HEADER HYDROLASE 19-JUL-13 4BYF
TITLE CRYSTAL STRUCTURE OF HUMAN MYOSIN 1C IN COMPLEX WITH CALMODULIN IN THE
TITLE 2 PRE-POWER STROKE STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCONVENTIONAL MYOSIN-IC;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: MOTOR DOMAIN, RESIDUES 36-760;
COMPND 5 SYNONYM: MYOSIN I BETA, MMI-BETA, MMIB;
COMPND 6 EC: 3.6.4.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CALMODULIN;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: CAM;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL
KEYWDS HYDROLASE, MYO1C, GLUT4 EXOCYTOSIS, ATPASE, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MUNNICH,M.H.TAFT,S.PATHAN-CHHATBAR,D.J.MANSTEIN
REVDAT 3 20-DEC-23 4BYF 1 REMARK LINK
REVDAT 2 14-MAY-14 4BYF 1 JRNL
REVDAT 1 26-MAR-14 4BYF 0
JRNL AUTH S.MUNNICH,M.H.TAFT,D.J.MANSTEIN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN MYOSIN 1C-THE MOTOR IN GLUT4
JRNL TITL 2 EXOCYTOSIS: IMPLICATIONS FOR CA(2+) REGULATION AND 14-3-3
JRNL TITL 3 BINDING.
JRNL REF J.MOL.BIOL. V. 426 2070 2014
JRNL REFN ISSN 0022-2836
JRNL PMID 24636949
JRNL DOI 10.1016/J.JMB.2014.03.004
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 51985
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 2.00
REMARK 3 SHRINKAGE RADIUS : 2.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.834 NULL
REMARK 3 ANGLE : 0.005 NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4BYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1290057287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.06450
REMARK 200 MONOCHROMATOR : SILICON (1 1 1) CHANNEL-CUT
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51985
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 47.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.85000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.150
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1LKX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.2 M SODIUM MALONATE PH
REMARK 280 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 79.22500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.7 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: 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: 3640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.7 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 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 LEU A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 289
REMARK 465 SER A 290
REMARK 465 ILE A 324
REMARK 465 ALA A 325
REMARK 465 LYS A 326
REMARK 465 GLY A 327
REMARK 465 GLU A 328
REMARK 465 GLN A 496
REMARK 465 ARG A 497
REMARK 465 THR A 498
REMARK 465 LEU A 556
REMARK 465 SER A 557
REMARK 465 ASP A 558
REMARK 465 LYS A 559
REMARK 465 ARG A 721
REMARK 465 VAL A 722
REMARK 465 LYS A 723
REMARK 465 ARG A 724
REMARK 465 SER A 725
REMARK 465 LYS B 149
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 LEU C 5
REMARK 465 THR C 6
REMARK 465 ALA C 7
REMARK 465 ARG C 8
REMARK 465 ASP C 9
REMARK 465 GLU C 289
REMARK 465 SER C 290
REMARK 465 ILE C 324
REMARK 465 ALA C 325
REMARK 465 LYS C 326
REMARK 465 GLY C 327
REMARK 465 GLU C 328
REMARK 465 GLN C 496
REMARK 465 ARG C 497
REMARK 465 THR C 498
REMARK 465 GLU C 555
REMARK 465 LEU C 556
REMARK 465 SER C 557
REMARK 465 ASP C 558
REMARK 465 LYS C 559
REMARK 465 ARG C 721
REMARK 465 VAL C 722
REMARK 465 LYS C 723
REMARK 465 ARG C 724
REMARK 465 SER C 725
REMARK 465 MET D 1
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 MG MG A 1000 H2G1 AOV A 1001 1.36
REMARK 500 MG MG C 1000 O2G AOV C 1001 1.59
REMARK 500 O LYS C 451 N LYS C 453 1.97
REMARK 500 O PHE A 627 NH2 ARG A 630 2.08
REMARK 500 OG SER A 375 OG SER A 378 2.09
REMARK 500 O PHE C 627 NH2 ARG C 630 2.13
REMARK 500 O HOH C 2050 O HOH C 2051 2.15
REMARK 500 OE2 GLU A 422 NH2 ARG A 623 2.16
REMARK 500 NH2 ARG A 465 OE2 GLU A 468 2.17
REMARK 500 OG SER C 107 O1G AOV C 1001 2.18
REMARK 500 NZ LYS C 111 O2B AOV C 1001 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 PRO C 79 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 PRO C 562 C - N - CA ANGL. DEV. = 10.3 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 ARG A 96 74.38 45.66
REMARK 500 THR A 125 -62.91 -95.56
REMARK 500 GLU A 130 -74.28 -89.51
REMARK 500 ALA A 134 -2.17 94.30
REMARK 500 LEU A 186 74.51 41.57
REMARK 500 GLN A 236 -2.12 70.77
REMARK 500 ASP A 260 39.84 70.73
REMARK 500 ALA A 285 -78.99 -108.97
REMARK 500 ALA A 286 163.96 172.55
REMARK 500 ASN A 287 -67.78 -129.24
REMARK 500 GLU A 372 -7.39 64.77
REMARK 500 SER A 375 -159.57 -81.44
REMARK 500 TRP A 376 -6.20 94.53
REMARK 500 SER A 397 -168.87 -127.06
REMARK 500 LEU A 419 -63.56 -129.54
REMARK 500 VAL A 448 -63.89 -90.43
REMARK 500 PHE A 452 -20.67 75.26
REMARK 500 ARG A 465 147.20 76.95
REMARK 500 GLU A 468 -64.70 -129.70
REMARK 500 HIS A 484 72.68 43.31
REMARK 500 ALA A 494 -139.97 56.11
REMARK 500 ARG A 499 142.36 -172.07
REMARK 500 ARG A 561 75.35 51.75
REMARK 500 ARG A 677 -71.16 -57.59
REMARK 500 LYS B 22 -114.45 55.75
REMARK 500 ASN B 43 69.27 -117.94
REMARK 500 ASN B 61 -13.45 74.36
REMARK 500 THR C 125 -62.02 -95.38
REMARK 500 GLU C 130 -74.37 -94.49
REMARK 500 LEU C 186 75.32 42.37
REMARK 500 VAL C 233 69.60 -115.73
REMARK 500 GLN C 236 -2.76 68.83
REMARK 500 ALA C 285 -79.72 -107.65
REMARK 500 ALA C 286 160.41 172.37
REMARK 500 ASN C 287 -66.83 -132.59
REMARK 500 VAL C 371 -79.49 -92.48
REMARK 500 SER C 373 167.93 66.56
REMARK 500 SER C 375 -60.81 -98.78
REMARK 500 TRP C 376 -8.20 89.04
REMARK 500 SER C 397 -168.75 -126.61
REMARK 500 LEU C 419 -64.64 -129.10
REMARK 500 VAL C 448 -64.34 -91.26
REMARK 500 PHE C 452 -46.56 58.93
REMARK 500 ARG C 465 150.09 74.90
REMARK 500 GLU C 468 -65.14 -127.36
REMARK 500 HIS C 484 72.33 43.18
REMARK 500 ALA C 494 -138.78 57.64
REMARK 500 ARG C 499 139.00 -172.22
REMARK 500 ARG C 553 -120.88 46.87
REMARK 500 ARG C 677 -70.39 -55.79
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2001 DISTANCE = 7.01 ANGSTROMS
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 A1000 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 112 OG1
REMARK 620 2 SER A 161 OG 89.2
REMARK 620 3 AOV A1001 O1B 103.0 166.3
REMARK 620 4 AOV A1001 O2G 171.5 83.3 84.9
REMARK 620 5 HOH A2010 O 103.2 91.2 80.0 81.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1000 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 112 OG1
REMARK 620 2 SER C 161 OG 84.9
REMARK 620 3 AOV C1001 O1B 83.8 158.6
REMARK 620 4 HOH C2019 O 73.0 75.5 83.8
REMARK 620 5 HOH C2021 O 83.8 96.7 100.1 156.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1000 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 94 OD1
REMARK 620 2 ASP D 96 OD2 133.1
REMARK 620 3 ASN D 98 OD1 92.7 75.7
REMARK 620 4 TYR D 100 O 92.9 131.7 90.7
REMARK 620 N 1 2 3
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 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOV A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOV C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1000
DBREF 4BYF A 1 725 UNP O00159 MYO1C_HUMAN 36 760
DBREF 4BYF B 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4BYF C 1 725 UNP O00159 MYO1C_HUMAN 36 760
DBREF 4BYF D 1 149 UNP P62158 CALM_HUMAN 1 149
SEQRES 1 A 725 MET GLU SER ALA LEU THR ALA ARG ASP ARG VAL GLY VAL
SEQRES 2 A 725 GLN ASP PHE VAL LEU LEU GLU ASN PHE THR SER GLU ALA
SEQRES 3 A 725 ALA PHE ILE GLU ASN LEU ARG ARG ARG PHE ARG GLU ASN
SEQRES 4 A 725 LEU ILE TYR THR TYR ILE GLY PRO VAL LEU VAL SER VAL
SEQRES 5 A 725 ASN PRO TYR ARG ASP LEU GLN ILE TYR SER ARG GLN HIS
SEQRES 6 A 725 MET GLU ARG TYR ARG GLY VAL SER PHE TYR GLU VAL PRO
SEQRES 7 A 725 PRO HIS LEU PHE ALA VAL ALA ASP THR VAL TYR ARG ALA
SEQRES 8 A 725 LEU ARG THR GLU ARG ARG ASP GLN ALA VAL MET ILE SER
SEQRES 9 A 725 GLY GLU SER GLY ALA GLY LYS THR GLU ALA THR LYS ARG
SEQRES 10 A 725 LEU LEU GLN PHE TYR ALA GLU THR CYS PRO ALA PRO GLU
SEQRES 11 A 725 ARG GLY GLY ALA VAL ARG ASP ARG LEU LEU GLN SER ASN
SEQRES 12 A 725 PRO VAL LEU GLU ALA PHE GLY ASN ALA LYS THR LEU ARG
SEQRES 13 A 725 ASN ASP ASN SER SER ARG PHE GLY LYS TYR MET ASP VAL
SEQRES 14 A 725 GLN PHE ASP PHE LYS GLY ALA PRO VAL GLY GLY HIS ILE
SEQRES 15 A 725 LEU SER TYR LEU LEU GLU LYS SER ARG VAL VAL HIS GLN
SEQRES 16 A 725 ASN HIS GLY GLU ARG ASN PHE HIS ILE PHE TYR GLN LEU
SEQRES 17 A 725 LEU GLU GLY GLY GLU GLU GLU THR LEU ARG ARG LEU GLY
SEQRES 18 A 725 LEU GLU ARG ASN PRO GLN SER TYR LEU TYR LEU VAL LYS
SEQRES 19 A 725 GLY GLN CYS ALA LYS VAL SER SER ILE ASN ASP LYS SER
SEQRES 20 A 725 ASP TRP LYS VAL VAL ARG LYS ALA LEU THR VAL ILE ASP
SEQRES 21 A 725 PHE THR GLU ASP GLU VAL GLU ASP LEU LEU SER ILE VAL
SEQRES 22 A 725 ALA SER VAL LEU HIS LEU GLY ASN ILE HIS PHE ALA ALA
SEQRES 23 A 725 ASN GLU GLU SER ASN ALA GLN VAL THR THR GLU ASN GLN
SEQRES 24 A 725 LEU LYS TYR LEU THR ARG LEU LEU SER VAL GLU GLY SER
SEQRES 25 A 725 THR LEU ARG GLU ALA LEU THR HIS ARG LYS ILE ILE ALA
SEQRES 26 A 725 LYS GLY GLU GLU LEU LEU SER PRO LEU ASN LEU GLU GLN
SEQRES 27 A 725 ALA ALA TYR ALA ARG ASP ALA LEU ALA LYS ALA VAL TYR
SEQRES 28 A 725 SER ARG THR PHE THR TRP LEU VAL GLY LYS ILE ASN ARG
SEQRES 29 A 725 SER LEU ALA SER LYS ASP VAL GLU SER PRO SER TRP ARG
SEQRES 30 A 725 SER THR THR VAL LEU GLY LEU LEU ASP ILE TYR GLY PHE
SEQRES 31 A 725 GLU VAL PHE GLN HIS ASN SER PHE GLU GLN PHE CYS ILE
SEQRES 32 A 725 ASN TYR CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU
SEQRES 33 A 725 LEU THR LEU LYS SER GLU GLN GLU GLU TYR GLU ALA GLU
SEQRES 34 A 725 GLY ILE ALA TRP GLU PRO VAL GLN TYR PHE ASN ASN LYS
SEQRES 35 A 725 ILE ILE CYS ASP LEU VAL GLU GLU LYS PHE LYS GLY ILE
SEQRES 36 A 725 ILE SER ILE LEU ASP GLU GLU CYS LEU ARG PRO GLY GLU
SEQRES 37 A 725 ALA THR ASP LEU THR PHE LEU GLU LYS LEU GLU ASP THR
SEQRES 38 A 725 VAL LYS HIS HIS PRO HIS PHE LEU THR HIS LYS LEU ALA
SEQRES 39 A 725 ASP GLN ARG THR ARG LYS SER LEU GLY ARG GLY GLU PHE
SEQRES 40 A 725 ARG LEU LEU HIS TYR ALA GLY GLU VAL THR TYR SER VAL
SEQRES 41 A 725 THR GLY PHE LEU ASP LYS ASN ASN ASP LEU LEU PHE ARG
SEQRES 42 A 725 ASN LEU LYS GLU THR MET CYS SER SER LYS ASN PRO ILE
SEQRES 43 A 725 MET SER GLN CYS PHE ASP ARG SER GLU LEU SER ASP LYS
SEQRES 44 A 725 LYS ARG PRO GLU THR VAL ALA THR GLN PHE LYS MET SER
SEQRES 45 A 725 LEU LEU GLN LEU VAL GLU ILE LEU GLN SER LYS GLU PRO
SEQRES 46 A 725 ALA TYR VAL ARG CYS ILE LYS PRO ASN ASP ALA LYS GLN
SEQRES 47 A 725 PRO GLY ARG PHE ASP GLU VAL LEU ILE ARG HIS GLN VAL
SEQRES 48 A 725 LYS TYR LEU GLY LEU LEU GLU ASN LEU ARG VAL ARG ARG
SEQRES 49 A 725 ALA GLY PHE ALA TYR ARG ARG LYS TYR GLU ALA PHE LEU
SEQRES 50 A 725 GLN ARG TYR LYS SER LEU CYS PRO GLU THR TRP PRO THR
SEQRES 51 A 725 TRP ALA GLY ARG PRO GLN ASP GLY VAL ALA VAL LEU VAL
SEQRES 52 A 725 ARG HIS LEU GLY TYR LYS PRO GLU GLU TYR LYS MET GLY
SEQRES 53 A 725 ARG THR LYS ILE PHE ILE ARG PHE PRO LYS THR LEU PHE
SEQRES 54 A 725 ALA THR GLU ASP ALA LEU GLU VAL ARG ARG GLN SER LEU
SEQRES 55 A 725 ALA THR LYS ILE GLN ALA ALA TRP ARG GLY PHE HIS TRP
SEQRES 56 A 725 ARG GLN LYS PHE LEU ARG VAL LYS ARG SER
SEQRES 1 B 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 B 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 B 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 B 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 B 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 B 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 B 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 B 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 B 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 B 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 B 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 B 149 GLN MET MET THR ALA LYS
SEQRES 1 C 725 MET GLU SER ALA LEU THR ALA ARG ASP ARG VAL GLY VAL
SEQRES 2 C 725 GLN ASP PHE VAL LEU LEU GLU ASN PHE THR SER GLU ALA
SEQRES 3 C 725 ALA PHE ILE GLU ASN LEU ARG ARG ARG PHE ARG GLU ASN
SEQRES 4 C 725 LEU ILE TYR THR TYR ILE GLY PRO VAL LEU VAL SER VAL
SEQRES 5 C 725 ASN PRO TYR ARG ASP LEU GLN ILE TYR SER ARG GLN HIS
SEQRES 6 C 725 MET GLU ARG TYR ARG GLY VAL SER PHE TYR GLU VAL PRO
SEQRES 7 C 725 PRO HIS LEU PHE ALA VAL ALA ASP THR VAL TYR ARG ALA
SEQRES 8 C 725 LEU ARG THR GLU ARG ARG ASP GLN ALA VAL MET ILE SER
SEQRES 9 C 725 GLY GLU SER GLY ALA GLY LYS THR GLU ALA THR LYS ARG
SEQRES 10 C 725 LEU LEU GLN PHE TYR ALA GLU THR CYS PRO ALA PRO GLU
SEQRES 11 C 725 ARG GLY GLY ALA VAL ARG ASP ARG LEU LEU GLN SER ASN
SEQRES 12 C 725 PRO VAL LEU GLU ALA PHE GLY ASN ALA LYS THR LEU ARG
SEQRES 13 C 725 ASN ASP ASN SER SER ARG PHE GLY LYS TYR MET ASP VAL
SEQRES 14 C 725 GLN PHE ASP PHE LYS GLY ALA PRO VAL GLY GLY HIS ILE
SEQRES 15 C 725 LEU SER TYR LEU LEU GLU LYS SER ARG VAL VAL HIS GLN
SEQRES 16 C 725 ASN HIS GLY GLU ARG ASN PHE HIS ILE PHE TYR GLN LEU
SEQRES 17 C 725 LEU GLU GLY GLY GLU GLU GLU THR LEU ARG ARG LEU GLY
SEQRES 18 C 725 LEU GLU ARG ASN PRO GLN SER TYR LEU TYR LEU VAL LYS
SEQRES 19 C 725 GLY GLN CYS ALA LYS VAL SER SER ILE ASN ASP LYS SER
SEQRES 20 C 725 ASP TRP LYS VAL VAL ARG LYS ALA LEU THR VAL ILE ASP
SEQRES 21 C 725 PHE THR GLU ASP GLU VAL GLU ASP LEU LEU SER ILE VAL
SEQRES 22 C 725 ALA SER VAL LEU HIS LEU GLY ASN ILE HIS PHE ALA ALA
SEQRES 23 C 725 ASN GLU GLU SER ASN ALA GLN VAL THR THR GLU ASN GLN
SEQRES 24 C 725 LEU LYS TYR LEU THR ARG LEU LEU SER VAL GLU GLY SER
SEQRES 25 C 725 THR LEU ARG GLU ALA LEU THR HIS ARG LYS ILE ILE ALA
SEQRES 26 C 725 LYS GLY GLU GLU LEU LEU SER PRO LEU ASN LEU GLU GLN
SEQRES 27 C 725 ALA ALA TYR ALA ARG ASP ALA LEU ALA LYS ALA VAL TYR
SEQRES 28 C 725 SER ARG THR PHE THR TRP LEU VAL GLY LYS ILE ASN ARG
SEQRES 29 C 725 SER LEU ALA SER LYS ASP VAL GLU SER PRO SER TRP ARG
SEQRES 30 C 725 SER THR THR VAL LEU GLY LEU LEU ASP ILE TYR GLY PHE
SEQRES 31 C 725 GLU VAL PHE GLN HIS ASN SER PHE GLU GLN PHE CYS ILE
SEQRES 32 C 725 ASN TYR CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU
SEQRES 33 C 725 LEU THR LEU LYS SER GLU GLN GLU GLU TYR GLU ALA GLU
SEQRES 34 C 725 GLY ILE ALA TRP GLU PRO VAL GLN TYR PHE ASN ASN LYS
SEQRES 35 C 725 ILE ILE CYS ASP LEU VAL GLU GLU LYS PHE LYS GLY ILE
SEQRES 36 C 725 ILE SER ILE LEU ASP GLU GLU CYS LEU ARG PRO GLY GLU
SEQRES 37 C 725 ALA THR ASP LEU THR PHE LEU GLU LYS LEU GLU ASP THR
SEQRES 38 C 725 VAL LYS HIS HIS PRO HIS PHE LEU THR HIS LYS LEU ALA
SEQRES 39 C 725 ASP GLN ARG THR ARG LYS SER LEU GLY ARG GLY GLU PHE
SEQRES 40 C 725 ARG LEU LEU HIS TYR ALA GLY GLU VAL THR TYR SER VAL
SEQRES 41 C 725 THR GLY PHE LEU ASP LYS ASN ASN ASP LEU LEU PHE ARG
SEQRES 42 C 725 ASN LEU LYS GLU THR MET CYS SER SER LYS ASN PRO ILE
SEQRES 43 C 725 MET SER GLN CYS PHE ASP ARG SER GLU LEU SER ASP LYS
SEQRES 44 C 725 LYS ARG PRO GLU THR VAL ALA THR GLN PHE LYS MET SER
SEQRES 45 C 725 LEU LEU GLN LEU VAL GLU ILE LEU GLN SER LYS GLU PRO
SEQRES 46 C 725 ALA TYR VAL ARG CYS ILE LYS PRO ASN ASP ALA LYS GLN
SEQRES 47 C 725 PRO GLY ARG PHE ASP GLU VAL LEU ILE ARG HIS GLN VAL
SEQRES 48 C 725 LYS TYR LEU GLY LEU LEU GLU ASN LEU ARG VAL ARG ARG
SEQRES 49 C 725 ALA GLY PHE ALA TYR ARG ARG LYS TYR GLU ALA PHE LEU
SEQRES 50 C 725 GLN ARG TYR LYS SER LEU CYS PRO GLU THR TRP PRO THR
SEQRES 51 C 725 TRP ALA GLY ARG PRO GLN ASP GLY VAL ALA VAL LEU VAL
SEQRES 52 C 725 ARG HIS LEU GLY TYR LYS PRO GLU GLU TYR LYS MET GLY
SEQRES 53 C 725 ARG THR LYS ILE PHE ILE ARG PHE PRO LYS THR LEU PHE
SEQRES 54 C 725 ALA THR GLU ASP ALA LEU GLU VAL ARG ARG GLN SER LEU
SEQRES 55 C 725 ALA THR LYS ILE GLN ALA ALA TRP ARG GLY PHE HIS TRP
SEQRES 56 C 725 ARG GLN LYS PHE LEU ARG VAL LYS ARG SER
SEQRES 1 D 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 D 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 D 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 D 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 D 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 D 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 D 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 D 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 D 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 D 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 D 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 D 149 GLN MET MET THR ALA LYS
HET MG A1000 1
HET AOV A1001 47
HET MG C1000 1
HET AOV C1001 47
HET MG D1000 1
HETNAM MG MAGNESIUM ION
HETNAM AOV ADP ORTHOVANADATE
FORMUL 5 MG 3(MG 2+)
FORMUL 6 AOV 2(C10 H17 N5 O14 P2 V)
FORMUL 10 HOH *194(H2 O)
HELIX 1 1 PHE A 16 LEU A 19 5 4
HELIX 2 2 SER A 24 GLU A 38 1 15
HELIX 3 3 SER A 62 ARG A 70 1 9
HELIX 4 4 SER A 73 VAL A 77 5 5
HELIX 5 5 HIS A 80 GLU A 95 1 16
HELIX 6 6 GLY A 110 CYS A 126 1 17
HELIX 7 7 ALA A 134 GLY A 150 1 17
HELIX 8 8 LYS A 189 VAL A 193 5 5
HELIX 9 9 PHE A 202 GLY A 212 1 11
HELIX 10 10 GLU A 213 LEU A 220 1 8
HELIX 11 11 ASN A 225 TYR A 229 5 5
HELIX 12 12 ASN A 244 ILE A 259 1 16
HELIX 13 13 THR A 262 ILE A 282 1 21
HELIX 14 14 GLU A 297 SER A 308 1 12
HELIX 15 15 GLU A 310 THR A 319 1 10
HELIX 16 16 ASN A 335 ALA A 367 1 33
HELIX 17 17 SER A 397 LEU A 419 1 23
HELIX 18 18 LEU A 419 GLY A 430 1 12
HELIX 19 19 ASN A 441 GLU A 450 1 10
HELIX 20 20 GLY A 454 GLU A 462 1 9
HELIX 21 21 THR A 470 VAL A 482 1 13
HELIX 22 22 GLY A 522 ASN A 528 1 7
HELIX 23 23 PHE A 532 SER A 541 1 10
HELIX 24 24 ASN A 544 PHE A 551 1 8
HELIX 25 25 THR A 564 SER A 582 1 19
HELIX 26 26 ASP A 603 GLY A 615 1 13
HELIX 27 27 GLY A 615 GLY A 626 1 12
HELIX 28 28 TYR A 633 LYS A 641 1 9
HELIX 29 29 SER A 642 CYS A 644 5 3
HELIX 30 30 ARG A 654 GLY A 667 1 14
HELIX 31 31 PHE A 684 PHE A 719 1 36
HELIX 32 32 THR B 6 PHE B 20 1 15
HELIX 33 33 GLU B 32 LEU B 40 1 9
HELIX 34 34 THR B 45 ASP B 57 1 13
HELIX 35 35 PHE B 66 MET B 77 1 12
HELIX 36 36 SER B 82 ASP B 94 1 13
HELIX 37 37 ALA B 103 LEU B 113 1 11
HELIX 38 38 THR B 118 ASP B 130 1 13
HELIX 39 39 TYR B 139 ALA B 148 1 10
HELIX 40 40 PHE C 16 LEU C 19 5 4
HELIX 41 41 SER C 24 GLU C 38 1 15
HELIX 42 42 SER C 62 ARG C 70 1 9
HELIX 43 43 SER C 73 VAL C 77 5 5
HELIX 44 44 HIS C 80 GLU C 95 1 16
HELIX 45 45 GLY C 110 CYS C 126 1 17
HELIX 46 46 VAL C 135 GLY C 150 1 16
HELIX 47 47 LYS C 189 VAL C 193 5 5
HELIX 48 48 PHE C 202 GLY C 212 1 11
HELIX 49 49 GLU C 213 LEU C 220 1 8
HELIX 50 50 ASN C 225 TYR C 229 5 5
HELIX 51 51 ASN C 244 ILE C 259 1 16
HELIX 52 52 THR C 262 ILE C 282 1 21
HELIX 53 53 GLU C 297 SER C 308 1 12
HELIX 54 54 GLU C 310 THR C 319 1 10
HELIX 55 55 ASN C 335 ALA C 367 1 33
HELIX 56 56 SER C 397 LEU C 419 1 23
HELIX 57 57 LEU C 419 GLU C 429 1 11
HELIX 58 58 ASN C 441 GLU C 450 1 10
HELIX 59 59 GLY C 454 GLU C 462 1 9
HELIX 60 60 THR C 470 VAL C 482 1 13
HELIX 61 61 GLY C 522 ASN C 528 1 7
HELIX 62 62 PHE C 532 SER C 541 1 10
HELIX 63 63 ASN C 544 PHE C 551 1 8
HELIX 64 64 THR C 564 SER C 582 1 19
HELIX 65 65 ASP C 603 GLY C 615 1 13
HELIX 66 66 GLY C 615 GLY C 626 1 12
HELIX 67 67 TYR C 633 LYS C 641 1 9
HELIX 68 68 SER C 642 CYS C 644 5 3
HELIX 69 69 ARG C 654 GLY C 667 1 14
HELIX 70 70 PHE C 684 PHE C 719 1 36
HELIX 71 71 THR D 6 PHE D 20 1 15
HELIX 72 72 GLU D 32 LEU D 40 1 9
HELIX 73 73 THR D 45 ASP D 57 1 13
HELIX 74 74 PHE D 66 ASP D 79 1 14
HELIX 75 75 SER D 82 ASP D 94 1 13
HELIX 76 76 ALA D 103 LEU D 113 1 11
HELIX 77 77 THR D 118 ASP D 130 1 13
HELIX 78 78 TYR D 139 ALA D 148 1 10
SHEET 1 AA 7 TYR A 42 ILE A 45 0
SHEET 2 AA 7 VAL A 48 VAL A 52 -1 O VAL A 48 N ILE A 45
SHEET 3 AA 7 GLU A 584 ILE A 591 1 O TYR A 587 N LEU A 49
SHEET 4 AA 7 GLN A 99 SER A 104 1 O ALA A 100 N ALA A 586
SHEET 5 AA 7 THR A 380 ASP A 386 1 O VAL A 381 N GLN A 99
SHEET 6 AA 7 GLY A 164 PHE A 171 -1 O LYS A 165 N ASP A 386
SHEET 7 AA 7 PRO A 177 TYR A 185 -1 N VAL A 178 O GLN A 170
SHEET 1 AB 2 ASN A 151 ALA A 152 0
SHEET 2 AB 2 SER A 160 SER A 161 -1 O SER A 160 N ALA A 152
SHEET 1 AC 2 HIS A 320 LYS A 322 0
SHEET 2 AC 2 LEU A 331 PRO A 333 -1 O SER A 332 N ARG A 321
SHEET 1 AD 3 PHE A 488 LEU A 489 0
SHEET 2 AD 3 GLU A 506 HIS A 511 -1 O ARG A 508 N LEU A 489
SHEET 3 AD 3 GLY A 514 SER A 519 -1 O GLY A 514 N HIS A 511
SHEET 1 AE 3 TYR A 629 LYS A 632 0
SHEET 2 AE 3 LYS A 679 ILE A 682 -1 O ILE A 680 N ARG A 631
SHEET 3 AE 3 TYR A 673 MET A 675 -1 O LYS A 674 N PHE A 681
SHEET 1 BA 2 THR B 27 THR B 29 0
SHEET 2 BA 2 THR B 63 ASP B 65 -1 O ILE B 64 N ILE B 28
SHEET 1 BB 2 TYR B 100 SER B 102 0
SHEET 2 BB 2 GLN B 136 ASN B 138 -1 O VAL B 137 N ILE B 101
SHEET 1 CA 7 TYR C 42 ILE C 45 0
SHEET 2 CA 7 VAL C 48 VAL C 52 -1 O VAL C 48 N ILE C 45
SHEET 3 CA 7 GLU C 584 ILE C 591 1 O TYR C 587 N LEU C 49
SHEET 4 CA 7 GLN C 99 SER C 104 1 O ALA C 100 N ALA C 586
SHEET 5 CA 7 THR C 380 ASP C 386 1 O VAL C 381 N GLN C 99
SHEET 6 CA 7 GLY C 164 PHE C 171 -1 O LYS C 165 N ASP C 386
SHEET 7 CA 7 PRO C 177 TYR C 185 -1 N VAL C 178 O GLN C 170
SHEET 1 CB 2 ASN C 151 ALA C 152 0
SHEET 2 CB 2 SER C 160 SER C 161 -1 O SER C 160 N ALA C 152
SHEET 1 CC 2 HIS C 320 LYS C 322 0
SHEET 2 CC 2 LEU C 331 PRO C 333 -1 O SER C 332 N ARG C 321
SHEET 1 CD 3 PHE C 488 THR C 490 0
SHEET 2 CD 3 GLU C 506 HIS C 511 -1 O ARG C 508 N LEU C 489
SHEET 3 CD 3 GLY C 514 SER C 519 -1 O GLY C 514 N HIS C 511
SHEET 1 CE 3 TYR C 629 LYS C 632 0
SHEET 2 CE 3 LYS C 679 ILE C 682 -1 O ILE C 680 N ARG C 631
SHEET 3 CE 3 TYR C 673 MET C 675 -1 O LYS C 674 N PHE C 681
SHEET 1 DA 2 THR D 27 THR D 29 0
SHEET 2 DA 2 THR D 63 ASP D 65 -1 O ILE D 64 N ILE D 28
SHEET 1 DB 2 TYR D 100 SER D 102 0
SHEET 2 DB 2 GLN D 136 ASN D 138 -1 O VAL D 137 N ILE D 101
LINK OG1 THR A 112 MG MG A1000 1555 1555 1.67
LINK OG SER A 161 MG MG A1000 1555 1555 2.46
LINK MG MG A1000 O1B AOV A1001 1555 1555 2.16
LINK MG MG A1000 O2G AOV A1001 1555 1555 1.99
LINK MG MG A1000 O HOH A2010 1555 1555 2.14
LINK OG1 THR C 112 MG MG C1000 1555 1555 2.10
LINK OG SER C 161 MG MG C1000 1555 1555 2.60
LINK MG MG C1000 O1B AOV C1001 1555 1555 2.24
LINK MG MG C1000 O HOH C2019 1555 1555 1.91
LINK MG MG C1000 O HOH C2021 1555 1555 1.73
LINK OD1 ASP D 94 MG MG D1000 1555 1555 2.15
LINK OD2 ASP D 96 MG MG D1000 1555 1555 2.85
LINK OD1 ASN D 98 MG MG D1000 1555 1555 2.44
LINK O TYR D 100 MG MG D1000 1555 1555 2.38
CISPEP 1 PRO A 374 SER A 375 0 7.50
CISPEP 2 ARG A 499 LYS A 500 0 14.89
CISPEP 3 LYS A 500 SER A 501 0 19.30
CISPEP 4 TRP A 648 PRO A 649 0 -6.27
CISPEP 5 SER C 373 PRO C 374 0 -12.40
CISPEP 6 PRO C 374 SER C 375 0 -19.73
CISPEP 7 ARG C 499 LYS C 500 0 13.38
CISPEP 8 LYS C 500 SER C 501 0 18.62
CISPEP 9 TRP C 648 PRO C 649 0 -7.08
SITE 1 AC1 4 THR A 112 SER A 161 AOV A1001 HOH A2010
SITE 1 AC2 21 ASN A 53 ARG A 56 TYR A 61 GLU A 106
SITE 2 AC2 21 SER A 107 GLY A 108 ALA A 109 GLY A 110
SITE 3 AC2 21 LYS A 111 THR A 112 GLU A 113 ASN A 157
SITE 4 AC2 21 ASN A 159 SER A 160 SER A 161 TYR A 388
SITE 5 AC2 21 GLY A 389 MG A1000 HOH A2010 HOH A2011
SITE 6 AC2 21 HOH A2056
SITE 1 AC3 5 THR C 112 SER C 161 AOV C1001 HOH C2019
SITE 2 AC3 5 HOH C2021
SITE 1 AC4 23 ASN C 53 ARG C 56 TYR C 61 GLU C 106
SITE 2 AC4 23 SER C 107 GLY C 108 ALA C 109 GLY C 110
SITE 3 AC4 23 LYS C 111 THR C 112 GLU C 113 ASN C 157
SITE 4 AC4 23 ASN C 159 SER C 160 SER C 161 TYR C 388
SITE 5 AC4 23 GLY C 389 MG C1000 HOH C2008 HOH C2019
SITE 6 AC4 23 HOH C2021 HOH C2055 HOH C2083
SITE 1 AC5 4 ASP D 94 ASP D 96 ASN D 98 TYR D 100
CRYST1 59.580 158.450 114.340 90.00 91.56 90.00 P 1 21 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 0.016784 0.000000 0.000457 0.00000
SCALE2 0.000000 0.006311 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008749 0.00000
(ATOM LINES ARE NOT SHOWN.)
END