HEADER PHOSPHORYLATION 05-MAR-97 1LXD
TITLE CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS,
TITLE 2 A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RALGDSB;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN WHICH BINDS TO ACTIVE RAS;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: RALGDS C-TERMINAL DOMAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5-ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX98 FROM PGEX2T;
SOURCE 10 EXPRESSION_SYSTEM_GENE: C-TERMINAL DOMAIN OF RALGDS FUSED
SOURCE 11 TO GLUTATHIONINE S TRANSFERASE
KEYWDS PHOSPHORYLATION, RALGDS, RAS BINDING, UBIQUITIN FOLD, CDC25
KEYWDS 2 FAMILY, SIGNAL TRANSDUCTION, CROSS-TALK
EXPDTA X-RAY DIFFRACTION
AUTHOR L.HUANG,X.W.WENG,F.HOFER,G.S.MARTIN,S.H.KIM
REVDAT 2 24-FEB-09 1LXD 1 VERSN
REVDAT 1 11-MAR-98 1LXD 0
JRNL AUTH L.HUANG,X.WENG,F.HOFER,G.S.MARTIN,S.H.KIM
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE RAS-INTERACTING
JRNL TITL 2 DOMAIN OF RALGDS.
JRNL REF NAT.STRUCT.BIOL. V. 4 609 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9253406
JRNL DOI 10.1038/NSB0897-609
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.HUANG,J.JANCARIK,S.-H.KIM,F.HOFER,G.S.MARTIN
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC
REMARK 1 TITL 2 ANALYSIS OF THE RAS BINDING DOMAIN OF RALGDS, A
REMARK 1 TITL 3 GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF THE
REMARK 1 TITL 4 RAL PROTEIN
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 1033 1996
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.HOFER,S.FIELDS,C.SCHNEIDER,G.S.MARTIN
REMARK 1 TITL ACTIVATED RAS INTERACTS WITH THE RAL GUANINE
REMARK 1 TITL 2 NUCLEOTIDE DISSOCIATION STIMULATOR
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 11089 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 15000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.0
REMARK 3 NUMBER OF REFLECTIONS : 6209
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 SET) : 0.212
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.040
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.48
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 408
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.045
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1395
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 58
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NO RESTRAINTS.
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : P19.PRO
REMARK 3 PARAMETER FILE 2 : P11.WAT
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : X19.PRO
REMARK 3 TOPOLOGY FILE 2 : H11.WAT
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: H19A.PEP IS THE PEPTIDE BOND FIL
REMARK 4
REMARK 4 1LXD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.008
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6485
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.920
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MADSYS, X-PLOR 3.85
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THIS STRUCTURE WAS SOLVED USING THE MAD DATA ON THE
REMARK 200 SELENOMETHIONINE MUTANT OF THE PROTEIN AT X4A NSLS. BUT THE
REMARK 200 STRUCTURE WAS REFINED AGAINST THE NATIVE DATA ABOVE.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 20%
REMARK 280 PEG 8000, 0.1 M TRIS PH 8.5, AND 0.2 M CALCIUM ACETATE.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 52.64100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 15.35700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 52.64100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 15.35700
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: 730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 LEU A 6
REMARK 465 PRO A 7
REMARK 465 LEU A 8
REMARK 465 TYR A 9
REMARK 465 ASN A 10
REMARK 465 GLN A 11
REMARK 465 GLN A 12
REMARK 465 VAL A 13
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 LEU B 6
REMARK 465 PRO B 7
REMARK 465 LEU B 8
REMARK 465 TYR B 9
REMARK 465 ASN B 10
REMARK 465 GLN B 11
REMARK 465 GLN B 12
REMARK 465 VAL B 13
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 HIS A 53 NE2 HIS A 53 CD2 -0.076
REMARK 500 GLU A 59 CD GLU A 59 OE2 -0.067
REMARK 500 HIS A 73 NE2 HIS A 73 CD2 -0.070
REMARK 500 HIS B 53 NE2 HIS B 53 CD2 -0.084
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 CYS A 16 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASN A 29 N - CA - C ANGL. DEV. = 20.2 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 58 N - CA - C ANGL. DEV. = 20.0 DEGREES
REMARK 500 ASP A 58 CA - C - N ANGL. DEV. = -15.8 DEGREES
REMARK 500 ARG A 100 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 CYS B 16 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP B 26 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASN B 27 N - CA - C ANGL. DEV. = 18.9 DEGREES
REMARK 500 ASN B 29 OD1 - CG - ND2 ANGL. DEV. = -16.5 DEGREES
REMARK 500 ASN B 29 CB - CG - ND2 ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG B 47 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU B 65 CA - C - N ANGL. DEV. = 22.8 DEGREES
REMARK 500 LEU B 65 O - C - N ANGL. DEV. = -19.2 DEGREES
REMARK 500 ARG B 100 NE - CZ - NH1 ANGL. DEV. = 3.5 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 ASP A 26 -31.29 -37.26
REMARK 500 ASN A 29 -110.04 42.77
REMARK 500 ASP A 58 150.71 55.31
REMARK 500 GLU A 59 138.17 -8.52
REMARK 500 ASN A 82 108.90 -58.87
REMARK 500 TYR A 93 38.98 -64.98
REMARK 500 VAL B 25 -100.05 -99.09
REMARK 500 ASN B 27 28.74 -30.11
REMARK 500 SER B 38 -35.64 -29.94
REMARK 500 LEU B 66 67.36 98.50
REMARK 500 ASP B 72 -4.77 66.25
REMARK 500 ASN B 92 123.67 -39.54
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 ASN A 29 MET A 30 -148.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 93 0.10 SIDE_CHAIN
REMARK 500 TYR B 31 0.07 SIDE_CHAIN
REMARK 500 TYR B 63 0.09 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 TERMINAL RESIDUE LYS 100 IN THE PDB FILE IS LYS 864
REMARK 999 IN THE RAT RALGDS SEQUENCE.
DBREF 1LXD A 1 100 UNP Q03386 GNDS_RAT 694 864
DBREF 1LXD B 1 100 UNP Q03386 GNDS_RAT 694 864
SEQADV 1LXD A UNP Q03386 SER 696 DELETION
SEQADV 1LXD A UNP Q03386 THR 697 DELETION
SEQADV 1LXD A UNP Q03386 SER 698 DELETION
SEQADV 1LXD A UNP Q03386 ASP 699 DELETION
SEQADV 1LXD A UNP Q03386 VAL 700 DELETION
SEQADV 1LXD A UNP Q03386 GLU 701 DELETION
SEQADV 1LXD A UNP Q03386 GLU 702 DELETION
SEQADV 1LXD A UNP Q03386 ILE 703 DELETION
SEQADV 1LXD A UNP Q03386 ASN 704 DELETION
SEQADV 1LXD A UNP Q03386 MET 705 DELETION
SEQADV 1LXD A UNP Q03386 SER 706 DELETION
SEQADV 1LXD A UNP Q03386 PHE 707 DELETION
SEQADV 1LXD A UNP Q03386 VAL 708 DELETION
SEQADV 1LXD A UNP Q03386 PRO 709 DELETION
SEQADV 1LXD A UNP Q03386 GLU 710 DELETION
SEQADV 1LXD A UNP Q03386 SER 711 DELETION
SEQADV 1LXD A UNP Q03386 PRO 712 DELETION
SEQADV 1LXD A UNP Q03386 ASP 713 DELETION
SEQADV 1LXD A UNP Q03386 GLY 714 DELETION
SEQADV 1LXD A UNP Q03386 GLN 715 DELETION
SEQADV 1LXD A UNP Q03386 GLU 716 DELETION
SEQADV 1LXD A UNP Q03386 LYS 717 DELETION
SEQADV 1LXD A UNP Q03386 LYS 718 DELETION
SEQADV 1LXD A UNP Q03386 PHE 719 DELETION
SEQADV 1LXD A UNP Q03386 TRP 720 DELETION
SEQADV 1LXD A UNP Q03386 GLU 721 DELETION
SEQADV 1LXD A UNP Q03386 SER 722 DELETION
SEQADV 1LXD A UNP Q03386 ALA 723 DELETION
SEQADV 1LXD A UNP Q03386 SER 724 DELETION
SEQADV 1LXD A UNP Q03386 GLN 725 DELETION
SEQADV 1LXD A UNP Q03386 SER 726 DELETION
SEQADV 1LXD A UNP Q03386 SER 727 DELETION
SEQADV 1LXD A UNP Q03386 PRO 728 DELETION
SEQADV 1LXD A UNP Q03386 GLU 729 DELETION
SEQADV 1LXD A UNP Q03386 THR 730 DELETION
SEQADV 1LXD A UNP Q03386 SER 731 DELETION
SEQADV 1LXD A UNP Q03386 GLY 732 DELETION
SEQADV 1LXD A UNP Q03386 ILE 733 DELETION
SEQADV 1LXD A UNP Q03386 SER 734 DELETION
SEQADV 1LXD A UNP Q03386 SER 735 DELETION
SEQADV 1LXD A UNP Q03386 ALA 736 DELETION
SEQADV 1LXD A UNP Q03386 SER 737 DELETION
SEQADV 1LXD A UNP Q03386 SER 738 DELETION
SEQADV 1LXD A UNP Q03386 SER 739 DELETION
SEQADV 1LXD A UNP Q03386 THR 740 DELETION
SEQADV 1LXD A UNP Q03386 SER 741 DELETION
SEQADV 1LXD A UNP Q03386 SER 742 DELETION
SEQADV 1LXD A UNP Q03386 SER 743 DELETION
SEQADV 1LXD A UNP Q03386 SER 744 DELETION
SEQADV 1LXD A UNP Q03386 ALA 745 DELETION
SEQADV 1LXD A UNP Q03386 SER 746 DELETION
SEQADV 1LXD A UNP Q03386 THR 747 DELETION
SEQADV 1LXD A UNP Q03386 THR 748 DELETION
SEQADV 1LXD A UNP Q03386 PRO 749 DELETION
SEQADV 1LXD A UNP Q03386 VAL 750 DELETION
SEQADV 1LXD A UNP Q03386 SER 751 DELETION
SEQADV 1LXD A UNP Q03386 THR 752 DELETION
SEQADV 1LXD A UNP Q03386 THR 753 DELETION
SEQADV 1LXD A UNP Q03386 ARG 754 DELETION
SEQADV 1LXD A UNP Q03386 THR 755 DELETION
SEQADV 1LXD A UNP Q03386 HIS 756 DELETION
SEQADV 1LXD A UNP Q03386 LYS 757 DELETION
SEQADV 1LXD A UNP Q03386 ARG 758 DELETION
SEQADV 1LXD A UNP Q03386 SER 759 DELETION
SEQADV 1LXD A UNP Q03386 VAL 760 DELETION
SEQADV 1LXD A UNP Q03386 SER 761 DELETION
SEQADV 1LXD A UNP Q03386 GLY 762 DELETION
SEQADV 1LXD A UNP Q03386 VAL 763 DELETION
SEQADV 1LXD A UNP Q03386 CYS 764 DELETION
SEQADV 1LXD A UNP Q03386 SER 765 DELETION
SEQADV 1LXD A UNP Q03386 TYR 766 DELETION
SEQADV 1LXD B UNP Q03386 SER 696 DELETION
SEQADV 1LXD B UNP Q03386 THR 697 DELETION
SEQADV 1LXD B UNP Q03386 SER 698 DELETION
SEQADV 1LXD B UNP Q03386 ASP 699 DELETION
SEQADV 1LXD B UNP Q03386 VAL 700 DELETION
SEQADV 1LXD B UNP Q03386 GLU 701 DELETION
SEQADV 1LXD B UNP Q03386 GLU 702 DELETION
SEQADV 1LXD B UNP Q03386 ILE 703 DELETION
SEQADV 1LXD B UNP Q03386 ASN 704 DELETION
SEQADV 1LXD B UNP Q03386 MET 705 DELETION
SEQADV 1LXD B UNP Q03386 SER 706 DELETION
SEQADV 1LXD B UNP Q03386 PHE 707 DELETION
SEQADV 1LXD B UNP Q03386 VAL 708 DELETION
SEQADV 1LXD B UNP Q03386 PRO 709 DELETION
SEQADV 1LXD B UNP Q03386 GLU 710 DELETION
SEQADV 1LXD B UNP Q03386 SER 711 DELETION
SEQADV 1LXD B UNP Q03386 PRO 712 DELETION
SEQADV 1LXD B UNP Q03386 ASP 713 DELETION
SEQADV 1LXD B UNP Q03386 GLY 714 DELETION
SEQADV 1LXD B UNP Q03386 GLN 715 DELETION
SEQADV 1LXD B UNP Q03386 GLU 716 DELETION
SEQADV 1LXD B UNP Q03386 LYS 717 DELETION
SEQADV 1LXD B UNP Q03386 LYS 718 DELETION
SEQADV 1LXD B UNP Q03386 PHE 719 DELETION
SEQADV 1LXD B UNP Q03386 TRP 720 DELETION
SEQADV 1LXD B UNP Q03386 GLU 721 DELETION
SEQADV 1LXD B UNP Q03386 SER 722 DELETION
SEQADV 1LXD B UNP Q03386 ALA 723 DELETION
SEQADV 1LXD B UNP Q03386 SER 724 DELETION
SEQADV 1LXD B UNP Q03386 GLN 725 DELETION
SEQADV 1LXD B UNP Q03386 SER 726 DELETION
SEQADV 1LXD B UNP Q03386 SER 727 DELETION
SEQADV 1LXD B UNP Q03386 PRO 728 DELETION
SEQADV 1LXD B UNP Q03386 GLU 729 DELETION
SEQADV 1LXD B UNP Q03386 THR 730 DELETION
SEQADV 1LXD B UNP Q03386 SER 731 DELETION
SEQADV 1LXD B UNP Q03386 GLY 732 DELETION
SEQADV 1LXD B UNP Q03386 ILE 733 DELETION
SEQADV 1LXD B UNP Q03386 SER 734 DELETION
SEQADV 1LXD B UNP Q03386 SER 735 DELETION
SEQADV 1LXD B UNP Q03386 ALA 736 DELETION
SEQADV 1LXD B UNP Q03386 SER 737 DELETION
SEQADV 1LXD B UNP Q03386 SER 738 DELETION
SEQADV 1LXD B UNP Q03386 SER 739 DELETION
SEQADV 1LXD B UNP Q03386 THR 740 DELETION
SEQADV 1LXD B UNP Q03386 SER 741 DELETION
SEQADV 1LXD B UNP Q03386 SER 742 DELETION
SEQADV 1LXD B UNP Q03386 SER 743 DELETION
SEQADV 1LXD B UNP Q03386 SER 744 DELETION
SEQADV 1LXD B UNP Q03386 ALA 745 DELETION
SEQADV 1LXD B UNP Q03386 SER 746 DELETION
SEQADV 1LXD B UNP Q03386 THR 747 DELETION
SEQADV 1LXD B UNP Q03386 THR 748 DELETION
SEQADV 1LXD B UNP Q03386 PRO 749 DELETION
SEQADV 1LXD B UNP Q03386 VAL 750 DELETION
SEQADV 1LXD B UNP Q03386 SER 751 DELETION
SEQADV 1LXD B UNP Q03386 THR 752 DELETION
SEQADV 1LXD B UNP Q03386 THR 753 DELETION
SEQADV 1LXD B UNP Q03386 ARG 754 DELETION
SEQADV 1LXD B UNP Q03386 THR 755 DELETION
SEQADV 1LXD B UNP Q03386 HIS 756 DELETION
SEQADV 1LXD B UNP Q03386 LYS 757 DELETION
SEQADV 1LXD B UNP Q03386 ARG 758 DELETION
SEQADV 1LXD B UNP Q03386 SER 759 DELETION
SEQADV 1LXD B UNP Q03386 VAL 760 DELETION
SEQADV 1LXD B UNP Q03386 SER 761 DELETION
SEQADV 1LXD B UNP Q03386 GLY 762 DELETION
SEQADV 1LXD B UNP Q03386 VAL 763 DELETION
SEQADV 1LXD B UNP Q03386 CYS 764 DELETION
SEQADV 1LXD B UNP Q03386 SER 765 DELETION
SEQADV 1LXD B UNP Q03386 TYR 766 DELETION
SEQRES 1 A 100 GLY SER SER SER SER LEU PRO LEU TYR ASN GLN GLN VAL
SEQRES 2 A 100 GLY ASP CYS CYS ILE ILE ARG VAL SER LEU ASP VAL ASP
SEQRES 3 A 100 ASN GLY ASN MET TYR LYS SER ILE LEU VAL THR SER GLN
SEQRES 4 A 100 ASP LYS ALA PRO THR VAL ILE ARG LYS ALA MET ASP LYS
SEQRES 5 A 100 HIS ASN LEU ASP GLU ASP GLU PRO GLU ASP TYR GLU LEU
SEQRES 6 A 100 LEU GLN ILE ILE SER GLU ASP HIS LYS LEU LYS ILE PRO
SEQRES 7 A 100 GLU ASN ALA ASN VAL PHE TYR ALA MET ASN SER ALA ALA
SEQRES 8 A 100 ASN TYR ASP PHE ILE LEU LYS LYS ARG
SEQRES 1 B 100 GLY SER SER SER SER LEU PRO LEU TYR ASN GLN GLN VAL
SEQRES 2 B 100 GLY ASP CYS CYS ILE ILE ARG VAL SER LEU ASP VAL ASP
SEQRES 3 B 100 ASN GLY ASN MET TYR LYS SER ILE LEU VAL THR SER GLN
SEQRES 4 B 100 ASP LYS ALA PRO THR VAL ILE ARG LYS ALA MET ASP LYS
SEQRES 5 B 100 HIS ASN LEU ASP GLU ASP GLU PRO GLU ASP TYR GLU LEU
SEQRES 6 B 100 LEU GLN ILE ILE SER GLU ASP HIS LYS LEU LYS ILE PRO
SEQRES 7 B 100 GLU ASN ALA ASN VAL PHE TYR ALA MET ASN SER ALA ALA
SEQRES 8 B 100 ASN TYR ASP PHE ILE LEU LYS LYS ARG
FORMUL 3 HOH *58(H2 O)
HELIX 1 1 ALA A 42 HIS A 53 1 12
HELIX 2 2 PRO A 60 ASP A 62 5 3
HELIX 3 3 VAL A 83 ALA A 86 1 4
HELIX 4 4 ALA B 42 LYS B 52 1 11
HELIX 5 5 PRO B 60 ASP B 62 5 3
HELIX 6 6 VAL B 83 ALA B 86 1 4
SHEET 1 A 5 LYS A 32 THR A 37 0
SHEET 2 A 5 CYS A 16 LEU A 23 -1 N VAL A 21 O LYS A 32
SHEET 3 A 5 ASP A 94 LYS A 99 1 N PHE A 95 O ARG A 20
SHEET 4 A 5 TYR A 63 SER A 70 -1 N LEU A 66 O ILE A 96
SHEET 5 A 5 HIS A 73 LYS A 76 -1 N LEU A 75 O GLN A 67
SHEET 1 B 3 LYS B 32 THR B 37 0
SHEET 2 B 3 CYS B 16 LEU B 23 -1 N VAL B 21 O LYS B 32
SHEET 3 B 3 ASP B 94 LEU B 97 1 N PHE B 95 O ARG B 20
SHEET 1 C 2 LEU B 66 SER B 70 0
SHEET 2 C 2 HIS B 73 LYS B 76 -1 N LEU B 75 O GLN B 67
SSBOND 1 CYS A 16 CYS B 16 1555 1555 2.05
CISPEP 1 LEU B 65 LEU B 66 0 -16.09
CRYST1 105.282 30.714 51.326 90.00 94.57 90.00 C 1 2 1 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 0.009498 0.000000 0.000759 0.00000
SCALE2 0.000000 0.032558 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019545 0.00000
MTRIX1 1 -0.219734 -0.826478 -0.518316 90.18680 1
MTRIX2 1 -0.811699 -0.139838 0.567089 3.10410 1
MTRIX3 1 -0.541167 0.545325 -0.640124 130.45880 1
(ATOM LINES ARE NOT SHOWN.)
END
