HEADER CONTRACTILE PROTEIN/PROTEIN TRANSPORT 29-JUL-13 4LX2
TITLE CRYSTAL STRUCTURE OF MYO5A GLOBULAR TAIL DOMAIN IN COMPLEX WITH
TITLE 2 MELANOPHILIN GTBD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCONVENTIONAL MYOSIN-VA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DILUTE DOMAIN RESIDUES 1464-1855;
COMPND 5 SYNONYM: DILUTE MYOSIN HEAVY CHAIN, NON-MUSCLE, MYOSIN HEAVY CHAIN
COMPND 6 12, MYOSIN-12, MYOXIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MELANOPHILIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 176-201;
COMPND 12 SYNONYM: EXOPHILIN-3, LEADEN PROTEIN, SLP HOMOLOG LACKING C2 DOMAINS
COMPND 13 A, SLAC2-A, SYNAPTOTAGMIN-LIKE PROTEIN 2A;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MYO5A, MYH12;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 OTHER_DETAILS: SYNTHESIZED
KEYWDS DIL, CONTRACTILE PROTEIN-PROTEIN TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR O.PYLYPENKO,W.ATTANDA,C.GAUQUELIN,A.HOUDUSSE
REVDAT 4 20-SEP-23 4LX2 1 REMARK
REVDAT 3 15-JAN-14 4LX2 1 JRNL
REVDAT 2 18-DEC-13 4LX2 1 JRNL
REVDAT 1 20-NOV-13 4LX2 0
JRNL AUTH O.PYLYPENKO,W.ATTANDA,C.GAUQUELIN,M.LAHMANI,D.COULIBALY,
JRNL AUTH 2 B.BARON,S.HOOS,M.A.TITUS,P.ENGLAND,A.M.HOUDUSSE
JRNL TITL STRUCTURAL BASIS OF MYOSIN V RAB GTPASE-DEPENDENT CARGO
JRNL TITL 2 RECOGNITION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 20443 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 24248336
JRNL DOI 10.1073/PNAS.1314329110
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869)
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 64346
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3219
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 35.5818 - 4.2635 0.99 2785 147 0.1805 0.1922
REMARK 3 2 4.2635 - 3.3849 1.00 2696 142 0.1434 0.1791
REMARK 3 3 3.3849 - 2.9573 0.99 2686 142 0.1519 0.2095
REMARK 3 4 2.9573 - 2.6870 1.00 2682 141 0.1549 0.1745
REMARK 3 5 2.6870 - 2.4945 1.00 2672 140 0.1499 0.2046
REMARK 3 6 2.4945 - 2.3474 1.00 2670 141 0.1461 0.1685
REMARK 3 7 2.3474 - 2.2299 0.99 2671 140 0.1481 0.1836
REMARK 3 8 2.2299 - 2.1328 0.99 2653 140 0.1491 0.1582
REMARK 3 9 2.1328 - 2.0507 0.99 2613 138 0.1552 0.1789
REMARK 3 10 2.0507 - 1.9800 0.99 2630 138 0.1537 0.1810
REMARK 3 11 1.9800 - 1.9181 1.00 2663 140 0.1557 0.1846
REMARK 3 12 1.9181 - 1.8632 0.99 2623 138 0.1599 0.2063
REMARK 3 13 1.8632 - 1.8142 0.99 2674 141 0.1697 0.1912
REMARK 3 14 1.8142 - 1.7699 1.00 2644 139 0.1867 0.2294
REMARK 3 15 1.7699 - 1.7297 1.00 2628 138 0.1890 0.2666
REMARK 3 16 1.7297 - 1.6929 1.00 2647 140 0.1963 0.2145
REMARK 3 17 1.6929 - 1.6590 1.00 2655 140 0.2084 0.2664
REMARK 3 18 1.6590 - 1.6277 1.00 2643 139 0.2100 0.2448
REMARK 3 19 1.6277 - 1.5986 1.00 2639 139 0.2284 0.2745
REMARK 3 20 1.5986 - 1.5715 1.00 2652 139 0.2432 0.3040
REMARK 3 21 1.5715 - 1.5462 1.00 2636 139 0.2490 0.2953
REMARK 3 22 1.5462 - 1.5224 1.00 2627 139 0.2556 0.2700
REMARK 3 23 1.5224 - 1.5000 1.00 2638 139 0.2846 0.3002
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 56.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.99410
REMARK 3 B22 (A**2) : 0.45470
REMARK 3 B33 (A**2) : -1.44880
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.31600
REMARK 3 B23 (A**2) : 0.00000
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 : 0.011 3145
REMARK 3 ANGLE : 1.279 4274
REMARK 3 CHIRALITY : 0.070 494
REMARK 3 PLANARITY : 0.006 546
REMARK 3 DIHEDRAL : 13.269 1220
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 1470:1853))
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4579 -20.5130 -16.7305
REMARK 3 T TENSOR
REMARK 3 T11: 0.0601 T22: 0.0943
REMARK 3 T33: 0.1121 T12: 0.0226
REMARK 3 T13: 0.0078 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.6431 L22: 0.7609
REMARK 3 L33: 2.3215 L12: 0.4225
REMARK 3 L13: 0.6979 L23: 0.6861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: -0.0541 S13: 0.0411
REMARK 3 S21: -0.0484 S22: -0.0154 S23: 0.0298
REMARK 3 S31: 0.0357 S32: -0.0475 S33: -0.0192
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 185:191))
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7768 -46.6486 -34.7343
REMARK 3 T TENSOR
REMARK 3 T11: 0.6939 T22: 0.1588
REMARK 3 T33: 0.3271 T12: 0.0419
REMARK 3 T13: -0.0226 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.8616 L22: 5.8436
REMARK 3 L33: 1.5858 L12: 1.0333
REMARK 3 L13: -0.1815 L23: 0.1955
REMARK 3 S TENSOR
REMARK 3 S11: 0.0791 S12: 0.0156 S13: -0.1245
REMARK 3 S21: -0.0906 S22: 0.0161 S23: -0.1628
REMARK 3 S31: 0.5039 S32: -0.0476 S33: -0.0999
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 192:196))
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5360 -41.9858 -32.6243
REMARK 3 T TENSOR
REMARK 3 T11: 0.7434 T22: 0.5341
REMARK 3 T33: 0.8151 T12: 0.2611
REMARK 3 T13: 0.0527 T23: -0.1139
REMARK 3 L TENSOR
REMARK 3 L11: 4.8539 L22: 6.3999
REMARK 3 L33: 1.2418 L12: -5.5377
REMARK 3 L13: -2.4225 L23: 2.8157
REMARK 3 S TENSOR
REMARK 3 S11: 0.2679 S12: -0.0704 S13: -0.8390
REMARK 3 S21: -0.0401 S22: 0.1089 S23: -0.3643
REMARK 3 S31: 1.1176 S32: 0.5291 S33: -0.3696
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 4LX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980110
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64638
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 37.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4LX0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MPD, PH 8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.93500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.93500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.55500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 VAL A 1462
REMARK 465 ASN A 1463
REMARK 465 ILE A 1464
REMARK 465 PRO A 1465
REMARK 465 ARG A 1466
REMARK 465 LYS A 1467
REMARK 465 GLU A 1468
REMARK 465 LYS A 1469
REMARK 465 THR A 1632
REMARK 465 ILE A 1633
REMARK 465 GLN A 1634
REMARK 465 GLY A 1635
REMARK 465 VAL A 1636
REMARK 465 SER A 1637
REMARK 465 GLY A 1638
REMARK 465 VAL A 1639
REMARK 465 LYS A 1640
REMARK 465 PRO A 1641
REMARK 465 THR A 1642
REMARK 465 GLY A 1643
REMARK 465 LEU A 1644
REMARK 465 ARG A 1645
REMARK 465 LYS A 1646
REMARK 465 ARG A 1647
REMARK 465 THR A 1648
REMARK 465 SER A 1649
REMARK 465 SER A 1650
REMARK 465 ILE A 1651
REMARK 465 ALA A 1652
REMARK 465 ASP A 1653
REMARK 465 GLU A 1654
REMARK 465 ARG B 176
REMARK 465 ASP B 177
REMARK 465 GLN B 178
REMARK 465 PRO B 179
REMARK 465 LEU B 180
REMARK 465 ASN B 181
REMARK 465 SER B 182
REMARK 465 LYS B 183
REMARK 465 LYS B 184
REMARK 465 GLU B 197
REMARK 465 GLU B 198
REMARK 465 ASP B 199
REMARK 465 SER B 200
REMARK 465 ASP B 201
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 LYS A1479 NZ
REMARK 470 LYS A1484 NZ
REMARK 470 LYS A1494 CE NZ
REMARK 470 LEU A1502 CG CD1 CD2
REMARK 470 GLU A1572 OE2
REMARK 470 GLU A1573 CD OE1 OE2
REMARK 470 LEU A1615 CG CD1 CD2
REMARK 470 ARG A1664 CD NE CZ NH1 NH2
REMARK 470 MET A1715 CE
REMARK 470 GLU A1726 OE2
REMARK 470 LYS A1739 CD CE NZ
REMARK 470 VAL A1787 CG1 CG2
REMARK 470 LYS A1810 CG CD CE NZ
REMARK 470 ASP A1811 OD1
REMARK 470 GLN A1814 CD OE1 NE2
REMARK 470 LYS B 185 CG CD CE NZ
REMARK 470 ARG B 192 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 193 CG OD1 OD2
REMARK 470 VAL B 194 CG1 CG2
REMARK 470 ASP B 195 CG OD1 OD2
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 ILE A1490 -62.74 -128.19
REMARK 500 CYS A1769 53.49 -98.37
REMARK 500 ASN A1788 -166.85 -161.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EPE A 1901
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LWZ RELATED DB: PDB
REMARK 900 RELATED ID: 4LX0 RELATED DB: PDB
REMARK 900 RELATED ID: 4LX1 RELATED DB: PDB
DBREF 4LX2 A 1462 1853 UNP Q9Y4I1 MYO5A_HUMAN 1464 1855
DBREF 4LX2 B 176 201 UNP Q91V27 MELPH_MOUSE 176 201
SEQRES 1 A 392 VAL ASN ILE PRO ARG LYS GLU LYS ASP PHE GLN GLY MET
SEQRES 2 A 392 LEU GLU TYR LYS LYS GLU ASP GLU GLN LYS LEU VAL LYS
SEQRES 3 A 392 ASN LEU ILE LEU GLU LEU LYS PRO ARG GLY VAL ALA VAL
SEQRES 4 A 392 ASN LEU ILE PRO GLY LEU PRO ALA TYR ILE LEU PHE MET
SEQRES 5 A 392 CYS VAL ARG HIS ALA ASP TYR LEU ASN ASP ASP GLN LYS
SEQRES 6 A 392 VAL ARG SER LEU LEU THR SER THR ILE ASN SER ILE LYS
SEQRES 7 A 392 LYS VAL LEU LYS LYS ARG GLY ASP ASP PHE GLU THR VAL
SEQRES 8 A 392 SER PHE TRP LEU SER ASN THR CYS ARG PHE LEU HIS CYS
SEQRES 9 A 392 LEU LYS GLN TYR SER GLY GLU GLU GLY PHE MET LYS HIS
SEQRES 10 A 392 ASN THR SER ARG GLN ASN GLU HIS CYS LEU THR ASN PHE
SEQRES 11 A 392 ASP LEU ALA GLU TYR ARG GLN VAL LEU SER ASP LEU ALA
SEQRES 12 A 392 ILE GLN ILE TYR GLN GLN LEU VAL ARG VAL LEU GLU ASN
SEQRES 13 A 392 ILE LEU GLN PRO MET ILE VAL SER GLY MET LEU GLU HIS
SEQRES 14 A 392 GLU THR ILE GLN GLY VAL SER GLY VAL LYS PRO THR GLY
SEQRES 15 A 392 LEU ARG LYS ARG THR SER SER ILE ALA ASP GLU GLY THR
SEQRES 16 A 392 TYR THR LEU ASP SER ILE LEU ARG GLN LEU ASN SER PHE
SEQRES 17 A 392 HIS SER VAL MET CYS GLN HIS GLY MET ASP PRO GLU LEU
SEQRES 18 A 392 ILE LYS GLN VAL VAL LYS GLN MET PHE TYR ILE ILE GLY
SEQRES 19 A 392 ALA ILE THR LEU ASN ASN LEU LEU LEU ARG LYS ASP MET
SEQRES 20 A 392 CYS SER TRP SER LYS GLY MET GLN ILE ARG TYR ASN VAL
SEQRES 21 A 392 SER GLN LEU GLU GLU TRP LEU ARG ASP LYS ASN LEU MET
SEQRES 22 A 392 ASN SER GLY ALA LYS GLU THR LEU GLU PRO LEU ILE GLN
SEQRES 23 A 392 ALA ALA GLN LEU LEU GLN VAL LYS LYS LYS THR ASP ASP
SEQRES 24 A 392 ASP ALA GLU ALA ILE CYS SER MET CYS ASN ALA LEU THR
SEQRES 25 A 392 THR ALA GLN ILE VAL LYS VAL LEU ASN LEU TYR THR PRO
SEQRES 26 A 392 VAL ASN GLU PHE GLU GLU ARG VAL SER VAL SER PHE ILE
SEQRES 27 A 392 ARG THR ILE GLN MET ARG LEU ARG ASP ARG LYS ASP SER
SEQRES 28 A 392 PRO GLN LEU LEU MET ASP ALA LYS HIS ILE PHE PRO VAL
SEQRES 29 A 392 THR PHE PRO PHE ASN PRO SER SER LEU ALA LEU GLU THR
SEQRES 30 A 392 ILE GLN ILE PRO ALA SER LEU GLY LEU GLY PHE ILE SER
SEQRES 31 A 392 ARG VAL
SEQRES 1 B 26 ARG ASP GLN PRO LEU ASN SER LYS LYS LYS LYS ARG LEU
SEQRES 2 B 26 LEU SER PHE ARG ASP VAL ASP PHE GLU GLU ASP SER ASP
HET EPE A1901 10
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 3 EPE C8 H18 N2 O4 S
FORMUL 4 HOH *436(H2 O)
HELIX 1 1 LYS A 1478 GLU A 1480 5 3
HELIX 2 2 ASP A 1481 ILE A 1490 1 10
HELIX 3 3 GLY A 1497 ASN A 1501 5 5
HELIX 4 4 GLY A 1505 LEU A 1521 1 17
HELIX 5 5 ASP A 1523 GLY A 1546 1 24
HELIX 6 6 ASP A 1548 TYR A 1569 1 22
HELIX 7 7 GLU A 1572 MET A 1576 5 5
HELIX 8 8 THR A 1580 GLU A 1585 1 6
HELIX 9 9 LEU A 1593 GLN A 1620 1 28
HELIX 10 10 MET A 1622 LEU A 1628 1 7
HELIX 11 11 THR A 1658 HIS A 1676 1 19
HELIX 12 12 ASP A 1679 ARG A 1705 1 27
HELIX 13 13 SER A 1710 LYS A 1731 1 22
HELIX 14 14 GLY A 1737 LEU A 1742 1 6
HELIX 15 15 LEU A 1742 VAL A 1754 1 13
HELIX 16 16 THR A 1758 CYS A 1769 1 12
HELIX 17 17 THR A 1773 TYR A 1784 1 12
HELIX 18 18 SER A 1795 LEU A 1806 1 12
HELIX 19 19 ALA A 1835 ILE A 1839 5 5
HELIX 20 20 PRO A 1842 GLY A 1846 5 5
HELIX 21 21 ARG B 192 PHE B 196 5 5
SHEET 1 A 2 MET A1474 GLU A1476 0
SHEET 2 A 2 SER A1851 VAL A1853 -1 O SER A1851 N GLU A1476
SHEET 1 B 2 PHE A1591 ASP A1592 0
SHEET 2 B 2 ARG B 187 LEU B 188 1 O ARG B 187 N ASP A1592
SITE 1 AC1 6 PHE A1471 ASN A1522 ASP A1523 ASP A1524
SITE 2 AC1 6 GLN A1525 HOH A2195
CRYST1 99.870 41.110 109.580 90.00 115.63 90.00 C 1 2 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 0.010013 0.000000 0.004804 0.00000
SCALE2 0.000000 0.024325 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END