 1 18
HELIX 114 AM6 GLY P 282 ILE P 284 5 3
HELIX 115 AM7 LYS P 303 SER P 314 1 12
HELIX 116 AM8 ASP P 316 SER P 325 1 10
HELIX 117 AM9 ASN P 341 LYS P 373 1 33
HELIX 118 AN1 SER P 398 GLU P 430 1 33
HELIX 119 AN2 ASN P 442 ASN P 451 1 10
HELIX 120 AN3 GLY P 455 ARG P 466 1 12
HELIX 121 AN4 THR P 471 CYS P 483 1 13
HELIX 122 AN5 GLY P 525 ASN P 531 1 7
HELIX 123 AN6 TYR P 535 ALA P 545 1 11
HELIX 124 AN7 HIS P 547 PHE P 554 1 8
HELIX 125 AN8 PRO P 555 ASN P 558 5 4
HELIX 126 AN9 THR P 569 THR P 587 1 19
HELIX 127 AO1 SER P 608 GLY P 620 1 13
HELIX 128 AO2 GLY P 620 ARG P 629 1 10
HELIX 129 AO3 TYR P 638 TYR P 645 1 8
HELIX 130 AO4 LYS P 646 CYS P 649 5 4
HELIX 131 AO5 PRO P 659 LEU P 671 1 13
HELIX 132 AO6 PRO P 674 GLU P 676 5 3
HELIX 133 AO7 ASN P 689 ASN P 731 1 43
HELIX 134 AO8 THR R 5 PHE R 19 1 15
HELIX 135 AO9 GLU R 31 LEU R 39 1 9
HELIX 136 AP1 THR R 44 ASP R 56 1 13
HELIX 137 AP2 ASP R 64 MET R 76 1 13
HELIX 138 AP3 LYS R 77 THR R 79 5 3
HELIX 139 AP4 SER R 81 ASP R 93 1 13
HELIX 140 AP5 ALA R 102 LEU R 112 1 11
HELIX 141 AP6 THR R 117 ASP R 129 1 13
HELIX 142 AP7 GLU R 140 THR R 146 1 7
SHEET 1 AA1 6 ALA A 29 PRO A 32 0
SHEET 2 AA1 6 LEU A 16 PHE A 21 -1 N VAL A 17 O PHE A 31
SHEET 3 AA1 6 LEU A 8 ASN A 12 -1 N VAL A 9 O GLY A 20
SHEET 4 AA1 6 THR A 103 GLU A 107 1 O LEU A 104 N LEU A 8
SHEET 5 AA1 6 ALA A 131 ILE A 136 1 O TYR A 133 N LEU A 105
SHEET 6 AA1 6 ILE A 357 THR A 358 -1 O ILE A 357 N MET A 132
SHEET 1 AA2 2 VAL A 35 GLY A 36 0
SHEET 2 AA2 2 TYR A 53 VAL A 54 -1 O TYR A 53 N GLY A 36
SHEET 1 AA3 2 ILE A 71 GLU A 72 0
SHEET 2 AA3 2 ILE A 75 ILE A 76 -1 O ILE A 75 N GLU A 72
SHEET 1 AA4 5 TYR A 169 ALA A 170 0
SHEET 2 AA4 5 VAL A 163 TYR A 166 -1 N TYR A 166 O TYR A 169
SHEET 3 AA4 5 GLY A 150 LEU A 153 -1 N GLY A 150 O ILE A 165
SHEET 4 AA4 5 ASN A 297 MET A 299 1 O VAL A 298 N ILE A 151
SHEET 5 AA4 5 ILE A 329 ILE A 330 1 O ILE A 330 N ASN A 297
SHEET 1 AA5 2 LYS A 238 GLU A 241 0
SHEET 2 AA5 2 VAL A 247 ILE A 250 -1 O ILE A 248 N TYR A 240
SHEET 1 AA6 6 ALA B 29 PRO B 32 0
SHEET 2 AA6 6 LEU B 16 PHE B 21 -1 N VAL B 17 O PHE B 31
SHEET 3 AA6 6 LEU B 8 ASN B 12 -1 N VAL B 9 O GLY B 20
SHEET 4 AA6 6 THR B 103 GLU B 107 1 O LEU B 104 N LEU B 8
SHEET 5 AA6 6 ALA B 131 ILE B 136 1 O TYR B 133 N LEU B 105
SHEET 6 AA6 6 ILE B 357 THR B 358 -1 O ILE B 357 N MET B 132
SHEET 1 AA7 2 VAL B 35 GLY B 36 0
SHEET 2 AA7 2 TYR B 53 VAL B 54 -1 O TYR B 53 N GLY B 36
SHEET 1 AA8 2 ILE B 71 GLU B 72 0
SHEET 2 AA8 2 ILE B 75 ILE B 76 -1 O ILE B 75 N GLU B 72
SHEET 1 AA9 5 TYR B 169 ALA B 170 0
SHEET 2 AA9 5 VAL B 163 TYR B 166 -1 N TYR B 166 O TYR B 169
SHEET 3 AA9 5 GLY B 150 LEU B 153 -1 N GLY B 150 O ILE B 165
SHEET 4 AA9 5 ASN B 297 MET B 299 1 O VAL B 298 N ILE B 151
SHEET 5 AA9 5 ILE B 329 ILE B 330 1 O ILE B 330 N ASN B 297
SHEET 1 AB1 2 LYS B 238 GLU B 241 0
SHEET 2 AB1 2 VAL B 247 ILE B 250 -1 O ILE B 248 N TYR B 240
SHEET 1 AB2 6 ALA C 29 PRO C 32 0
SHEET 2 AB2 6 LEU C 16 PHE C 21 -1 N VAL C 17 O PHE C 31
SHEET 3 AB2 6 LEU C 8 ASN C 12 -1 N VAL C 9 O GLY C 20
SHEET 4 AB2 6 THR C 103 GLU C 107 1 O LEU C 104 N LEU C 8
SHEET 5 AB2 6 ALA C 131 ILE C 136 1 O TYR C 133 N LEU C 105
SHEET 6 AB2 6 ILE C 357 THR C 358 -1 O ILE C 357 N MET C 132
SHEET 1 AB3 2 VAL C 35 GLY C 36 0
SHEET 2 AB3 2 TYR C 53 VAL C 54 -1 O TYR C 53 N GLY C 36
SHEET 1 AB4 2 ILE C 71 GLU C 72 0
SHEET 2 AB4 2 ILE C 75 ILE C 76 -1 O ILE C 75 N GLU C 72
SHEET 1 AB5 5 TYR C 169 ALA C 170 0
SHEET 2 AB5 5 VAL C 163 TYR C 166 -1 N TYR C 166 O TYR C 169
SHEET 3 AB5 5 GLY C 150 LEU C 153 -1 N GLY C 150 O ILE C 165
SHEET 4 AB5 5 ASN C 297 MET C 299 1 O VAL C 298 N ILE C 151
SHEET 5 AB5 5 ILE C 329 ILE C 330 1 O ILE C 330 N ASN C 297
SHEET 1 AB6 2 LYS C 238 GLU C 241 0
SHEET 2 AB6 2 VAL C 247 ILE C 250 -1 O ILE C 248 N TYR C 240
SHEET 1 AB7 6 ALA D 29 PRO D 32 0
SHEET 2 AB7 6 LEU D 16 PHE D 21 -1 N VAL D 17 O PHE D 31
SHEET 3 AB7 6 LEU D 8 ASN D 12 -1 N VAL D 9 O GLY D 20
SHEET 4 AB7 6 THR D 103 GLU D 107 1 O LEU D 104 N LEU D 8
SHEET 5 AB7 6 ALA D 131 ILE D 136 1 O TYR D 133 N LEU D 105
SHEET 6 AB7 6 ILE D 357 THR D 358 -1 O ILE D 357 N MET D 132
SHEET 1 AB8 2 VAL D 35 GLY D 36 0
SHEET 2 AB8 2 TYR D 53 VAL D 54 -1 O TYR D 53 N GLY D 36
SHEET 1 AB9 2 ILE D 71 GLU D 72 0
SHEET 2 AB9 2 ILE D 75 ILE D 76 -1 O ILE D 75 N GLU D 72
SHEET 1 AC1 5 TYR D 169 ALA D 170 0
SHEET 2 AC1 5 VAL D 163 TYR D 166 -1 N TYR D 166 O TYR D 169
SHEET 3 AC1 5 GLY D 150 LEU D 153 -1 N GLY D 150 O ILE D 165
SHEET 4 AC1 5 ASN D 297 MET D 299 1 O VAL D 298 N ILE D 151
SHEET 5 AC1 5 ILE D 329 ILE D 330 1 O ILE D 330 N ASN D 297
SHEET 1 AC2 2 LYS D 238 GLU D 241 0
SHEET 2 AC2 2 VAL D 247 ILE D 250 -1 O ILE D 248 N TYR D 240
SHEET 1 AC3 6 ALA E 29 PRO E 32 0
SHEET 2 AC3 6 LEU E 16 PHE E 21 -1 N VAL E 17 O PHE E 31
SHEET 3 AC3 6 LEU E 8 ASN E 12 -1 N VAL E 9 O GLY E 20
SHEET 4 AC3 6 THR E 103 GLU E 107 1 O LEU E 104 N LEU E 8
SHEET 5 AC3 6 ALA E 131 ILE E 136 1 O TYR E 133 N LEU E 105
SHEET 6 AC3 6 ILE E 357 THR E 358 -1 O ILE E 357 N MET E 132
SHEET 1 AC4 2 VAL E 35 GLY E 36 0
SHEET 2 AC4 2 TYR E 53 VAL E 54 -1 O TYR E 53 N GLY E 36
SHEET 1 AC5 2 ILE E 71 GLU E 72 0
SHEET 2 AC5 2 ILE E 75 ILE E 76 -1 O ILE E 75 N GLU E 72
SHEET 1 AC6 5 TYR E 169 ALA E 170 0
SHEET 2 AC6 5 VAL E 163 TYR E 166 -1 N TYR E 166 O TYR E 169
SHEET 3 AC6 5 GLY E 150 LEU E 153 -1 N GLY E 150 O ILE E 165
SHEET 4 AC6 5 ASN E 297 MET E 299 1 O VAL E 298 N ILE E 151
SHEET 5 AC6 5 ILE E 329 ILE E 330 1 O ILE E 330 N ASN E 297
SHEET 1 AC7 2 LYS E 238 GLU E 241 0
SHEET 2 AC7 2 VAL E 247 ILE E 250 -1 O ILE E 248 N TYR E 240
SHEET 1 AC8 7 TYR P 45 ILE P 48 0
SHEET 2 AC8 7 VAL P 51 VAL P 55 -1 O ILE P 53 N THR P 46
SHEET 3 AC8 7 ASN P 589 ILE P 596 1 O ARG P 594 N VAL P 52
SHEET 4 AC8 7 GLN P 102 GLY P 108 1 N LEU P 105 O ASN P 591
SHEET 5 AC8 7 LYS P 380 TYR P 389 1 O LEU P 386 N ILE P 106
SHEET 6 AC8 7 GLY P 167 ASP P 175 -1 N LYS P 168 O ASP P 387
SHEET 7 AC8 7 PRO P 180 TYR P 188 -1 O TYR P 188 N GLY P 167
SHEET 1 AC9 2 ASN P 154 ALA P 155 0
SHEET 2 AC9 2 SER P 163 SER P 164 -1 O SER P 163 N ALA P 155
SHEET 1 AD1 2 PHE P 286 GLU P 289 0
SHEET 2 AD1 2 GLU P 297 ILE P 300 -1 O GLU P 297 N GLU P 289
SHEET 1 AD2 2 PHE P 326 GLU P 330 0
SHEET 2 AD2 2 LYS P 335 THR P 339 -1 O THR P 338 N ARG P 327
SHEET 1 AD3 3 PHE P 489 GLU P 490 0
SHEET 2 AD3 3 CYS P 509 HIS P 514 -1 O ARG P 511 N GLU P 490
SHEET 3 AD3 3 GLY P 517 GLN P 522 -1 O TYR P 521 N PHE P 510
SHEET 1 AD4 3 PHE P 634 ALA P 637 0
SHEET 2 AD4 3 LYS P 684 ILE P 687 -1 O ILE P 687 N PHE P 634
SHEET 3 AD4 3 TYR P 678 PHE P 680 -1 N SER P 679 O PHE P 686
SHEET 1 AD5 2 TYR R 99 SER R 101 0
SHEET 2 AD5 2 GLN R 135 ASN R 137 -1 O VAL R 136 N ILE R 100
LINK O1B ADP A 401 MG MG A 402 1555 1555 2.71
LINK O3B ADP A 401 MG MG A 402 1555 1555 2.48
LINK O1A ADP A 401 MG MG A 402 1555 1555 2.16
LINK O1B ADP B 401 MG MG B 402 1555 1555 2.93
LINK O3B ADP B 401 MG MG B 402 1555 1555 2.39
LINK O1A ADP B 401 MG MG B 402 1555 1555 2.23
LINK O1B ADP C 401 MG MG C 402 1555 1555 2.84
LINK O3B ADP C 401 MG MG C 402 1555 1555 2.49
LINK O1A ADP C 401 MG MG C 402 1555 1555 2.17
LINK O1B ADP D 401 MG MG D 402 1555 1555 2.86
LINK O3B ADP D 401 MG MG D 402 1555 1555 2.72
LINK O1A ADP D 401 MG MG D 402 1555 1555 2.19
LINK O1B ADP E 401 MG MG E 402 1555 1555 2.40
LINK O3B ADP E 401 MG MG E 402 1555 1555 2.44
LINK O1A ADP E 401 MG MG E 402 1555 1555 2.19
CISPEP 1 GLU P 24 PRO P 25 0 -8.21
CISPEP 2 ARG P 291 MET P 292 0 1.88
CISPEP 3 GLY P 294 LEU P 295 0 -16.89
CISPEP 4 SER P 494 LYS P 495 0 12.04
CISPEP 5 LYS P 495 CYS P 496 0 12.48
CISPEP 6 SER P 497 ARG P 498 0 9.73
CISPEP 7 TRP P 653 PRO P 654 0 -3.03
CISPEP 8 HIS P 655 TRP P 656 0 -12.87
CISPEP 9 TRP P 656 LYS P 657 0 -12.46
CISPEP 10 GLY P 658 PRO P 659 0 -3.70
CISPEP 11 ASP R 2 GLN R 3 0 25.44
CISPEP 12 GLY R 132 ASP R 133 0 -1.63
SITE 1 AC1 16 GLY A 13 SER A 14 GLY A 15 LEU A 16
SITE 2 AC1 16 LYS A 18 GLY A 156 ASP A 157 ARG A 210
SITE 3 AC1 16 LYS A 213 GLU A 214 GLY A 302 THR A 303
SITE 4 AC1 16 MET A 305 TYR A 306 LYS A 336 MG A 402
SITE 1 AC2 2 GLN A 137 ADP A 401
SITE 1 AC3 17 ASN B 12 GLY B 13 SER B 14 GLY B 15
SITE 2 AC3 17 LEU B 16 LYS B 18 GLY B 156 ASP B 157
SITE 3 AC3 17 ARG B 210 LYS B 213 GLU B 214 GLY B 302
SITE 4 AC3 17 THR B 303 MET B 305 TYR B 306 LYS B 336
SITE 5 AC3 17 MG B 402
SITE 1 AC4 2 GLN B 137 ADP B 401
SITE 1 AC5 16 GLY C 13 SER C 14 GLY C 15 LEU C 16
SITE 2 AC5 16 LYS C 18 GLY C 156 ASP C 157 ARG C 210
SITE 3 AC5 16 LYS C 213 GLU C 214 GLY C 302 THR C 303
SITE 4 AC5 16 MET C 305 TYR C 306 LYS C 336 MG C 402
SITE 1 AC6 2 GLN C 137 ADP C 401
SITE 1 AC7 16 GLY D 13 SER D 14 GLY D 15 LEU D 16
SITE 2 AC7 16 LYS D 18 GLY D 156 ASP D 157 ARG D 210
SITE 3 AC7 16 LYS D 213 GLU D 214 GLY D 302 THR D 303
SITE 4 AC7 16 MET D 305 TYR D 306 LYS D 336 MG D 402
SITE 1 AC8 3 GLN D 137 GLY D 156 ADP D 401
SITE 1 AC9 17 GLY E 13 SER E 14 GLY E 15 LEU E 16
SITE 2 AC9 17 LYS E 18 GLN E 137 GLY E 156 ASP E 157
SITE 3 AC9 17 ARG E 210 LYS E 213 GLU E 214 GLY E 302
SITE 4 AC9 17 THR E 303 MET E 305 TYR E 306 LYS E 336
SITE 5 AC9 17 MG E 402
SITE 1 AD1 2 GLN E 137 ADP E 401
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
