HEADER SIGNALING PROTEIN 20-OCT-17 6BCA
TITLE A COMPLEX BETWEEN PH DOMAIN OF LBCRHOGEF (AKAP-LBC) AND ACTIVATED RHOA
TITLE 2 BOUND TO A GTP ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFORMING PROTEIN RHOA;
COMPND 3 CHAIN: F, C;
COMPND 4 SYNONYM: RHO CDNA CLONE 12,H12;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: A-KINASE ANCHOR PROTEIN 13;
COMPND 8 CHAIN: A, B;
COMPND 9 SYNONYM: AKAP-13,AKAP-LBC,BREAST CANCER NUCLEAR RECEPTOR-BINDING
COMPND 10 AUXILIARY PROTEIN,GUANINE NUCLEOTIDE EXCHANGE FACTOR LBC,HUMAN
COMPND 11 THYROID-ANCHORING PROTEIN 31,LYMPHOID BLAST CRISIS ONCOGENE,LBC
COMPND 12 ONCOGENE,NON-ONCOGENIC RHO GTPASE-SPECIFIC GTP EXCHANGE FACTOR,
COMPND 13 PROTEIN KINASE A-ANCHORING PROTEIN 13,PRKA13,P47;
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: RHOA, ARH12, ARHA, RHO12;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-KG-TEV;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: AKAP13, BRX, HT31, LBC;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX-KG-TEV
KEYWDS RHO GTPASE GUANINE NUCLEOTIDE EXCHANGE FACTORS RHOGEF PLECKSTRIN
KEYWDS 2 HOMOLOGY PH DOMAIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.STERNWEIS,Z.CHEN
REVDAT 5 13-MAR-24 6BCA 1 LINK
REVDAT 4 01-JAN-20 6BCA 1 REMARK
REVDAT 3 27-JUN-18 6BCA 1 JRNL
REVDAT 2 17-JAN-18 6BCA 1 REMARK
REVDAT 1 13-DEC-17 6BCA 0
JRNL AUTH Z.CHEN,S.GUTOWSKI,P.C.STERNWEIS
JRNL TITL CRYSTAL STRUCTURES OF THE PH DOMAINS FROM LBC FAMILY OF
JRNL TITL 2 RHOGEFS BOUND TO ACTIVATED RHOA GTPASE.
JRNL REF DATA BRIEF V. 17 356 2018
JRNL REFN ESSN 2352-3409
JRNL PMID 29876405
JRNL DOI 10.1016/J.DIB.2018.01.024
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 34.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 50522
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2500
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 34.2173 - 5.2235 0.99 2713 154 0.2118 0.2385
REMARK 3 2 5.2235 - 4.1483 0.99 2733 138 0.1593 0.1357
REMARK 3 3 4.1483 - 3.6246 0.99 2716 134 0.1782 0.1965
REMARK 3 4 3.6246 - 3.2935 0.99 2715 139 0.1904 0.2138
REMARK 3 5 3.2935 - 3.0576 0.98 2682 139 0.2117 0.2902
REMARK 3 6 3.0576 - 2.8774 0.98 2723 128 0.2058 0.2542
REMARK 3 7 2.8774 - 2.7334 0.98 2702 136 0.1971 0.2640
REMARK 3 8 2.7334 - 2.6145 0.98 2714 140 0.1902 0.2384
REMARK 3 9 2.6145 - 2.5138 0.98 2705 135 0.1813 0.2564
REMARK 3 10 2.5138 - 2.4271 0.98 2652 146 0.1931 0.2298
REMARK 3 11 2.4271 - 2.3512 0.98 2671 152 0.1864 0.2632
REMARK 3 12 2.3512 - 2.2840 0.98 2698 139 0.2013 0.2709
REMARK 3 13 2.2840 - 2.2239 0.97 2650 145 0.2026 0.2474
REMARK 3 14 2.2239 - 2.1697 0.97 2693 141 0.2094 0.2580
REMARK 3 15 2.1697 - 2.1204 0.97 2636 143 0.2250 0.2703
REMARK 3 16 2.1204 - 2.0752 0.96 2664 130 0.2291 0.2977
REMARK 3 17 2.0752 - 2.0337 0.94 2588 124 0.2406 0.2968
REMARK 3 18 2.0337 - 1.9954 0.87 2367 137 0.2626 0.3431
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.00
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 : 0.015 5260
REMARK 3 ANGLE : 1.532 7102
REMARK 3 CHIRALITY : 0.081 790
REMARK 3 PLANARITY : 0.007 895
REMARK 3 DIHEDRAL : 15.985 2038
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1972 46.5359 75.7532
REMARK 3 T TENSOR
REMARK 3 T11: 0.1191 T22: 0.1313
REMARK 3 T33: 0.1053 T12: 0.0212
REMARK 3 T13: -0.0055 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.4121 L22: 0.4804
REMARK 3 L33: 0.0478 L12: 0.3736
REMARK 3 L13: 0.0783 L23: 0.0544
REMARK 3 S TENSOR
REMARK 3 S11: 0.0224 S12: -0.0236 S13: -0.0058
REMARK 3 S21: 0.0094 S22: -0.0140 S23: -0.0155
REMARK 3 S31: 0.0087 S32: 0.0037 S33: -0.0035
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 6BCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : SILICON CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50558
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.995
REMARK 200 RESOLUTION RANGE LOW (A) : 34.212
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
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 (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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 (%): 53.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24-26% PEG 3350, 100MM BIS-TRIS, 200MM
REMARK 280 AMMONIUM SULFATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 2220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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 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: 2210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 F -3
REMARK 465 ILE F -2
REMARK 465 LEU F -1
REMARK 465 ASP F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLY A 2189
REMARK 465 ILE A 2190
REMARK 465 LEU A 2191
REMARK 465 ASP A 2192
REMARK 465 MET A 2305
REMARK 465 THR A 2306
REMARK 465 HIS A 2334
REMARK 465 HIS A 2335
REMARK 465 HIS A 2336
REMARK 465 HIS A 2337
REMARK 465 HIS A 2338
REMARK 465 HIS A 2339
REMARK 465 GLY B 2189
REMARK 465 ILE B 2190
REMARK 465 LEU B 2191
REMARK 465 ASP B 2192
REMARK 465 ALA B 2193
REMARK 465 SER B 2194
REMARK 465 MET B 2305
REMARK 465 THR B 2306
REMARK 465 HIS B 2336
REMARK 465 HIS B 2337
REMARK 465 HIS B 2338
REMARK 465 HIS B 2339
REMARK 465 GLY C -3
REMARK 465 ILE C -2
REMARK 465 LEU C -1
REMARK 465 ASP C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
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 F 201 HOG2 GSP F 202 1.26
REMARK 500 HZ2 LYS C 18 HOG3 GSP C 202 1.28
REMARK 500 HZ3 LYS F 18 HOG3 GSP F 202 1.29
REMARK 500 MG MG C 201 HOG2 GSP C 202 1.33
REMARK 500 H GLN B 2276 O HOH B 2403 1.46
REMARK 500 HZ2 LYS C 162 O HOH C 301 1.56
REMARK 500 HH22 ARG F 122 OE1 GLU F 158 1.59
REMARK 500 O HOH F 333 O HOH F 418 1.95
REMARK 500 O HOH C 311 O HOH C 421 2.01
REMARK 500 O HOH C 327 O HOH C 395 2.01
REMARK 500 O HOH A 2432 O HOH A 2440 2.02
REMARK 500 O ALA F 3 O HOH F 301 2.08
REMARK 500 O HOH B 2457 O HOH B 2483 2.09
REMARK 500 OD2 ASP B 2275 O HOH B 2401 2.09
REMARK 500 O HOH C 308 O HOH C 396 2.11
REMARK 500 O HOH C 421 O HOH C 422 2.12
REMARK 500 NZ LYS B 2241 O HOH B 2402 2.14
REMARK 500 O HOH B 2453 O HOH B 2478 2.15
REMARK 500 O HOH C 430 O HOH C 446 2.16
REMARK 500 N GLN B 2276 O HOH B 2403 2.17
REMARK 500 O HOH C 328 O HOH C 441 2.17
REMARK 500 O HOH B 2426 O HOH B 2482 2.17
REMARK 500 O HOH B 2442 O HOH B 2468 2.18
REMARK 500 OG SER C 85 OD1 ASP C 87 2.19
REMARK 500 O HOH F 359 O HOH F 410 2.19
REMARK 500 O HOH B 2414 O HOH B 2417 2.19
REMARK 500 OE1 GLU F 102 O HOH F 302 2.19
REMARK 500 O HOH B 2473 O HOH B 2485 2.19
REMARK 500 O HOH B 2472 O HOH B 2479 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS F 107 CB CYS F 107 SG -0.101
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 ARG F 122 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG F 122 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG C 70 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 70 NE - CZ - NH2 ANGL. DEV. = -3.6 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 ALA F 15 4.61 80.64
REMARK 500 VAL F 38 -62.31 -97.03
REMARK 500 LYS F 98 -53.56 -135.23
REMARK 500 LYS F 164 -9.11 83.98
REMARK 500 GLN A2267 15.86 58.06
REMARK 500 LEU A2274 86.58 -151.61
REMARK 500 GLU A2295 -36.41 -39.20
REMARK 500 ASP B2275 73.24 29.84
REMARK 500 GLN B2276 5.04 56.51
REMARK 500 ALA C 15 1.60 83.07
REMARK 500 VAL C 38 -65.33 -98.40
REMARK 500 LYS C 98 -50.83 -124.47
REMARK 500 CYS C 107 44.35 -145.99
REMARK 500 LYS C 164 -14.31 81.72
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 F 456 DISTANCE = 6.83 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 F 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 19 OG1
REMARK 620 2 THR F 37 OG1 81.1
REMARK 620 3 GSP F 202 O2G 168.7 87.7
REMARK 620 4 GSP F 202 O1B 89.4 168.7 101.9
REMARK 620 5 HOH F 349 O 86.7 81.2 92.8 92.3
REMARK 620 6 HOH F 364 O 85.2 91.0 93.9 94.3 169.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 19 OG1
REMARK 620 2 THR C 37 OG1 80.0
REMARK 620 3 GSP C 202 O2G 167.5 87.8
REMARK 620 4 GSP C 202 O2B 88.9 167.1 103.6
REMARK 620 5 HOH C 332 O 86.2 84.1 95.4 88.8
REMARK 620 6 HOH C 340 O 82.6 89.3 94.6 95.7 167.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSP F 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSP C 202
DBREF 6BCA F 1 181 UNP P61586 RHOA_HUMAN 1 181
DBREF 6BCA A 2193 2333 UNP Q12802 AKP13_HUMAN 2173 2313
DBREF 6BCA B 2193 2333 UNP Q12802 AKP13_HUMAN 2173 2313
DBREF 6BCA C 1 181 UNP P61586 RHOA_HUMAN 1 181
SEQADV 6BCA GLY F -3 UNP P61586 EXPRESSION TAG
SEQADV 6BCA ILE F -2 UNP P61586 EXPRESSION TAG
SEQADV 6BCA LEU F -1 UNP P61586 EXPRESSION TAG
SEQADV 6BCA ASP F 0 UNP P61586 EXPRESSION TAG
SEQADV 6BCA GLY A 2189 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA ILE A 2190 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA LEU A 2191 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA ASP A 2192 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS A 2334 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS A 2335 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS A 2336 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS A 2337 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS A 2338 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS A 2339 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA GLY B 2189 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA ILE B 2190 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA LEU B 2191 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA ASP B 2192 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS B 2334 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS B 2335 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS B 2336 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS B 2337 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS B 2338 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA HIS B 2339 UNP Q12802 EXPRESSION TAG
SEQADV 6BCA GLY C -3 UNP P61586 EXPRESSION TAG
SEQADV 6BCA ILE C -2 UNP P61586 EXPRESSION TAG
SEQADV 6BCA LEU C -1 UNP P61586 EXPRESSION TAG
SEQADV 6BCA ASP C 0 UNP P61586 EXPRESSION TAG
SEQRES 1 F 185 GLY ILE LEU ASP MET ALA ALA ILE ARG LYS LYS LEU VAL
SEQRES 2 F 185 ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU
SEQRES 3 F 185 ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL
SEQRES 4 F 185 PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL
SEQRES 5 F 185 ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA
SEQRES 6 F 185 GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR
SEQRES 7 F 185 PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP
SEQRES 8 F 185 SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR
SEQRES 9 F 185 PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE
SEQRES 10 F 185 LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS
SEQRES 11 F 185 THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL
SEQRES 12 F 185 LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY
SEQRES 13 F 185 ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP
SEQRES 14 F 185 GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA
SEQRES 15 F 185 LEU GLN ALA
SEQRES 1 A 151 GLY ILE LEU ASP ALA SER TYR GLU LYS LYS VAL ARG LEU
SEQRES 2 A 151 ASN GLU ILE TYR THR LYS THR ASP SER LYS SER ILE MET
SEQRES 3 A 151 ARG MET LYS SER GLY GLN MET PHE ALA LYS GLU ASP LEU
SEQRES 4 A 151 LYS ARG LYS LYS LEU VAL ARG ASP GLY SER VAL PHE LEU
SEQRES 5 A 151 LYS ASN ALA ALA GLY ARG LEU LYS GLU VAL GLN ALA VAL
SEQRES 6 A 151 LEU LEU THR ASP ILE LEU VAL PHE LEU GLN GLU LYS ASP
SEQRES 7 A 151 GLN LYS TYR ILE PHE ALA SER LEU ASP GLN LYS SER THR
SEQRES 8 A 151 VAL ILE SER LEU LYS LYS LEU ILE VAL ARG GLU VAL ALA
SEQRES 9 A 151 HIS GLU GLU LYS GLY LEU PHE LEU ILE SER MET GLY MET
SEQRES 10 A 151 THR ASP PRO GLU MET VAL GLU VAL HIS ALA SER SER LYS
SEQRES 11 A 151 GLU GLU ARG ASN SER TRP ILE GLN ILE ILE GLN ASP THR
SEQRES 12 A 151 ILE ASN HIS HIS HIS HIS HIS HIS
SEQRES 1 B 151 GLY ILE LEU ASP ALA SER TYR GLU LYS LYS VAL ARG LEU
SEQRES 2 B 151 ASN GLU ILE TYR THR LYS THR ASP SER LYS SER ILE MET
SEQRES 3 B 151 ARG MET LYS SER GLY GLN MET PHE ALA LYS GLU ASP LEU
SEQRES 4 B 151 LYS ARG LYS LYS LEU VAL ARG ASP GLY SER VAL PHE LEU
SEQRES 5 B 151 LYS ASN ALA ALA GLY ARG LEU LYS GLU VAL GLN ALA VAL
SEQRES 6 B 151 LEU LEU THR ASP ILE LEU VAL PHE LEU GLN GLU LYS ASP
SEQRES 7 B 151 GLN LYS TYR ILE PHE ALA SER LEU ASP GLN LYS SER THR
SEQRES 8 B 151 VAL ILE SER LEU LYS LYS LEU ILE VAL ARG GLU VAL ALA
SEQRES 9 B 151 HIS GLU GLU LYS GLY LEU PHE LEU ILE SER MET GLY MET
SEQRES 10 B 151 THR ASP PRO GLU MET VAL GLU VAL HIS ALA SER SER LYS
SEQRES 11 B 151 GLU GLU ARG ASN SER TRP ILE GLN ILE ILE GLN ASP THR
SEQRES 12 B 151 ILE ASN HIS HIS HIS HIS HIS HIS
SEQRES 1 C 185 GLY ILE LEU ASP MET ALA ALA ILE ARG LYS LYS LEU VAL
SEQRES 2 C 185 ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU
SEQRES 3 C 185 ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL
SEQRES 4 C 185 PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL
SEQRES 5 C 185 ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA
SEQRES 6 C 185 GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR
SEQRES 7 C 185 PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP
SEQRES 8 C 185 SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR
SEQRES 9 C 185 PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE
SEQRES 10 C 185 LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS
SEQRES 11 C 185 THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL
SEQRES 12 C 185 LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY
SEQRES 13 C 185 ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP
SEQRES 14 C 185 GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA
SEQRES 15 C 185 LEU GLN ALA
HET MG F 201 1
HET GSP F 202 45
HET MG C 201 1
HET GSP C 202 45
HETNAM MG MAGNESIUM ION
HETNAM GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
FORMUL 5 MG 2(MG 2+)
FORMUL 6 GSP 2(C10 H16 N5 O13 P3 S)
FORMUL 9 HOH *487(H2 O)
HELIX 1 AA1 GLY F 17 ASP F 28 1 12
HELIX 2 AA2 GLN F 63 ASP F 67 5 5
HELIX 3 AA3 LEU F 69 TYR F 74 5 6
HELIX 4 AA4 SER F 88 LYS F 98 1 11
HELIX 5 AA5 LYS F 98 CYS F 107 1 10
HELIX 6 AA6 LYS F 118 ARG F 122 5 5
HELIX 7 AA7 ASP F 124 LYS F 133 1 10
HELIX 8 AA8 LYS F 140 GLY F 152 1 13
HELIX 9 AA9 GLY F 166 GLN F 180 1 15
HELIX 10 AB1 SER A 2194 THR A 2208 1 15
HELIX 11 AB2 GLU A 2225 LYS A 2228 5 4
HELIX 12 AB3 SER A 2317 ASN A 2333 1 17
HELIX 13 AB4 GLU B 2196 THR B 2208 1 13
HELIX 14 AB5 GLU B 2225 LYS B 2228 5 4
HELIX 15 AB6 SER B 2317 ASN B 2333 1 17
HELIX 16 AB7 GLY C 17 ASP C 28 1 12
HELIX 17 AB8 GLN C 63 ASP C 67 5 5
HELIX 18 AB9 LEU C 69 TYR C 74 5 6
HELIX 19 AC1 SER C 88 LYS C 98 1 11
HELIX 20 AC2 LYS C 98 CYS C 107 1 10
HELIX 21 AC3 LYS C 118 ARG C 122 5 5
HELIX 22 AC4 ASP C 124 MET C 134 1 11
HELIX 23 AC5 LYS C 140 GLY C 152 1 13
HELIX 24 AC6 GLY C 166 GLN C 180 1 15
SHEET 1 AA1 6 PHE F 39 VAL F 48 0
SHEET 2 AA1 6 LYS F 51 THR F 60 -1 O LEU F 57 N TYR F 42
SHEET 3 AA1 6 ILE F 4 GLY F 12 1 N ILE F 4 O GLU F 54
SHEET 4 AA1 6 VAL F 79 SER F 85 1 O CYS F 83 N VAL F 11
SHEET 5 AA1 6 ILE F 112 ASN F 117 1 O ASN F 117 N PHE F 84
SHEET 6 AA1 6 GLY F 155 GLU F 158 1 O MET F 157 N LEU F 114
SHEET 1 AA2 2 ILE A2213 ARG A2215 0
SHEET 2 AA2 2 MET A2221 ALA A2223 -1 O PHE A2222 N MET A2214
SHEET 1 AA3 3 LYS A2268 PHE A2271 0
SHEET 2 AA3 3 ILE A2258 LYS A2265 -1 N LYS A2265 O LYS A2268
SHEET 3 AA3 3 VAL A2280 SER A2282 -1 O ILE A2281 N LEU A2259
SHEET 1 AA4 7 LYS A2268 PHE A2271 0
SHEET 2 AA4 7 ILE A2258 LYS A2265 -1 N LYS A2265 O LYS A2268
SHEET 3 AA4 7 LEU A2247 LEU A2255 -1 N VAL A2253 O VAL A2260
SHEET 4 AA4 7 LEU A2232 LYS A2241 -1 N GLY A2236 O ALA A2252
SHEET 5 AA4 7 GLU A2309 HIS A2314 -1 O GLU A2312 N LYS A2241
SHEET 6 AA4 7 GLY A2297 SER A2302 -1 N LEU A2298 O VAL A2313
SHEET 7 AA4 7 LEU A2286 GLU A2290 -1 N ARG A2289 O PHE A2299
SHEET 1 AA5 2 ILE B2213 ARG B2215 0
SHEET 2 AA5 2 MET B2221 ALA B2223 -1 O PHE B2222 N MET B2214
SHEET 1 AA6 3 LYS B2268 PHE B2271 0
SHEET 2 AA6 3 ILE B2258 LYS B2265 -1 N LYS B2265 O LYS B2268
SHEET 3 AA6 3 VAL B2280 SER B2282 -1 O ILE B2281 N LEU B2259
SHEET 1 AA7 7 LYS B2268 PHE B2271 0
SHEET 2 AA7 7 ILE B2258 LYS B2265 -1 N LYS B2265 O LYS B2268
SHEET 3 AA7 7 LEU B2247 LEU B2255 -1 N VAL B2253 O VAL B2260
SHEET 4 AA7 7 LEU B2232 LYS B2241 -1 N VAL B2238 O VAL B2250
SHEET 5 AA7 7 GLU B2309 HIS B2314 -1 O GLU B2312 N LYS B2241
SHEET 6 AA7 7 GLY B2297 SER B2302 -1 N LEU B2298 O VAL B2313
SHEET 7 AA7 7 LEU B2286 GLU B2290 -1 N ILE B2287 O ILE B2301
SHEET 1 AA8 6 PHE C 39 VAL C 48 0
SHEET 2 AA8 6 LYS C 51 THR C 60 -1 O LEU C 57 N TYR C 42
SHEET 3 AA8 6 ILE C 4 GLY C 12 1 N ILE C 4 O GLU C 54
SHEET 4 AA8 6 VAL C 79 SER C 85 1 O CYS C 83 N VAL C 11
SHEET 5 AA8 6 ILE C 112 ASN C 117 1 O ILE C 113 N ILE C 80
SHEET 6 AA8 6 GLY C 155 GLU C 158 1 O MET C 157 N GLY C 116
LINK OG1 THR F 19 MG MG F 201 1555 1555 2.15
LINK OG1 THR F 37 MG MG F 201 1555 1555 2.11
LINK MG MG F 201 O2G GSP F 202 1555 1555 1.99
LINK MG MG F 201 O1B GSP F 202 1555 1555 2.06
LINK MG MG F 201 O HOH F 349 1555 1555 2.09
LINK MG MG F 201 O HOH F 364 1555 1555 2.23
LINK OG1 THR C 19 MG MG C 201 1555 1555 2.17
LINK OG1 THR C 37 MG MG C 201 1555 1555 2.21
LINK MG MG C 201 O2G GSP C 202 1555 1555 2.03
LINK MG MG C 201 O2B GSP C 202 1555 1555 1.97
LINK MG MG C 201 O HOH C 332 1555 1555 2.09
LINK MG MG C 201 O HOH C 340 1555 1555 2.21
SITE 1 AC1 5 THR F 19 THR F 37 GSP F 202 HOH F 349
SITE 2 AC1 5 HOH F 364
SITE 1 AC2 27 PHE C 154 ALA F 15 CYS F 16 GLY F 17
SITE 2 AC2 27 LYS F 18 THR F 19 CYS F 20 PHE F 30
SITE 3 AC2 27 TYR F 34 PRO F 36 THR F 37 GLY F 62
SITE 4 AC2 27 LYS F 118 ASP F 120 SER F 160 ALA F 161
SITE 5 AC2 27 LYS F 162 MG F 201 HOH F 308 HOH F 335
SITE 6 AC2 27 HOH F 345 HOH F 349 HOH F 355 HOH F 362
SITE 7 AC2 27 HOH F 364 HOH F 378 HOH F 416
SITE 1 AC3 5 THR C 19 THR C 37 GSP C 202 HOH C 332
SITE 2 AC3 5 HOH C 340
SITE 1 AC4 29 ALA C 15 CYS C 16 GLY C 17 LYS C 18
SITE 2 AC4 29 THR C 19 CYS C 20 PHE C 30 TYR C 34
SITE 3 AC4 29 PRO C 36 THR C 37 GLY C 62 LYS C 118
SITE 4 AC4 29 ASP C 120 LEU C 121 SER C 160 ALA C 161
SITE 5 AC4 29 LYS C 162 MG C 201 HOH C 322 HOH C 326
SITE 6 AC4 29 HOH C 332 HOH C 340 HOH C 349 HOH C 364
SITE 7 AC4 29 HOH C 373 HOH C 392 HOH C 408 PHE F 154
SITE 8 AC4 29 HOH F 447
CRYST1 51.346 60.525 63.618 91.83 92.97 90.01 P 1 2
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 0.019476 0.000004 0.001010 0.00000
SCALE2 0.000000 0.016522 0.000527 0.00000
SCALE3 0.000000 0.000000 0.015748 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
