HEADER CELL CYCLE 29-APR-14 4D0N
TITLE AKAP13 (AKAP-LBC) RHOGEF DOMAIN IN COMPLEX WITH RHOA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFORMING PROTEIN RHOA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-184;
COMPND 5 SYNONYM: RHOA, RHO CDNA CLONE 12, H12;
COMPND 6 EC: 3.6.5.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: A-KINASE ANCHOR PROTEIN 13;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RHOGEF DOMAIN, RESIDUES 1968-2338;
COMPND 12 SYNONYM: AKAP13, AKAP-13, AKAP-LBC, BREAST CANCER NUCLEAR
COMPND 13 RECEPTOR-BINDING AUXILIARY PROTEIN, GUANINE NUCLEOTIDE EXCHANGE
COMPND 14 FACTOR LBC, HUMAN THYROID-ANCHORING PROTEIN 31, LYMPHOID BLAST
COMPND 15 CRISIS ONCOGENE, LBC ONCOGENE, NON-ONCOGENIC RHO GTPASE-SPECIFIC
COMPND 16 GTP EXCHANGE FACTOR, PROTEIN KINASE A-ANCHORING PROTEIN 13,
COMPND 17 PRKA13, P47;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS CELL CYCLE, AKAP13, LBC, AKAP-LBC, GEF, RHOGEF, DH DOMAIN, PH DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.ABDUL AZEEZ,L.SHRESTHA,T.KROJER,C.ALLERSTON,F.VON DELFT,
AUTHOR 2 C.BOUNTRA,C.ARROWSMITH,A.M.EDWARDS,S.KNAPP,E.KLUSSMANN,J.M.ELKINS
REVDAT 3 26-NOV-14 4D0N 1 JRNL
REVDAT 2 17-SEP-14 4D0N 1 JRNL
REVDAT 1 21-MAY-14 4D0N 0
JRNL AUTH K.R.ABDUL AZEEZ,S.KNAPP,J.M.P.FERNANDES,E.KLUSSMANN,
JRNL AUTH 2 J.M.ELKINS
JRNL TITL THE CRYSTAL STRUCTURE OF THE RHOA : AKAP-LBC DH-PH DOMAIN
JRNL TITL 2 COMPLEX.
JRNL REF BIOCHEM.J. V. 464 231 2014
JRNL REFN ISSN 0264-6021
JRNL PMID 25186459
JRNL DOI 10.1042/BJ20140606
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.07
REMARK 3 NUMBER OF REFLECTIONS : 46509
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.21098
REMARK 3 R VALUE (WORKING SET) : 0.20943
REMARK 3 FREE R VALUE : 0.23946
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2476
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.100
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.155
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3237
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.368
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.392
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4373
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.162
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.39
REMARK 3 B22 (A**2) : 0.16
REMARK 3 B33 (A**2) : 1.22
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.182
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.162
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.293
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4496 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4353 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6063 ; 1.070 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10020 ; 0.739 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 552 ; 5.327 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 201 ;35.880 ;24.677
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 857 ;14.478 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;17.898 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 694 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4970 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 976 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2202 ; 1.045 ; 3.146
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2201 ; 1.044 ; 3.146
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2750 ; 1.756 ; 4.711
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2294 ; 1.161 ; 3.321
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4D0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-14.
REMARK 100 THE PDBE ID CODE IS EBI-60341.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-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 : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49042
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 82.32
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.9
REMARK 200 R MERGE FOR SHELL (I) : 0.45
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.60
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULPHATE, 0.1 M
REMARK 280 BIS-TRIS PH 5.5, 25% (W/V) PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 41.16000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.41000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.41000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.16000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.30500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.2 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 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ARG A 182
REMARK 465 ARG A 183
REMARK 465 GLY A 184
REMARK 465 ARG B 2341
REMARK 465 ASP B 2342
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 27 CE NZ
REMARK 470 ASP A 28 CG OD1 OD2
REMARK 470 GLN A 29 CG CD OE1 NE2
REMARK 470 GLU A 32 CG CD OE1 OE2
REMARK 470 LYS A 51 CE NZ
REMARK 470 LYS A 135 NZ
REMARK 470 LYS B1973 CG CD CE NZ
REMARK 470 LYS B1987 CE NZ
REMARK 470 LYS B1990 CG CD CE NZ
REMARK 470 LYS B1993 CG CD CE NZ
REMARK 470 LYS B1994 CE NZ
REMARK 470 GLN B2026 CD OE1 NE2
REMARK 470 LYS B2064 NZ
REMARK 470 LYS B2065 CE NZ
REMARK 470 LYS B2071 CG CD CE NZ
REMARK 470 LYS B2074 NZ
REMARK 470 LYS B2079 CE NZ
REMARK 470 LYS B2131 CE NZ
REMARK 470 SER B2136 OG
REMARK 470 LYS B2169 CE NZ
REMARK 470 GLN B2224 CG CD OE1 NE2
REMARK 470 LYS B2232 CD CE NZ
REMARK 470 ARG B2233 NE CZ NH1 NH2
REMARK 470 LYS B2269 CD CE NZ
REMARK 470 LYS B2272 CE NZ
REMARK 470 GLN B2280 CG CD OE1 NE2
REMARK 470 LYS B2288 CE NZ
REMARK 470 SER B2320 OG
REMARK 470 GLN B2330 CD OE1 NE2
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 O HOH A 2034 O HOH B 3556 2.11
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 PRO A 31 92.27 -69.60
REMARK 500 GLU A 40 -78.29 -86.50
REMARK 500 VAL B2023 -62.57 -100.85
REMARK 500 ASP B2070 -143.44 69.18
REMARK 500 SER B2135 -44.56 -139.00
REMARK 500 ARG B2140 -18.46 -45.47
REMARK 500 ARG B2233 70.12 -104.22
REMARK 500 LEU B2278 89.95 -155.00
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 GDP A1182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B3341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B3342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B3343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B3344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1184
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4D0O RELATED DB: PDB
REMARK 900 AKAP13 (AKAP-LBC) DH DOMAIN
DBREF 4D0N A 1 184 UNP P61586 RHOA_HUMAN 1 184
DBREF 4D0N B 1972 2342 UNP Q12802 AKP13_HUMAN 1968 2338
SEQADV 4D0N SER A 0 UNP P61586 EXPRESSION TAG
SEQADV 4D0N SER B 1970 UNP Q12802 EXPRESSION TAG
SEQADV 4D0N MET B 1971 UNP Q12802 EXPRESSION TAG
SEQRES 1 A 185 SER MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY
SEQRES 2 A 185 ASP GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL PHE
SEQRES 3 A 185 SER LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL
SEQRES 4 A 185 PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS
SEQRES 5 A 185 GLN VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU
SEQRES 6 A 185 ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR
SEQRES 7 A 185 ASP VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP
SEQRES 8 A 185 SER LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL
SEQRES 9 A 185 LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY
SEQRES 10 A 185 ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG
SEQRES 11 A 185 GLU LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU
SEQRES 12 A 185 GLU GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY
SEQRES 13 A 185 TYR MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG
SEQRES 14 A 185 GLU VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA
SEQRES 15 A 185 ARG ARG GLY
SEQRES 1 B 373 SER MET SER LYS GLN LEU GLU ALA GLU SER TRP SER ARG
SEQRES 2 B 373 ILE ILE ASP SER LYS PHE LEU LYS GLN GLN LYS LYS ASP
SEQRES 3 B 373 VAL VAL LYS ARG GLN GLU VAL ILE TYR GLU LEU MET GLN
SEQRES 4 B 373 THR GLU PHE HIS HIS VAL ARG THR LEU LYS ILE MET SER
SEQRES 5 B 373 GLY VAL TYR SER GLN GLY MET MET ALA ASP LEU LEU PHE
SEQRES 6 B 373 GLU GLN GLN MET VAL GLU LYS LEU PHE PRO CYS LEU ASP
SEQRES 7 B 373 GLU LEU ILE SER ILE HIS SER GLN PHE PHE GLN ARG ILE
SEQRES 8 B 373 LEU GLU ARG LYS LYS GLU SER LEU VAL ASP LYS SER GLU
SEQRES 9 B 373 LYS ASN PHE LEU ILE LYS ARG ILE GLY ASP VAL LEU VAL
SEQRES 10 B 373 ASN GLN PHE SER GLY GLU ASN ALA GLU ARG LEU LYS LYS
SEQRES 11 B 373 THR TYR GLY LYS PHE CYS GLY GLN HIS ASN GLN SER VAL
SEQRES 12 B 373 ASN TYR PHE LYS ASP LEU TYR ALA LYS ASP LYS ARG PHE
SEQRES 13 B 373 GLN ALA PHE VAL LYS LYS LYS MET SER SER SER VAL VAL
SEQRES 14 B 373 ARG ARG LEU GLY ILE PRO GLU CYS ILE LEU LEU VAL THR
SEQRES 15 B 373 GLN ARG ILE THR LYS TYR PRO VAL LEU PHE GLN ARG ILE
SEQRES 16 B 373 LEU GLN CYS THR LYS ASP ASN GLU VAL GLU GLN GLU ASP
SEQRES 17 B 373 LEU ALA GLN SER LEU SER LEU VAL LYS ASP VAL ILE GLY
SEQRES 18 B 373 ALA VAL ASP SER LYS VAL ALA SER TYR GLU LYS LYS VAL
SEQRES 19 B 373 ARG LEU ASN GLU ILE TYR THR LYS THR ASP SER LYS SER
SEQRES 20 B 373 ILE MET ARG MET LYS SER GLY GLN MET PHE ALA LYS GLU
SEQRES 21 B 373 ASP LEU LYS ARG LYS LYS LEU VAL ARG ASP GLY SER VAL
SEQRES 22 B 373 PHE LEU LYS ASN ALA ALA GLY ARG LEU LYS GLU VAL GLN
SEQRES 23 B 373 ALA VAL LEU LEU THR ASP ILE LEU VAL PHE LEU GLN GLU
SEQRES 24 B 373 LYS ASP GLN LYS TYR ILE PHE ALA SER LEU ASP GLN LYS
SEQRES 25 B 373 SER THR VAL ILE SER LEU LYS LYS LEU ILE VAL ARG GLU
SEQRES 26 B 373 VAL ALA HIS GLU GLU LYS GLY LEU PHE LEU ILE SER MET
SEQRES 27 B 373 GLY MET THR ASP PRO GLU MET VAL GLU VAL HIS ALA SER
SEQRES 28 B 373 SER LYS GLU GLU ARG ASN SER TRP ILE GLN ILE ILE GLN
SEQRES 29 B 373 ASP THR ILE ASN THR LEU ASN ARG ASP
HET GDP A1182 28
HET SO4 B3341 5
HET SO4 B3342 5
HET SO4 B3343 5
HET SO4 A1183 5
HET SO4 B3344 5
HET EDO A1184 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO C2 H6 O2
FORMUL 4 GDP C10 H15 N5 O11 P2
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 6 HOH *183(H2 O)
HELIX 1 1 GLY A 17 LYS A 27 1 11
HELIX 2 2 LEU A 69 TYR A 74 5 6
HELIX 3 3 SER A 88 CYS A 107 1 20
HELIX 4 4 LYS A 118 ARG A 122 5 5
HELIX 5 5 ASP A 124 LYS A 133 1 10
HELIX 6 6 LYS A 140 GLY A 152 1 13
HELIX 7 7 GLY A 166 GLN A 180 1 15
HELIX 8 8 SER B 1970 LEU B 1975 1 6
HELIX 9 9 SER B 1979 ILE B 1984 1 6
HELIX 10 10 ASP B 1985 GLN B 1991 1 7
HELIX 11 11 LYS B 1993 VAL B 2023 1 31
HELIX 12 12 VAL B 2023 LEU B 2032 1 10
HELIX 13 13 GLU B 2035 PHE B 2043 1 9
HELIX 14 14 CYS B 2045 GLU B 2066 1 22
HELIX 15 15 ILE B 2081 PHE B 2089 1 9
HELIX 16 16 SER B 2090 SER B 2136 1 47
HELIX 17 17 VAL B 2138 LEU B 2141 5 4
HELIX 18 18 GLY B 2142 ILE B 2154 1 13
HELIX 19 19 LYS B 2156 THR B 2168 1 13
HELIX 20 20 ASN B 2171 THR B 2212 1 42
HELIX 21 21 GLU B 2229 LEU B 2231 5 3
HELIX 22 22 SER B 2321 ASN B 2340 1 20
SHEET 1 AA 6 TYR A 42 VAL A 48 0
SHEET 2 AA 6 LYS A 51 ASP A 59 -1 O LYS A 51 N VAL A 48
SHEET 3 AA 6 ARG A 5 GLY A 12 1 O LYS A 6 N ALA A 56
SHEET 4 AA 6 VAL A 79 SER A 85 1 O VAL A 79 N VAL A 9
SHEET 5 AA 6 ILE A 112 ASN A 117 1 O ILE A 113 N MET A 82
SHEET 6 AA 6 GLY A 155 GLU A 158 1 O GLY A 155 N LEU A 114
SHEET 1 BA 2 ILE B2217 ARG B2219 0
SHEET 2 BA 2 MET B2225 ALA B2227 -1 O PHE B2226 N MET B2218
SHEET 1 BB 2 LYS B2272 PHE B2275 0
SHEET 2 BB 2 ILE B2262 LYS B2269 1 O GLN B2267 N ILE B2274
SHEET 1 BC 2 VAL B2284 SER B2286 0
SHEET 2 BC 2 ILE B2262 LYS B2269 -1 O LEU B2263 N ILE B2285
SHEET 1 BD 7 LEU B2290 GLU B2294 0
SHEET 2 BD 7 GLY B2301 SER B2306 -1 O PHE B2303 N ARG B2293
SHEET 3 BD 7 MET B2314 HIS B2318 -1 O VAL B2315 N LEU B2304
SHEET 4 BD 7 LEU B2236 LYS B2245 -1 O PHE B2243 N HIS B2318
SHEET 5 BD 7 LEU B2251 LEU B2259 -1 O LYS B2252 N LEU B2244
SHEET 6 BD 7 ILE B2262 LYS B2269 -1 O ILE B2262 N LEU B2259
SHEET 7 BD 7 LYS B2272 PHE B2275 1 O LYS B2272 N LYS B2269
SHEET 1 BE 7 LEU B2290 GLU B2294 0
SHEET 2 BE 7 GLY B2301 SER B2306 -1 O PHE B2303 N ARG B2293
SHEET 3 BE 7 MET B2314 HIS B2318 -1 O VAL B2315 N LEU B2304
SHEET 4 BE 7 LEU B2236 LYS B2245 -1 O PHE B2243 N HIS B2318
SHEET 5 BE 7 LEU B2251 LEU B2259 -1 O LYS B2252 N LEU B2244
SHEET 6 BE 7 ILE B2262 LYS B2269 -1 O ILE B2262 N LEU B2259
SHEET 7 BE 7 VAL B2284 SER B2286 -1 O ILE B2285 N LEU B2263
CISPEP 1 ALA A 3 ILE A 4 0 0.25
CISPEP 2 LYS B 2232 ARG B 2233 0 1.29
SITE 1 AC1 17 ALA A 15 CYS A 16 GLY A 17 LYS A 18
SITE 2 AC1 17 THR A 19 CYS A 20 ALA A 61 LYS A 118
SITE 3 AC1 17 ASP A 120 LEU A 121 SER A 160 ALA A 161
SITE 4 AC1 17 LYS A 162 HOH A2007 HOH A2030 HOH A2074
SITE 5 AC1 17 SO4 B3342
SITE 1 AC2 4 GLN B2055 ARG B2059 ASN B2087 ASN B2093
SITE 1 AC3 4 GDP A1182 LYS B1998 ARG B2163 GLN B2166
SITE 1 AC4 2 LYS B1993 LYS B1994
SITE 1 AC5 2 ARG A 68 SER B2194
SITE 1 AC6 3 VAL B2138 ARG B2139 ARG B2140
SITE 1 AC7 7 LYS A 7 LEU A 72 PRO A 75 HOH A2038
SITE 2 AC7 7 HOH A2076 HOH A3577 HIS B2108
CRYST1 82.320 86.610 116.820 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012148 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
