HEADER MOTOR PROTEIN/PROTEIN BINDING 03-DEC-15 5F3Y
TITLE CRYSTAL STRUCTURE OF MYO7B N-MYTH4-FERM-SH3 IN COMPLEX WITH ANKS4B CEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCONVENTIONAL MYOSIN-VIIB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-MYTH4-FERM-SH3, UNP RESIDUES 962-1578;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 4B;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: CEN, UNP RESIDUES 252-352;
COMPND 10 SYNONYM: ANKS4B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: MYO7B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: ANKS4B, HARP;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MOTOR PROTEIN, PROTEIN BINDING, STRUCTURAL PROTEIN, PROTEIN
KEYWDS 2 TRANSPORT, MOTOR PROTEIN-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LI,Y.HE,Q.LU,M.ZHANG
REVDAT 2 08-NOV-23 5F3Y 1 REMARK
REVDAT 1 16-MAR-16 5F3Y 0
JRNL AUTH J.LI,Y.HE,Q.LU,M.ZHANG
JRNL TITL MECHANISTIC BASIS OF ORGANIZATION OF THE
JRNL TITL 2 HARMONIN/USH1C-MEDIATED BRUSH BORDER MICROVILLI TIP-LINK
JRNL TITL 3 COMPLEX
JRNL REF DEV.CELL V. 36 179 2016
JRNL REFN ISSN 1534-5807
JRNL PMID 26812017
JRNL DOI 10.1016/J.DEVCEL.2015.12.020
REMARK 2
REMARK 2 RESOLUTION. 3.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2142: ???)
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) : 3.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 24781
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1288
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 30.7189 - 7.0650 0.89 2671 147 0.1935 0.2195
REMARK 3 2 7.0650 - 5.6189 0.93 2673 148 0.2409 0.2948
REMARK 3 3 5.6189 - 4.9119 0.94 2650 148 0.2120 0.2723
REMARK 3 4 4.9119 - 4.4643 0.92 2584 150 0.1932 0.2375
REMARK 3 5 4.4643 - 4.1451 0.91 2554 149 0.2573 0.2792
REMARK 3 6 4.1451 - 3.9012 0.92 2571 134 0.3050 0.3634
REMARK 3 7 3.9012 - 3.7062 0.94 2611 141 0.2991 0.3402
REMARK 3 8 3.7062 - 3.5451 0.95 2664 139 0.2997 0.3495
REMARK 3 9 3.5451 - 3.4088 0.91 2515 132 0.3602 0.3865
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.530
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 92.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.21
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 : 0.008 4143
REMARK 3 ANGLE : 1.111 5700
REMARK 3 CHIRALITY : 0.062 697
REMARK 3 PLANARITY : 0.008 719
REMARK 3 DIHEDRAL : 13.943 2401
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 972 THROUGH 1251 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2610 51.2034 -4.7002
REMARK 3 T TENSOR
REMARK 3 T11: 0.4570 T22: 1.0982
REMARK 3 T33: 1.0623 T12: 0.0583
REMARK 3 T13: -0.0523 T23: -0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 2.7625 L22: 0.5460
REMARK 3 L33: 0.8920 L12: 1.0025
REMARK 3 L13: 1.2058 L23: 0.1607
REMARK 3 S TENSOR
REMARK 3 S11: 0.1037 S12: 0.1651 S13: -0.6675
REMARK 3 S21: -0.3046 S22: 0.1597 S23: -0.1686
REMARK 3 S31: 0.3644 S32: 0.3477 S33: -0.4077
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1252 THROUGH 1559 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.7321 52.1259 -9.9929
REMARK 3 T TENSOR
REMARK 3 T11: 0.5054 T22: 0.6951
REMARK 3 T33: 0.5979 T12: -0.1445
REMARK 3 T13: -0.0911 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 2.1260 L22: 1.9558
REMARK 3 L33: 1.7983 L12: 0.9199
REMARK 3 L13: 1.3015 L23: 1.0983
REMARK 3 S TENSOR
REMARK 3 S11: 0.0284 S12: -0.8212 S13: 0.0258
REMARK 3 S21: 0.0764 S22: -0.1914 S23: -0.1055
REMARK 3 S31: -0.3162 S32: -0.1583 S33: -0.0662
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 263 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7965 58.2905 5.4387
REMARK 3 T TENSOR
REMARK 3 T11: 1.4607 T22: 1.9109
REMARK 3 T33: 1.8086 T12: -0.2864
REMARK 3 T13: -0.3114 T23: 0.4135
REMARK 3 L TENSOR
REMARK 3 L11: 2.1426 L22: 4.6048
REMARK 3 L33: 2.6009 L12: -1.0081
REMARK 3 L13: 1.0747 L23: -2.8277
REMARK 3 S TENSOR
REMARK 3 S11: -1.7857 S12: -1.5105 S13: -0.3952
REMARK 3 S21: 0.7221 S22: 0.3906 S23: 0.1832
REMARK 3 S31: -0.2988 S32: -0.1876 S33: 0.5824
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 5F3Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215888.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24972
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.88800
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: PHASER
REMARK 200 STARTING MODEL: 3PVL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25%(W/V) PENTAERYTHRITOL ETHOXYLATE
REMARK 280 (3/4 EO/OH), 0.1 M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 48.85450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 98.75800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 98.75800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.42725
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 98.75800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 98.75800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 73.28175
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 98.75800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 98.75800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 24.42725
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 98.75800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 98.75800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 73.28175
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.85450
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: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 GLY A 958
REMARK 465 SER A 959
REMARK 465 GLU A 960
REMARK 465 PHE A 961
REMARK 465 GLU A 962
REMARK 465 GLU A 963
REMARK 465 GLU A 964
REMARK 465 VAL A 965
REMARK 465 ASP A 966
REMARK 465 SER A 967
REMARK 465 LEU A 968
REMARK 465 ALA A 969
REMARK 465 GLU A 970
REMARK 465 TYR A 971
REMARK 465 TYR A 1030
REMARK 465 GLY A 1031
REMARK 465 ARG A 1032
REMARK 465 ASN A 1033
REMARK 465 SER A 1034
REMARK 465 LEU A 1035
REMARK 465 THR A 1036
REMARK 465 GLY A 1037
REMARK 465 SER A 1038
REMARK 465 SER A 1039
REMARK 465 VAL A 1040
REMARK 465 MET A 1041
REMARK 465 ARG A 1042
REMARK 465 GLN A 1043
REMARK 465 ILE A 1044
REMARK 465 HIS A 1045
REMARK 465 ASP A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLY A 1049
REMARK 465 LYS A 1050
REMARK 465 ASP A 1051
REMARK 465 SER A 1052
REMARK 465 VAL A 1053
REMARK 465 THR A 1054
REMARK 465 GLN A 1055
REMARK 465 HIS A 1056
REMARK 465 ASN A 1057
REMARK 465 ARG A 1058
REMARK 465 SER A 1059
REMARK 465 SER A 1060A
REMARK 465 GLN A 1060B
REMARK 465 VAL A 1060C
REMARK 465 ALA A 1060D
REMARK 465 SER A 1060E
REMARK 465 GLN A 1060F
REMARK 465 LEU A 1060G
REMARK 465 ASN A 1060H
REMARK 465 PHE A 1060I
REMARK 465 GLY A 1060J
REMARK 465 GLU A 1060K
REMARK 465 GLU A 1060L
REMARK 465 ALA A 1060M
REMARK 465 PHE A 1060N
REMARK 465 LYS A 1060O
REMARK 465 PHE A 1060P
REMARK 465 ASP A 1060Q
REMARK 465 GLY A 1060R
REMARK 465 PRO A 1060S
REMARK 465 SER A 1364
REMARK 465 LYS A 1365
REMARK 465 ARG A 1440
REMARK 465 ASP A 1441
REMARK 465 ALA A 1442
REMARK 465 PRO A 1443
REMARK 465 GLY A 1444
REMARK 465 GLY A 1445
REMARK 465 MET A 1560
REMARK 465 GLY B 251
REMARK 465 SER B 252
REMARK 465 VAL B 253
REMARK 465 GLU B 254
REMARK 465 GLU B 255
REMARK 465 ASP B 256
REMARK 465 ASP B 257
REMARK 465 ASP B 258
REMARK 465 VAL B 259
REMARK 465 GLN B 260
REMARK 465 HIS B 261
REMARK 465 GLU B 262
REMARK 465 SER B 276
REMARK 465 ARG B 277
REMARK 465 ASN B 278
REMARK 465 ARG B 279
REMARK 465 VAL B 280
REMARK 465 LEU B 281
REMARK 465 ASP B 282
REMARK 465 PHE B 283
REMARK 465 GLU B 284
REMARK 465 ASP B 285
REMARK 465 ILE B 286
REMARK 465 SER B 287
REMARK 465 ASP B 288
REMARK 465 SER B 289
REMARK 465 LYS B 290
REMARK 465 ARG B 291
REMARK 465 GLU B 292
REMARK 465 LEU B 293
REMARK 465 GLY B 294
REMARK 465 PHE B 295
REMARK 465 LYS B 296
REMARK 465 MET B 297
REMARK 465 PRO B 298
REMARK 465 SER B 299
REMARK 465 GLU B 300
REMARK 465 LEU B 301
REMARK 465 PHE B 302
REMARK 465 GLN B 303
REMARK 465 ARG B 304
REMARK 465 GLN B 305
REMARK 465 GLY B 306
REMARK 465 ALA B 307
REMARK 465 ALA B 308
REMARK 465 GLY B 309
REMARK 465 THR B 310
REMARK 465 VAL B 311
REMARK 465 GLU B 312
REMARK 465 GLU B 313
REMARK 465 GLU B 314
REMARK 465 GLU B 315
REMARK 465 GLU B 316
REMARK 465 GLU B 317
REMARK 465 GLU B 318
REMARK 465 GLU B 319
REMARK 465 GLU B 320
REMARK 465 GLU B 321
REMARK 465 GLU B 322
REMARK 465 GLU B 323
REMARK 465 GLU B 324
REMARK 465 LYS B 325
REMARK 465 ARG B 326
REMARK 465 GLU B 327
REMARK 465 ALA B 328
REMARK 465 ASN B 329
REMARK 465 GLY B 330
REMARK 465 THR B 331
REMARK 465 ALA B 332
REMARK 465 GLY B 333
REMARK 465 ASP B 334
REMARK 465 LEU B 335
REMARK 465 PRO B 336
REMARK 465 TRP B 337
REMARK 465 ASP B 338
REMARK 465 GLU B 339
REMARK 465 GLU B 340
REMARK 465 GLU B 341
REMARK 465 VAL B 342
REMARK 465 GLU B 343
REMARK 465 TRP B 344
REMARK 465 GLU B 345
REMARK 465 GLU B 346
REMARK 465 ASP B 347
REMARK 465 ALA B 348
REMARK 465 VAL B 349
REMARK 465 ASP B 350
REMARK 465 ALA B 351
REMARK 465 THR B 352
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 A 975 CG CD CE NZ
REMARK 470 GLN A 982 CG CD OE1 NE2
REMARK 470 LYS A 983 CG CD CE NZ
REMARK 470 LYS A 992 CG CD CE NZ
REMARK 470 ARG A 995 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1002 CG CD OE1 OE2
REMARK 470 ASN A1003 CG OD1 ND2
REMARK 470 ASP A1004 CG OD1 OD2
REMARK 470 ARG A1019 CG CD NE CZ NH1 NH2
REMARK 470 ILE A1061 CG1 CG2 CD1
REMARK 470 ASP A1063 CG OD1 OD2
REMARK 470 ARG A1064 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1070 CG CD OE1 OE2
REMARK 470 LYS A1071 CG CD CE NZ
REMARK 470 MET A1081 CG SD CE
REMARK 470 ARG A1082 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1086 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1095 CG CD CE NZ
REMARK 470 GLU A1099 CG CD OE1 OE2
REMARK 470 LYS A1102 CG CD CE NZ
REMARK 470 ARG A1106 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1124 CG CD OE1 OE2
REMARK 470 ARG A1125 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1128 CG CD CE NZ
REMARK 470 GLN A1136 CG CD OE1 NE2
REMARK 470 ARG A1148 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1150 CG CD OE1 NE2
REMARK 470 ARG A1158 CG CD NE CZ NH1 NH2
REMARK 470 THR A1163 CG2
REMARK 470 LYS A1171 CG CD CE NZ
REMARK 470 LYS A1173 CG CD CE NZ
REMARK 470 LYS A1174 CG CD CE NZ
REMARK 470 GLN A1179 CG CD OE1 NE2
REMARK 470 ARG A1186 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1199 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1203 CG CD OE1 NE2
REMARK 470 GLN A1207 CG CD OE1 NE2
REMARK 470 LYS A1208 CG CD CE NZ
REMARK 470 ARG A1212 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1220 CG CD OE1 NE2
REMARK 470 ASP A1225 CG OD1 OD2
REMARK 470 LYS A1226 CG CD CE NZ
REMARK 470 GLN A1243 CG CD OE1 NE2
REMARK 470 GLN A1246 CG CD OE1 NE2
REMARK 470 ARG A1249 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1251 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1253 CG CD OE1 OE2
REMARK 470 GLN A1255 CG CD OE1 NE2
REMARK 470 ARG A1256 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1257 CG CD OE1 NE2
REMARK 470 LYS A1266 CG CD CE NZ
REMARK 470 GLN A1276 CG CD OE1 NE2
REMARK 470 ARG A1291 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1301 CG CD OE1 OE2
REMARK 470 LYS A1302 CG CD CE NZ
REMARK 470 GLU A1303 CG CD OE1 OE2
REMARK 470 GLU A1304 CG CD OE1 OE2
REMARK 470 GLN A1317 CD OE1 NE2
REMARK 470 LYS A1323 CG CD CE NZ
REMARK 470 ASN A1325 CG OD1 ND2
REMARK 470 GLN A1328 CG CD OE1 NE2
REMARK 470 GLU A1329 CG CD OE1 OE2
REMARK 470 LYS A1338 CG CD CE NZ
REMARK 470 ARG A1341 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1343 CG CD CE NZ
REMARK 470 GLU A1346 CG CD OE1 OE2
REMARK 470 LYS A1347 CG CD CE NZ
REMARK 470 LYS A1358 CG CD CE NZ
REMARK 470 GLN A1360 CG CD OE1 NE2
REMARK 470 TYR A1361 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A1363 CG CD OE1 NE2
REMARK 470 GLU A1392 CG CD OE1 OE2
REMARK 470 ARG A1400 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1403 CG CD CE NZ
REMARK 470 GLN A1405 CG CD OE1 NE2
REMARK 470 GLN A1420 CG CD OE1 NE2
REMARK 470 LYS A1421 CG CD CE NZ
REMARK 470 GLU A1422 CG CD OE1 OE2
REMARK 470 ARG A1423 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1446 CG CD CE NZ
REMARK 470 LYS A1447 CG CD CE NZ
REMARK 470 GLU A1456 CG CD OE1 OE2
REMARK 470 GLU A1458 CG CD OE1 OE2
REMARK 470 GLU A1469 CG CD OE1 OE2
REMARK 470 LYS A1479 CG CD CE NZ
REMARK 470 ARG A1491 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1492 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1495 CG OD1 OD2
REMARK 470 LYS A1503 CG CD CE NZ
REMARK 470 LYS A1504 CG CD CE NZ
REMARK 470 LYS A1512 CG CD CE NZ
REMARK 470 LYS A1513 CG CD CE NZ
REMARK 470 GLU A1520 CG CD OE1 OE2
REMARK 470 LYS A1532 CG CD CE NZ
REMARK 470 THR A1538 OG1 CG2
REMARK 470 LYS A1549 CG CD CE NZ
REMARK 470 GLN A1553 CG CD OE1 NE2
REMARK 470 ARG B 267 CG CD NE CZ NH1 NH2
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 OG1 THR A 1395 O LYS A 1403 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ARG A 1341 OG SER A 1344 8555 2.13
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 THR A1005 -57.08 71.60
REMARK 500 ALA A1258 65.25 39.14
REMARK 500 LEU A1318 -57.12 -129.95
REMARK 500 ARG A1400 -4.89 83.77
REMARK 500 GLU A1422 -0.60 86.91
REMARK 500 LEU A1488 -75.73 -101.34
REMARK 500 THR A1511 73.95 53.06
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 SER A 1062 ASP A 1063 147.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5F3Y A 962 1560 UNP Q99MZ6 MYO7B_MOUSE 962 1578
DBREF 5F3Y B 252 352 UNP Q8K3X6 ANS4B_MOUSE 252 352
SEQADV 5F3Y GLY A 958 UNP Q99MZ6 EXPRESSION TAG
SEQADV 5F3Y SER A 959 UNP Q99MZ6 EXPRESSION TAG
SEQADV 5F3Y GLU A 960 UNP Q99MZ6 EXPRESSION TAG
SEQADV 5F3Y PHE A 961 UNP Q99MZ6 EXPRESSION TAG
SEQADV 5F3Y GLY B 251 UNP Q8K3X6 EXPRESSION TAG
SEQRES 1 A 621 GLY SER GLU PHE GLU GLU GLU VAL ASP SER LEU ALA GLU
SEQRES 2 A 621 TYR THR PHE PRO LYS PHE ALA VAL THR TYR PHE GLN LYS
SEQRES 3 A 621 SER ALA SER HIS THR HIS ILE GLN LYS PRO LEU ARG TYR
SEQRES 4 A 621 PRO LEU LEU TYR HIS GLU ASN ASP THR ASP HIS SER ALA
SEQRES 5 A 621 ALA LEU ASP VAL TRP ILE ILE ILE LEU ARG PHE MET GLY
SEQRES 6 A 621 ASP LEU PRO GLU PRO VAL VAL TYR GLY ARG ASN SER LEU
SEQRES 7 A 621 THR GLY SER SER VAL MET ARG GLN ILE HIS ASP LYS LEU
SEQRES 8 A 621 GLY LYS ASP SER VAL THR GLN HIS ASN ARG SER SER GLN
SEQRES 9 A 621 VAL ALA SER GLN LEU ASN PHE GLY GLU GLU ALA PHE LYS
SEQRES 10 A 621 PHE ASP GLY PRO ILE SER ASP ARG PRO MET SER ASN LEU
SEQRES 11 A 621 GLU LYS VAL HIS PHE ILE VAL GLY TYR ALA ILE MET ARG
SEQRES 12 A 621 PRO GLY LEU ARG ASP GLU ILE TYR CYS GLN ILE CYS LYS
SEQRES 13 A 621 GLN LEU SER GLU ASN TYR LYS THR SER SER ARG ALA ARG
SEQRES 14 A 621 GLY TRP ILE LEU LEU SER LEU CYS LEU GLY CYS PHE PRO
SEQRES 15 A 621 PRO SER GLU ARG PHE MET LYS TYR LEU LEU ASN PHE ILE
SEQRES 16 A 621 SER GLN GLY PRO PRO SER TYR GLY PRO PHE CYS ALA GLU
SEQRES 17 A 621 ARG LEU GLN ARG THR PHE ALA ASN GLY VAL ARG ALA GLU
SEQRES 18 A 621 PRO PRO THR TRP LEU GLU LEU GLN ALA VAL LYS SER LYS
SEQRES 19 A 621 LYS HIS ILE PRO ILE GLN VAL ILE LEU ALA THR GLY ARG
SEQRES 20 A 621 SER LEU THR ILE SER VAL ASP SER ALA SER THR SER ARG
SEQRES 21 A 621 GLU ILE CYS GLN HIS VAL ALA GLN LYS GLN GLY LEU ARG
SEQRES 22 A 621 ASP ASN LEU GLY PHE SER LEU GLN VAL ALA VAL TYR ASP
SEQRES 23 A 621 LYS PHE TRP SER LEU GLY SER GLY CYS ASP HIS LEU MET
SEQRES 24 A 621 ASP ALA VAL ALA GLN CYS GLU GLN LEU ALA ARG GLU ARG
SEQRES 25 A 621 GLY GLU SER GLN ARG GLN ALA PRO TRP ARG ILE TYR PHE
SEQRES 26 A 621 ARG LYS GLU PHE PHE THR PRO TRP HIS ASP SER GLN GLU
SEQRES 27 A 621 ASP PRO VAL SER THR GLU LEU ILE TYR HIS GLN VAL LEU
SEQRES 28 A 621 ARG GLY VAL TRP SER GLY GLU TYR ASN PHE GLU LYS GLU
SEQRES 29 A 621 GLU GLU LEU VAL GLU LEU LEU ALA ARG HIS CYS TYR VAL
SEQRES 30 A 621 GLN LEU GLY ALA THR VAL LYS SER ASN ALA VAL GLN GLU
SEQRES 31 A 621 LEU LEU PRO SER CYS VAL PRO SER LYS LEU TYR ARG THR
SEQRES 32 A 621 LYS SER PRO GLU LYS TRP ALA SER LEU VAL THR ALA ALA
SEQRES 33 A 621 HIS ALA LYS ALA GLN TYR THR GLN SER LYS ALA THR PRO
SEQRES 34 A 621 LEU ALA VAL ARG GLU GLN THR VAL GLU ALA ALA ARG LEU
SEQRES 35 A 621 LEU TRP PRO LEU LEU PHE SER ARG LEU PHE GLU VAL THR
SEQRES 36 A 621 THR LEU SER GLY PRO ARG LEU PRO LYS THR GLN LEU VAL
SEQRES 37 A 621 LEU ALA ILE ASN TRP LYS GLY MET TYR PHE LEU ASP GLN
SEQRES 38 A 621 LYS GLU ARG THR LEU LEU GLY LEU SER PHE ALA GLU VAL
SEQRES 39 A 621 MET GLY LEU VAL ALA ASN ARG ASP ALA PRO GLY GLY LYS
SEQRES 40 A 621 LYS LEU LEU LEU ALA THR LEU GLN GLU GLU TYR GLU PHE
SEQRES 41 A 621 VAL SER PRO SER SER VAL ALA ILE ALA GLU MET VAL ALA
SEQRES 42 A 621 LEU PHE LEU GLY GLY LEU LYS GLU ARG SER VAL PHE ALA
SEQRES 43 A 621 MET ALA LEU GLN ASP ARG ARG ALA THR ASP ASP ILE THR
SEQRES 44 A 621 LEU LEU PRO PHE LYS LYS GLY ASP LEU LEU ILE LEU THR
SEQRES 45 A 621 LYS LYS GLN GLY LEU LEU ALA SER GLU ASN TRP ALA LEU
SEQRES 46 A 621 GLY GLN ASN ASP ARG THR GLY LYS THR GLY LEU VAL PRO
SEQRES 47 A 621 THR ALA CYS LEU TYR THR ILE PRO SER VAL THR LYS PRO
SEQRES 48 A 621 SER THR GLN LEU LEU SER LEU LEU ALA MET
SEQRES 1 B 102 GLY SER VAL GLU GLU ASP ASP ASP VAL GLN HIS GLU SER
SEQRES 2 B 102 ILE LEU ASN ARG PRO GLY LEU GLY SER ILE VAL PHE SER
SEQRES 3 B 102 ARG ASN ARG VAL LEU ASP PHE GLU ASP ILE SER ASP SER
SEQRES 4 B 102 LYS ARG GLU LEU GLY PHE LYS MET PRO SER GLU LEU PHE
SEQRES 5 B 102 GLN ARG GLN GLY ALA ALA GLY THR VAL GLU GLU GLU GLU
SEQRES 6 B 102 GLU GLU GLU GLU GLU GLU GLU GLU GLU LYS ARG GLU ALA
SEQRES 7 B 102 ASN GLY THR ALA GLY ASP LEU PRO TRP ASP GLU GLU GLU
SEQRES 8 B 102 VAL GLU TRP GLU GLU ASP ALA VAL ASP ALA THR
HELIX 1 AA1 THR A 972 PHE A 981 1 10
HELIX 2 AA2 THR A 1005 MET A 1021 1 17
HELIX 3 AA3 SER A 1067 ARG A 1082 1 16
HELIX 4 AA4 GLY A 1084 SER A 1098 1 15
HELIX 5 AA5 LYS A 1102 PHE A 1120 1 19
HELIX 6 AA6 PHE A 1126 GLN A 1136 1 11
HELIX 7 AA7 TYR A 1141 GLY A 1156 1 16
HELIX 8 AA8 THR A 1163 LYS A 1173 1 11
HELIX 9 AA9 THR A 1197 GLY A 1210 1 14
HELIX 10 AB1 HIS A 1236 GLY A 1252 1 17
HELIX 11 AB2 ASP A 1278 GLY A 1296 1 19
HELIX 12 AB3 LYS A 1302 LEU A 1318 1 17
HELIX 13 AB4 LYS A 1323 VAL A 1335 1 13
HELIX 14 AB5 PRO A 1336 ARG A 1341 1 6
HELIX 15 AB6 SER A 1344 GLN A 1360 1 17
HELIX 16 AB7 THR A 1367 TRP A 1383 1 17
HELIX 17 AB8 SER A 1429 ALA A 1431 5 3
HELIX 18 AB9 SER A 1463 SER A 1482 1 20
HELIX 19 AC1 SER A 1551 LEU A 1558 1 8
SHEET 1 AA1 5 SER A1187 VAL A1192 0
SHEET 2 AA1 5 ILE A1176 LEU A1182 -1 N ILE A1178 O ILE A1190
SHEET 3 AA1 5 TRP A1260 LYS A1266 1 O ILE A1262 N ILE A1181
SHEET 4 AA1 5 PHE A1217 VAL A1223 -1 N SER A1218 O ARG A1265
SHEET 5 AA1 5 LYS A1226 SER A1229 -1 O TRP A1228 N VAL A1221
SHEET 1 AA2 7 THR A1424 LEU A1428 0
SHEET 2 AA2 7 MET A1415 LEU A1418 -1 N PHE A1417 O LEU A1425
SHEET 3 AA2 7 LEU A1406 ILE A1410 -1 N ALA A1409 O TYR A1416
SHEET 4 AA2 7 ARG A1389 SER A1397 -1 N VAL A1393 O LEU A1406
SHEET 5 AA2 7 GLU A1456 VAL A1460 -1 O GLU A1458 N LEU A1396
SHEET 6 AA2 7 LYS A1447 THR A1452 -1 N LEU A1450 O TYR A1457
SHEET 7 AA2 7 VAL A1433 ALA A1438 -1 N GLY A1435 O ALA A1451
SHEET 1 AA3 5 THR A1533 PRO A1537 0
SHEET 2 AA3 5 TRP A1522 ASN A1527 -1 N ALA A1523 O VAL A1536
SHEET 3 AA3 5 LEU A1507 ILE A1509 -1 N ILE A1509 O GLN A1526
SHEET 4 AA3 5 PHE A1484 ALA A1487 -1 N ALA A1485 O LEU A1508
SHEET 5 AA3 5 LEU A1541 THR A1543 -1 O TYR A1542 N MET A1486
SHEET 1 AA4 2 ASN B 266 ARG B 267 0
SHEET 2 AA4 2 GLY B 271 SER B 272 -1 O GLY B 271 N ARG B 267
CRYST1 197.516 197.516 97.709 90.00 90.00 90.00 P 41 21 2 8
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 0.005063 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005063 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010234 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
