HEADER MOTOR PROTEIN 18-JUL-17 5WI4
TITLE CRYSTAL STRUCTURE OF DYNLT1/TCTEX-1 IN COMPLEX WITH ARHGEF2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DYNEIN LIGHT CHAIN TCTEX-TYPE 1,RHO GUANINE NUCLEOTIDE
COMPND 3 EXCHANGE FACTOR 2;
COMPND 4 CHAIN: A, B, C;
COMPND 5 FRAGMENT: UNP RESIDUE 1-113; UNP RESIDUES 139-164;
COMPND 6 SYNONYM: ACTIVATOR OF G-PROTEIN SIGNALING 2,AGS2,T-COMPLEX TESTIS-
COMPND 7 SPECIFIC PROTEIN 1,TCTEX-1,GUANINE NUCLEOTIDE EXCHANGE FACTOR H1,GEF-
COMPND 8 H1,LBC'S FIRST COUSIN,LYMPHOID BLAST CRISIS-LIKE 1,ONCOGENE LFC,
COMPND 9 RHOBIN;
COMPND 10 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: DYNLT1, TCTEL1, TCTEX-1, TCTEX1, ARHGEF2, KIAA0651, LBCL1,
SOURCE 6 LFC;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1
KEYWDS DYNEIN LIGHT CHAIN, RHO GEF, MOTOR PROTEIN, CARGO TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BALAN,N.ISHIYAMA,C.B.MARSHALL,M.IKURA
REVDAT 2 04-OCT-23 5WI4 1 REMARK
REVDAT 1 15-NOV-17 5WI4 0
JRNL AUTH M.J.SANDI,C.B.MARSHALL,M.BALAN,E.COYAUD,M.ZHOU,D.M.MONSON,
JRNL AUTH 2 N.ISHIYAMA,A.A.CHANDRAKUMAR,J.LA ROSE,A.L.COUZENS,
JRNL AUTH 3 A.C.GINGRAS,B.RAUGHT,W.XU,M.IKURA,D.K.MORRISON,R.ROTTAPEL
JRNL TITL MARK3-MEDIATED PHOSPHORYLATION OF ARHGEF2 COUPLES
JRNL TITL 2 MICROTUBULES TO THE ACTIN CYTOSKELETON TO ESTABLISH CELL
JRNL TITL 3 POLARITY.
JRNL REF SCI SIGNAL V. 10 2017
JRNL REFN ESSN 1937-9145
JRNL PMID 29089450
JRNL DOI 10.1126/SCISIGNAL.AAN3286
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.130
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 27423
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.330
REMARK 3 FREE R VALUE TEST SET COUNT : 2010
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 36.8373 - 4.8137 0.93 1962 152 0.1693 0.2058
REMARK 3 2 4.8137 - 3.8220 0.93 1879 143 0.1283 0.1783
REMARK 3 3 3.8220 - 3.3393 0.93 1880 144 0.1447 0.1632
REMARK 3 4 3.3393 - 3.0341 0.93 1857 145 0.1647 0.1850
REMARK 3 5 3.0341 - 2.8167 0.93 1829 143 0.1868 0.2336
REMARK 3 6 2.8167 - 2.6507 0.92 1821 143 0.1979 0.2628
REMARK 3 7 2.6507 - 2.5180 0.92 1822 140 0.1938 0.2370
REMARK 3 8 2.5180 - 2.4084 0.91 1787 145 0.2017 0.2313
REMARK 3 9 2.4084 - 2.3157 0.91 1795 141 0.2052 0.2531
REMARK 3 10 2.3157 - 2.2358 0.91 1780 136 0.2003 0.2322
REMARK 3 11 2.2358 - 2.1659 0.90 1785 139 0.1988 0.2057
REMARK 3 12 2.1659 - 2.1040 0.89 1766 143 0.2042 0.2196
REMARK 3 13 2.1040 - 2.0486 0.89 1741 140 0.2066 0.2576
REMARK 3 14 2.0486 - 2.0000 0.88 1703 137 0.2157 0.2334
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 2874
REMARK 3 ANGLE : 1.043 3897
REMARK 3 CHIRALITY : 0.068 473
REMARK 3 PLANARITY : 0.003 474
REMARK 3 DIHEDRAL : 13.688 983
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 5WI4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000229035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27423
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.4920
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.20
REMARK 200 R MERGE FOR SHELL (I) : 0.34800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.578
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COOT (0.7)
REMARK 200 STARTING MODEL: 1YGT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.33M AMMONIUM SULPHATE, 0.25MM SODIUM
REMARK 280 MALONATE, 7.2MM CALCIUM CHLORIDE, PH 7, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.38600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.69300
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.69300
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.38600
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 228 LIES ON A SPECIAL POSITION.
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 -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 3
REMARK 465 PHE A 4
REMARK 465 GLY A 74
REMARK 465 ALA A 75
REMARK 465 GLY A 114
REMARK 465 GLY A 115
REMARK 465 SER A 116
REMARK 465 ARG A 117
REMARK 465 GLY A 136
REMARK 465 HIS A 137
REMARK 465 PHE A 138
REMARK 465 ASN A 139
REMARK 465 ASP A 140
REMARK 465 GLU A 141
REMARK 465 SER A 142
REMARK 465 PRO A 143
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASP B 3
REMARK 465 PHE B 4
REMARK 465 ASN B 73
REMARK 465 GLY B 74
REMARK 465 ALA B 75
REMARK 465 GLY B 115
REMARK 465 SER B 116
REMARK 465 ARG B 117
REMARK 465 GLY B 136
REMARK 465 HIS B 137
REMARK 465 PHE B 138
REMARK 465 ASN B 139
REMARK 465 ASP B 140
REMARK 465 GLU B 141
REMARK 465 SER B 142
REMARK 465 PRO B 143
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ASP C 3
REMARK 465 PHE C 4
REMARK 465 GLY C 74
REMARK 465 ALA C 75
REMARK 465 GLY C 114
REMARK 465 GLY C 115
REMARK 465 SER C 116
REMARK 465 ALA C 135
REMARK 465 GLY C 136
REMARK 465 HIS C 137
REMARK 465 PHE C 138
REMARK 465 ASN C 139
REMARK 465 ASP C 140
REMARK 465 GLU C 141
REMARK 465 SER C 142
REMARK 465 PRO C 143
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 GLN A 5 CG CD OE1 NE2
REMARK 470 ASN A 73 CG OD1 ND2
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 ARG A 118 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 5 CG CD OE1 NE2
REMARK 470 ARG B 118 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 5 CG CD OE1 NE2
REMARK 470 ASN C 73 CG OD1 ND2
REMARK 470 LYS C 100 CG CD CE NZ
REMARK 470 ILE C 113 CG1 CG2 CD1
REMARK 470 ARG C 117 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 134 CG1 CG2 CD1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 22 CD CE NZ
REMARK 480 GLN A 41 CD OE1 NE2
REMARK 480 GLU A 48 CG CD OE1 OE2
REMARK 480 GLU A 98 CD OE1 OE2
REMARK 480 SER A 124 OG
REMARK 480 LYS A 127 CE NZ
REMARK 480 LYS B 22 CD CE NZ
REMARK 480 ASN B 40 OD1 ND2
REMARK 480 GLN B 41 CG CD OE1 NE2
REMARK 480 GLU B 48 CG CD OE1 OE2
REMARK 480 LYS B 100 CG CD CE NZ
REMARK 480 SER C 37 CA
REMARK 480 GLN C 41 CG CD OE1 NE2
REMARK 480 GLU C 48 CG CD OE1 OE2
REMARK 480 GLN C 71 CG
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 99 -161.49 -127.02
REMARK 500 ASN C 99 -153.92 -126.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201
DBREF 5WI4 A 1 113 UNP P51807 DYLT1_MOUSE 1 113
DBREF 5WI4 A 118 143 UNP Q60875 ARHG2_MOUSE 139 164
DBREF 5WI4 B 1 113 UNP P51807 DYLT1_MOUSE 1 113
DBREF 5WI4 B 118 143 UNP Q60875 ARHG2_MOUSE 139 164
DBREF 5WI4 C 1 113 UNP P51807 DYLT1_MOUSE 1 113
DBREF 5WI4 C 118 143 UNP Q60875 ARHG2_MOUSE 139 164
SEQADV 5WI4 GLY A -1 UNP P51807 EXPRESSION TAG
SEQADV 5WI4 SER A 0 UNP P51807 EXPRESSION TAG
SEQADV 5WI4 GLY A 114 UNP P51807 LINKER
SEQADV 5WI4 GLY A 115 UNP P51807 LINKER
SEQADV 5WI4 SER A 116 UNP P51807 LINKER
SEQADV 5WI4 ARG A 117 UNP P51807 LINKER
SEQADV 5WI4 GLY B -1 UNP P51807 EXPRESSION TAG
SEQADV 5WI4 SER B 0 UNP P51807 EXPRESSION TAG
SEQADV 5WI4 GLY B 114 UNP P51807 LINKER
SEQADV 5WI4 GLY B 115 UNP P51807 LINKER
SEQADV 5WI4 SER B 116 UNP P51807 LINKER
SEQADV 5WI4 ARG B 117 UNP P51807 LINKER
SEQADV 5WI4 GLY C -1 UNP P51807 EXPRESSION TAG
SEQADV 5WI4 SER C 0 UNP P51807 EXPRESSION TAG
SEQADV 5WI4 GLY C 114 UNP P51807 LINKER
SEQADV 5WI4 GLY C 115 UNP P51807 LINKER
SEQADV 5WI4 SER C 116 UNP P51807 LINKER
SEQADV 5WI4 ARG C 117 UNP P51807 LINKER
SEQRES 1 A 145 GLY SER MET GLU ASP PHE GLN ALA SER GLU GLU THR ALA
SEQRES 2 A 145 PHE VAL VAL ASP GLU VAL SER SER ILE VAL LYS GLU ALA
SEQRES 3 A 145 ILE GLU SER ALA ILE GLY GLY ASN ALA TYR GLN HIS SER
SEQRES 4 A 145 LYS VAL ASN GLN TRP THR THR ASN VAL LEU GLU GLN THR
SEQRES 5 A 145 LEU SER GLN LEU THR LYS LEU GLY ARG PRO PHE LYS TYR
SEQRES 6 A 145 ILE VAL THR CYS VAL ILE MET GLN LYS ASN GLY ALA GLY
SEQRES 7 A 145 LEU HIS SER ALA SER SER CYS PHE TRP ASP SER SER THR
SEQRES 8 A 145 ASP GLY SER CYS THR VAL ARG TRP GLU ASN LYS THR MET
SEQRES 9 A 145 TYR CYS ILE VAL SER THR PHE GLY LEU SER ILE GLY GLY
SEQRES 10 A 145 SER ARG ARG GLY LEU SER SER LEU SER LEU ALA LYS SER
SEQRES 11 A 145 VAL SER THR THR ASN ILE ALA GLY HIS PHE ASN ASP GLU
SEQRES 12 A 145 SER PRO
SEQRES 1 B 145 GLY SER MET GLU ASP PHE GLN ALA SER GLU GLU THR ALA
SEQRES 2 B 145 PHE VAL VAL ASP GLU VAL SER SER ILE VAL LYS GLU ALA
SEQRES 3 B 145 ILE GLU SER ALA ILE GLY GLY ASN ALA TYR GLN HIS SER
SEQRES 4 B 145 LYS VAL ASN GLN TRP THR THR ASN VAL LEU GLU GLN THR
SEQRES 5 B 145 LEU SER GLN LEU THR LYS LEU GLY ARG PRO PHE LYS TYR
SEQRES 6 B 145 ILE VAL THR CYS VAL ILE MET GLN LYS ASN GLY ALA GLY
SEQRES 7 B 145 LEU HIS SER ALA SER SER CYS PHE TRP ASP SER SER THR
SEQRES 8 B 145 ASP GLY SER CYS THR VAL ARG TRP GLU ASN LYS THR MET
SEQRES 9 B 145 TYR CYS ILE VAL SER THR PHE GLY LEU SER ILE GLY GLY
SEQRES 10 B 145 SER ARG ARG GLY LEU SER SER LEU SER LEU ALA LYS SER
SEQRES 11 B 145 VAL SER THR THR ASN ILE ALA GLY HIS PHE ASN ASP GLU
SEQRES 12 B 145 SER PRO
SEQRES 1 C 145 GLY SER MET GLU ASP PHE GLN ALA SER GLU GLU THR ALA
SEQRES 2 C 145 PHE VAL VAL ASP GLU VAL SER SER ILE VAL LYS GLU ALA
SEQRES 3 C 145 ILE GLU SER ALA ILE GLY GLY ASN ALA TYR GLN HIS SER
SEQRES 4 C 145 LYS VAL ASN GLN TRP THR THR ASN VAL LEU GLU GLN THR
SEQRES 5 C 145 LEU SER GLN LEU THR LYS LEU GLY ARG PRO PHE LYS TYR
SEQRES 6 C 145 ILE VAL THR CYS VAL ILE MET GLN LYS ASN GLY ALA GLY
SEQRES 7 C 145 LEU HIS SER ALA SER SER CYS PHE TRP ASP SER SER THR
SEQRES 8 C 145 ASP GLY SER CYS THR VAL ARG TRP GLU ASN LYS THR MET
SEQRES 9 C 145 TYR CYS ILE VAL SER THR PHE GLY LEU SER ILE GLY GLY
SEQRES 10 C 145 SER ARG ARG GLY LEU SER SER LEU SER LEU ALA LYS SER
SEQRES 11 C 145 VAL SER THR THR ASN ILE ALA GLY HIS PHE ASN ASP GLU
SEQRES 12 C 145 SER PRO
HET SO4 A 201 5
HET SO4 A 202 5
HET SO4 A 203 5
HET SO4 B 201 5
HETNAM SO4 SULFATE ION
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 8 HOH *178(H2 O)
HELIX 1 AA1 VAL A 13 GLY A 30 1 18
HELIX 2 AA2 GLN A 35 SER A 37 5 3
HELIX 3 AA3 LYS A 38 LYS A 56 1 19
HELIX 4 AA4 ARG A 118 LEU A 123 5 6
HELIX 5 AA5 VAL B 13 GLY B 30 1 18
HELIX 6 AA6 LYS B 38 LEU B 57 1 20
HELIX 7 AA7 ARG B 118 LEU B 123 5 6
HELIX 8 AA8 VAL C 13 GLY C 30 1 18
HELIX 9 AA9 GLN C 35 SER C 37 5 3
HELIX 10 AB1 LYS C 38 LEU C 57 1 20
HELIX 11 AB2 ARG C 118 LEU C 123 5 6
SHEET 1 AA1 5 GLY A 91 GLU A 98 0
SHEET 2 AA1 5 MET A 102 SER A 112 -1 O CYS A 104 N TRP A 97
SHEET 3 AA1 5 PHE A 61 GLN A 71 -1 N ILE A 64 O PHE A 109
SHEET 4 AA1 5 LEU B 77 TRP B 85 -1 O SER B 82 N VAL A 65
SHEET 5 AA1 5 SER B 124 ILE B 134 -1 O ILE B 134 N LEU B 77
SHEET 1 AA2 3 SER A 124 ALA A 126 0
SHEET 2 AA2 3 LEU A 77 TRP A 85 -1 N CYS A 83 O ALA A 126
SHEET 3 AA2 3 THR A 132 ILE A 134 -1 O ILE A 134 N LEU A 77
SHEET 1 AA3 5 SER A 124 ALA A 126 0
SHEET 2 AA3 5 LEU A 77 TRP A 85 -1 N CYS A 83 O ALA A 126
SHEET 3 AA3 5 PHE B 61 GLN B 71 -1 O VAL B 65 N SER A 82
SHEET 4 AA3 5 MET B 102 SER B 112 -1 O ILE B 105 N VAL B 68
SHEET 5 AA3 5 GLY B 91 GLU B 98 -1 N TRP B 97 O CYS B 104
SHEET 1 AA4 3 PHE C 61 GLN C 71 0
SHEET 2 AA4 3 MET C 102 SER C 112 -1 O ILE C 105 N VAL C 68
SHEET 3 AA4 3 GLY C 91 GLU C 98 -1 N CYS C 93 O THR C 108
SHEET 1 AA5 2 LEU C 77 SER C 79 0
SHEET 2 AA5 2 THR C 132 ILE C 134 -1 O ILE C 134 N LEU C 77
SHEET 1 AA6 2 CYS C 83 TRP C 85 0
SHEET 2 AA6 2 SER C 124 ALA C 126 -1 O SER C 124 N TRP C 85
SITE 1 AC1 6 ASN A 32 LYS A 38 TRP A 42 SER A 121
SITE 2 AC1 6 HOH A 329 HOH A 335
SITE 1 AC2 5 TYR A 34 HIS A 36 GLN A 71 HIS B 78
SITE 2 AC2 5 ALA B 135
SITE 1 AC3 6 GLY A 76 HIS A 78 ALA A 135 TYR B 34
SITE 2 AC3 6 HIS B 36 GLN B 71
SITE 1 AC4 4 ASN B 32 LYS B 38 TRP B 42 SER C 121
CRYST1 91.967 91.967 83.079 90.00 90.00 120.00 P 32 2 1 18
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 0.010873 0.006278 0.000000 0.00000
SCALE2 0.000000 0.012556 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012037 0.00000
(ATOM LINES ARE NOT SHOWN.)
END