HEADER PROTEIN BINDING 19-SEP-13 4MT7
TITLE CRYSTAL STRUCTURE OF COLLYBISTIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 10-493;
COMPND 5 SYNONYM: COLLYBISTIN, RAC/CDC42 GUANINE NUCLEOTIDE EXCHANGE FACTOR 9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ARHGEF9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTXB1
KEYWDS EXTENDED CONFORMATION, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR D.SCHNEEBERGER,H.SCHINDELIN
REVDAT 2 01-OCT-14 4MT7 1 JRNL
REVDAT 1 13-AUG-14 4MT7 0
JRNL AUTH T.SOYKAN,D.SCHNEEBERGER,G.TRIA,C.BUECHNER,N.BADER,D.SVERGUN,
JRNL AUTH 2 I.TESSMER,A.POULOPOULOS,T.PAPADOPOULOS,F.VAROQUEAUX,
JRNL AUTH 3 H.SCHINDELIN,N.BROSE
JRNL TITL A CONFORMATIONAL SWITCH IN COLLYBISTIN DETERMINES THE
JRNL TITL 2 DIFFERENTIATION OF INHIBITORY POSTSYNAPSES.
JRNL REF EMBO J. V. 33 2113 2014
JRNL REFN ISSN 0261-4189
JRNL PMID 25082542
JRNL DOI 10.15252/EMBJ.201488143
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 11474
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.540
REMARK 3 FREE R VALUE TEST SET COUNT : 865
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 50.8984 - 6.3568 0.99 1871 135 0.1880 0.2125
REMARK 3 2 6.3568 - 5.0471 1.00 1792 141 0.2457 0.2484
REMARK 3 3 5.0471 - 4.4095 0.99 1742 146 0.1867 0.2183
REMARK 3 4 4.4095 - 4.0065 0.99 1767 131 0.2425 0.2763
REMARK 3 5 4.0065 - 3.7194 0.99 1712 159 0.2946 0.3351
REMARK 3 6 3.7194 - 3.5002 0.99 1725 153 0.3506 0.3977
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) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 131.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 120.89
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 : 0.005 2917
REMARK 3 ANGLE : 0.923 3915
REMARK 3 CHIRALITY : 0.072 401
REMARK 3 PLANARITY : 0.003 512
REMARK 3 DIHEDRAL : 17.056 1128
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 45 through 233 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5157 -18.6597 12.8240
REMARK 3 T TENSOR
REMARK 3 T11: 0.7014 T22: 0.7301
REMARK 3 T33: 0.5593 T12: 0.1668
REMARK 3 T13: 0.0381 T23: 0.4281
REMARK 3 L TENSOR
REMARK 3 L11: 6.0402 L22: 5.6561
REMARK 3 L33: 5.0792 L12: 0.0146
REMARK 3 L13: -0.7009 L23: -2.5188
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.9860 S13: 0.9047
REMARK 3 S21: -0.5207 S22: -0.7310 S23: -0.6567
REMARK 3 S31: -0.2957 S32: 0.6011 S33: 0.3312
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 234 through 306 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0627 -51.6849 -9.7989
REMARK 3 T TENSOR
REMARK 3 T11: 0.8435 T22: 0.6035
REMARK 3 T33: 0.6365 T12: 0.1822
REMARK 3 T13: 0.2117 T23: -0.1698
REMARK 3 L TENSOR
REMARK 3 L11: 3.6816 L22: 1.9441
REMARK 3 L33: 2.9471 L12: -0.8335
REMARK 3 L13: 0.0787 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: -0.5578 S12: -0.2777 S13: -0.5094
REMARK 3 S21: 0.5608 S22: -0.1518 S23: -0.0409
REMARK 3 S31: 0.5182 S32: -0.6220 S33: 0.6309
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 307 through 381 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9718 -63.4248 -1.5960
REMARK 3 T TENSOR
REMARK 3 T11: 2.1452 T22: 1.3773
REMARK 3 T33: 1.0322 T12: -0.4028
REMARK 3 T13: 0.2884 T23: 0.3284
REMARK 3 L TENSOR
REMARK 3 L11: 5.4005 L22: 4.9392
REMARK 3 L33: 5.4125 L12: -2.2816
REMARK 3 L13: 0.3881 L23: -2.1864
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.8511 S13: -1.8362
REMARK 3 S21: 1.0710 S22: -0.0288 S23: 0.9659
REMARK 3 S31: 2.4461 S32: -0.5688 S33: 0.5333
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 4MT7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB082334.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : HORIZONTALLY DIFFRACTING SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11560
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 129.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.71400
REMARK 200 R SYM FOR SHELL (I) : 0.71400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 15% PEG 20000, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 64.56000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.56000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.46500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.71500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.46500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.71500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.56000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.46500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.71500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.56000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.46500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.71500
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 -50
REMARK 465 LEU A -49
REMARK 465 ILE A -48
REMARK 465 THR A -47
REMARK 465 GLY A -46
REMARK 465 ASP A -45
REMARK 465 SER A -44
REMARK 465 ILE A -43
REMARK 465 VAL A -42
REMARK 465 SER A -41
REMARK 465 ALA A -40
REMARK 465 GLU A -39
REMARK 465 ALA A -38
REMARK 465 VAL A -37
REMARK 465 TRP A -36
REMARK 465 ASP A -35
REMARK 465 HIS A -34
REMARK 465 VAL A -33
REMARK 465 THR A -32
REMARK 465 MET A -31
REMARK 465 ALA A -30
REMARK 465 ASN A -29
REMARK 465 ARG A -28
REMARK 465 GLY A -27
REMARK 465 VAL A -26
REMARK 465 ALA A -25
REMARK 465 PHE A -24
REMARK 465 LYS A -23
REMARK 465 ALA A -22
REMARK 465 GLY A -21
REMARK 465 ASP A -20
REMARK 465 VAL A -19
REMARK 465 ILE A -18
REMARK 465 LYS A -17
REMARK 465 VAL A -16
REMARK 465 LEU A -15
REMARK 465 ASP A -14
REMARK 465 ALA A -13
REMARK 465 SER A -12
REMARK 465 ASN A -11
REMARK 465 LYS A -10
REMARK 465 ASP A -9
REMARK 465 TRP A -8
REMARK 465 TRP A -7
REMARK 465 TRP A -6
REMARK 465 GLY A -5
REMARK 465 GLN A -4
REMARK 465 ILE A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 GLU A 0
REMARK 465 GLU A 1
REMARK 465 GLY A 2
REMARK 465 TRP A 3
REMARK 465 PHE A 4
REMARK 465 PRO A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 PHE A 8
REMARK 465 VAL A 9
REMARK 465 ARG A 10
REMARK 465 LEU A 11
REMARK 465 TRP A 12
REMARK 465 VAL A 13
REMARK 465 ASN A 14
REMARK 465 GLN A 15
REMARK 465 GLU A 16
REMARK 465 ASP A 17
REMARK 465 GLY A 18
REMARK 465 VAL A 19
REMARK 465 GLU A 20
REMARK 465 GLU A 21
REMARK 465 GLY A 22
REMARK 465 PRO A 23
REMARK 465 SER A 24
REMARK 465 ASP A 25
REMARK 465 VAL A 26
REMARK 465 GLN A 27
REMARK 465 ASN A 28
REMARK 465 GLY A 29
REMARK 465 HIS A 30
REMARK 465 LEU A 31
REMARK 465 ASP A 32
REMARK 465 PRO A 33
REMARK 465 ASN A 34
REMARK 465 SER A 35
REMARK 465 ASP A 36
REMARK 465 CYS A 37
REMARK 465 LEU A 38
REMARK 465 CYS A 39
REMARK 465 LEU A 40
REMARK 465 GLY A 41
REMARK 465 ARG A 42
REMARK 465 PRO A 43
REMARK 465 LEU A 44
REMARK 465 PHE A 382
REMARK 465 GLU A 383
REMARK 465 ILE A 384
REMARK 465 SER A 385
REMARK 465 GLU A 386
REMARK 465 ASN A 387
REMARK 465 GLN A 388
REMARK 465 LYS A 389
REMARK 465 ARG A 390
REMARK 465 GLN A 391
REMARK 465 ALA A 392
REMARK 465 ALA A 393
REMARK 465 MET A 394
REMARK 465 THR A 395
REMARK 465 VAL A 396
REMARK 465 ARG A 397
REMARK 465 LYS A 398
REMARK 465 ALA A 399
REMARK 465 SER A 400
REMARK 465 LYS A 401
REMARK 465 GLN A 402
REMARK 465 LYS A 403
REMARK 465 GLY A 404
REMARK 465 ARG A 405
REMARK 465 VAL A 406
REMARK 465 GLY A 407
REMARK 465 GLU A 408
REMARK 465 GLU A 409
REMARK 465 GLU A 410
REMARK 465 ASN A 411
REMARK 465 GLN A 412
REMARK 465 SER A 413
REMARK 465 LEU A 414
REMARK 465 GLU A 415
REMARK 465 LEU A 416
REMARK 465 LYS A 417
REMARK 465 ARG A 418
REMARK 465 ALA A 419
REMARK 465 CYS A 420
REMARK 465 GLU A 421
REMARK 465 VAL A 422
REMARK 465 LEU A 423
REMARK 465 GLN A 424
REMARK 465 ARG A 425
REMARK 465 LEU A 426
REMARK 465 TRP A 427
REMARK 465 SER A 428
REMARK 465 PRO A 429
REMARK 465 GLY A 430
REMARK 465 LYS A 431
REMARK 465 LYS A 432
REMARK 465 SER A 433
REMARK 465 CYS A 434
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 ASN A 46 50.99 35.50
REMARK 500 ARG A 47 -48.71 169.62
REMARK 500 SER A 88 -175.80 -66.61
REMARK 500 ASN A 98 32.94 -90.74
REMARK 500 ASN A 147 31.96 -95.31
REMARK 500 LEU A 260 11.40 -68.50
REMARK 500 SER A 264 49.06 -176.92
REMARK 500 GLU A 265 127.27 169.10
REMARK 500 ILE A 267 -71.11 -78.88
REMARK 500 HIS A 292 -34.68 84.00
REMARK 500 ILE A 302 -55.06 -123.32
REMARK 500 PHE A 331 -87.36 22.03
REMARK 500 ASN A 332 68.94 86.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE A 331 23.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MT6 RELATED DB: PDB
DBREF 4MT7 A -50 433 UNP Q9QX73 ARHG9_RAT 10 493
SEQADV 4MT7 CYS A 434 UNP Q9QX73 EXPRESSION TAG
SEQRES 1 A 485 MET LEU ILE THR GLY ASP SER ILE VAL SER ALA GLU ALA
SEQRES 2 A 485 VAL TRP ASP HIS VAL THR MET ALA ASN ARG GLY VAL ALA
SEQRES 3 A 485 PHE LYS ALA GLY ASP VAL ILE LYS VAL LEU ASP ALA SER
SEQRES 4 A 485 ASN LYS ASP TRP TRP TRP GLY GLN ILE ASP ASP GLU GLU
SEQRES 5 A 485 GLY TRP PHE PRO ALA SER PHE VAL ARG LEU TRP VAL ASN
SEQRES 6 A 485 GLN GLU ASP GLY VAL GLU GLU GLY PRO SER ASP VAL GLN
SEQRES 7 A 485 ASN GLY HIS LEU ASP PRO ASN SER ASP CYS LEU CYS LEU
SEQRES 8 A 485 GLY ARG PRO LEU GLN ASN ARG ASP GLN MET ARG ALA ASN
SEQRES 9 A 485 VAL ILE ASN GLU ILE MET SER THR GLU ARG HIS TYR ILE
SEQRES 10 A 485 LYS HIS LEU LYS ASP ILE CYS GLU GLY TYR LEU LYS GLN
SEQRES 11 A 485 CYS ARG LYS ARG ARG ASP MET PHE SER ASP GLU GLN LEU
SEQRES 12 A 485 LYS VAL ILE PHE GLY ASN ILE GLU ASP ILE TYR ARG PHE
SEQRES 13 A 485 GLN MET GLY PHE VAL ARG ASP LEU GLU LYS GLN TYR ASN
SEQRES 14 A 485 ASN ASP ASP PRO HIS LEU SER GLU ILE GLY PRO CYS PHE
SEQRES 15 A 485 LEU GLU HIS GLN ASP GLY PHE TRP ILE TYR SER GLU TYR
SEQRES 16 A 485 CYS ASN ASN HIS LEU ASP ALA CYS MET GLU LEU SER LYS
SEQRES 17 A 485 LEU MET LYS ASP SER ARG TYR GLN HIS PHE PHE GLU ALA
SEQRES 18 A 485 CYS ARG LEU LEU GLN GLN MET ILE ASP ILE ALA ILE ASP
SEQRES 19 A 485 GLY PHE LEU LEU THR PRO VAL GLN LYS ILE CYS LYS TYR
SEQRES 20 A 485 PRO LEU GLN LEU ALA GLU LEU LEU LYS TYR THR ALA GLN
SEQRES 21 A 485 ASP HIS SER ASP TYR ARG TYR VAL ALA ALA ALA LEU ALA
SEQRES 22 A 485 VAL MET ARG ASN VAL THR GLN GLN ILE ASN GLU ARG LYS
SEQRES 23 A 485 ARG ARG LEU GLU ASN ILE ASP LYS ILE ALA GLN TRP GLN
SEQRES 24 A 485 ALA SER VAL LEU ASP TRP GLU GLY ASP ASP ILE LEU ASP
SEQRES 25 A 485 ARG SER SER GLU LEU ILE TYR THR GLY GLU MET ALA TRP
SEQRES 26 A 485 ILE TYR GLN PRO TYR GLY ARG ASN GLN GLN ARG VAL PHE
SEQRES 27 A 485 PHE LEU PHE ASP HIS GLN MET VAL LEU CYS LYS LYS ASP
SEQRES 28 A 485 LEU ILE ARG ARG ASP ILE LEU TYR TYR LYS GLY ARG ILE
SEQRES 29 A 485 ASP MET ASP LYS TYR GLU VAL ILE ASP ILE GLU ASP GLY
SEQRES 30 A 485 ARG ASP ASP ASP PHE ASN VAL SER MET LYS ASN ALA PHE
SEQRES 31 A 485 LYS LEU HIS ASN LYS GLU THR GLU GLU VAL HIS LEU PHE
SEQRES 32 A 485 PHE ALA LYS LYS LEU GLU GLU LYS ILE ARG TRP LEU ARG
SEQRES 33 A 485 ALA PHE ARG GLU GLU ARG LYS MET VAL GLN GLU ASP GLU
SEQRES 34 A 485 LYS ILE GLY PHE GLU ILE SER GLU ASN GLN LYS ARG GLN
SEQRES 35 A 485 ALA ALA MET THR VAL ARG LYS ALA SER LYS GLN LYS GLY
SEQRES 36 A 485 ARG VAL GLY GLU GLU GLU ASN GLN SER LEU GLU LEU LYS
SEQRES 37 A 485 ARG ALA CYS GLU VAL LEU GLN ARG LEU TRP SER PRO GLY
SEQRES 38 A 485 LYS LYS SER CYS
HELIX 1 1 GLN A 49 TYR A 76 1 28
HELIX 2 2 TYR A 76 ARG A 83 1 8
HELIX 3 3 SER A 88 GLY A 97 1 10
HELIX 4 4 ASN A 98 GLN A 116 1 19
HELIX 5 5 ASP A 121 SER A 125 5 5
HELIX 6 6 ILE A 127 HIS A 134 1 8
HELIX 7 7 ASP A 136 PHE A 138 5 3
HELIX 8 8 TRP A 139 ASN A 147 1 9
HELIX 9 9 ASN A 147 MET A 159 1 13
HELIX 10 10 ASP A 161 GLN A 175 1 15
HELIX 11 11 ALA A 181 LEU A 186 1 6
HELIX 12 12 LEU A 187 TYR A 206 1 20
HELIX 13 13 ASP A 213 VAL A 251 1 39
HELIX 14 14 ASP A 258 ARG A 262 5 5
HELIX 15 15 LYS A 356 GLY A 381 1 26
SHEET 1 A 7 LEU A 307 ASP A 314 0
SHEET 2 A 7 GLN A 293 LYS A 299 -1 N LEU A 296 O GLY A 311
SHEET 3 A 7 GLN A 283 PHE A 290 -1 N PHE A 288 O VAL A 295
SHEET 4 A 7 LEU A 266 ILE A 275 -1 N TYR A 268 O LEU A 289
SHEET 5 A 7 VAL A 349 PHE A 353 -1 O PHE A 353 N ALA A 273
SHEET 6 A 7 ALA A 338 ASN A 343 -1 N PHE A 339 O PHE A 352
SHEET 7 A 7 TYR A 318 ASP A 322 -1 N GLU A 319 O HIS A 342
SHEET 1 B 2 GLY A 326 ARG A 327 0
SHEET 2 B 2 SER A 334 MET A 335 -1 O MET A 335 N GLY A 326
CISPEP 1 ASP A 330 PHE A 331 0 -6.02
CRYST1 82.930 165.430 129.120 90.00 90.00 90.00 C 2 2 21 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 0.012058 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006045 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007745 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
