HEADER SIGNALING PROTEIN 17-DEC-07 2ZET
TITLE CRYSTAL STRUCTURE OF THE SMALL GTPASE RAB27B COMPLEXED WITH THE SLP
TITLE 2 HOMOLOGY DOMAIN OF SLAC2-A/MELANOPHILIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAB-27B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: GTPASE DOMAIN, UNP RESIDUES 1-201;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MELANOPHILIN;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: SLP HOMOLOGY DOMAIN, UNP RESIDUES 1-146;
COMPND 11 SYNONYM: EXOPHILIN-3, LEADEN PROTEIN, SYNAPTOTAGMIN-LIKE PROTEIN 2A,
COMPND 12 SLP HOMOLOG LACKING C2 DOMAINS A, SLAC2-A;
COMPND 13 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: RAB27B;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PX070112-08;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: SLAC2A;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PX051201-06;
SOURCE 16 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS COMPLEX, GTP-BINDING PROTEIN, GTPASE, G-PROTEIN, RAB, RAB27B,
KEYWDS 2 EFFECTOR, MELANOPHILIN, SLP HOMOLOGY DOMAIN, ACETYLATION,
KEYWDS 3 LIPOPROTEIN, MEMBRANE, METHYLATION, NUCLEOTIDE-BINDING, PRENYLATION,
KEYWDS 4 COILED COIL, METAL-BINDING, ZINC, ZINC-FINGER, STRUCTURAL GENOMICS,
KEYWDS 5 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 6 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 7 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KUKIMOTO-NIINO,A.SAKAMOTO,E.KANNO,K.HANAWA-SUETSUGU,T.TERADA,
AUTHOR 2 M.SHIROUZU,M.FUKUDA,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 3 INITIATIVE (RSGI)
REVDAT 5 10-NOV-21 2ZET 1 REMARK SEQADV LINK
REVDAT 4 05-JAN-10 2ZET 1 JRNL
REVDAT 3 24-FEB-09 2ZET 1 VERSN
REVDAT 2 14-OCT-08 2ZET 1 JRNL
REVDAT 1 30-SEP-08 2ZET 0
JRNL AUTH M.KUKIMOTO-NIINO,A.SAKAMOTO,E.KANNO,K.HANAWA-SUETSUGU,
JRNL AUTH 2 T.TERADA,M.SHIROUZU,M.FUKUDA,S.YOKOYAMA
JRNL TITL STRUCTURAL BASIS FOR THE EXCLUSIVE SPECIFICITY OF
JRNL TITL 2 SLAC2-A/MELANOPHILIN FOR THE RAB27 GTPASES.
JRNL REF STRUCTURE V. 16 1478 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18940604
JRNL DOI 10.1016/J.STR.2008.07.014
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2503339.380
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23411
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) : 0.247
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2311
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3473
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE : 0.4000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 326
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5208
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 9
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.57000
REMARK 3 B22 (A**2) : 9.57000
REMARK 3 B33 (A**2) : -19.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.53
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.60
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 24.56
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : GTP_PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : GTP_XPLOR_TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000027881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23600
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.78100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.450
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.65M (NH4)2SO4, 0.1M TRIS-HCL, PH
REMARK 280 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 162.74200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.10400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.10400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.37100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.10400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.10400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 244.11300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.10400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.10400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.37100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.10400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.10400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 244.11300
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 162.74200
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: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 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: 4720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 ASP A 3
REMARK 465 GLY A 4
REMARK 465 ASP A 59
REMARK 465 GLY A 60
REMARK 465 ALA A 61
REMARK 465 VAL A 189
REMARK 465 GLU A 190
REMARK 465 LYS A 191
REMARK 465 THR A 192
REMARK 465 GLN A 193
REMARK 465 VAL A 194
REMARK 465 PRO A 195
REMARK 465 ASP A 196
REMARK 465 THR A 197
REMARK 465 VAL A 198
REMARK 465 ASN A 199
REMARK 465 GLY A 200
REMARK 465 GLY A 201
REMARK 465 GLY C -6
REMARK 465 SER C -5
REMARK 465 SER C -4
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 SER C -1
REMARK 465 GLY C 0
REMARK 465 MSE C 1
REMARK 465 GLY C 2
REMARK 465 LYS C 3
REMARK 465 LEU C 145
REMARK 465 GLN C 146
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 ASP B 3
REMARK 465 GLY B 4
REMARK 465 GLN B 56
REMARK 465 GLY B 57
REMARK 465 ALA B 58
REMARK 465 ASP B 59
REMARK 465 GLY B 60
REMARK 465 ALA B 61
REMARK 465 SER B 62
REMARK 465 GLY B 63
REMARK 465 LYS B 64
REMARK 465 ALA B 65
REMARK 465 VAL B 189
REMARK 465 GLU B 190
REMARK 465 LYS B 191
REMARK 465 THR B 192
REMARK 465 GLN B 193
REMARK 465 VAL B 194
REMARK 465 PRO B 195
REMARK 465 ASP B 196
REMARK 465 THR B 197
REMARK 465 VAL B 198
REMARK 465 ASN B 199
REMARK 465 GLY B 200
REMARK 465 GLY B 201
REMARK 465 GLY D -6
REMARK 465 SER D -5
REMARK 465 SER D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 SER D -1
REMARK 465 GLY D 0
REMARK 465 MSE D 1
REMARK 465 GLY D 2
REMARK 465 LYS D 3
REMARK 465 LEU D 145
REMARK 465 GLN D 146
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 PRO C 97 C - N - CA ANGL. DEV. = 12.0 DEGREES
REMARK 500 PRO D 97 C - N - CA ANGL. DEV. = 11.9 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 TYR A 6 164.04 175.71
REMARK 500 THR A 40 124.42 -34.69
REMARK 500 SER A 103 91.80 -171.88
REMARK 500 GLN A 105 -71.51 -58.63
REMARK 500 LYS A 134 49.86 75.47
REMARK 500 LEU A 137 64.34 -118.94
REMARK 500 GLN A 168 99.74 -47.62
REMARK 500 ASN A 169 -12.05 76.20
REMARK 500 GLU A 186 -15.00 -47.03
REMARK 500 LYS A 187 41.31 -92.16
REMARK 500 ALA C 57 128.72 -26.47
REMARK 500 ARG C 66 -61.28 -100.96
REMARK 500 LEU C 68 -0.92 64.32
REMARK 500 ASN C 76 -162.65 -111.84
REMARK 500 ARG C 78 144.69 -26.78
REMARK 500 GLU C 83 -68.21 -94.22
REMARK 500 PRO C 97 -54.77 -27.30
REMARK 500 GLU C 99 132.84 161.31
REMARK 500 LYS B 22 -71.90 -46.79
REMARK 500 ILE B 39 79.06 -103.98
REMARK 500 THR B 40 131.65 -21.82
REMARK 500 ASP B 45 137.81 176.25
REMARK 500 GLU B 79 11.27 -63.95
REMARK 500 THR B 102 59.99 -100.44
REMARK 500 SER B 103 92.86 170.40
REMARK 500 LYS B 134 67.41 70.43
REMARK 500 ARG B 141 98.97 -56.62
REMARK 500 MSE B 182 -6.83 -57.29
REMARK 500 LEU D 7 51.26 -101.93
REMARK 500 LEU D 53 20.47 -75.27
REMARK 500 ALA D 57 125.94 -38.36
REMARK 500 GLU D 83 -81.73 -81.10
REMARK 500 LEU D 86 -167.29 -115.07
REMARK 500 PRO D 97 -37.71 -23.74
REMARK 500 GLU D 99 153.30 162.15
REMARK 500 ASP D 105 -58.42 -27.67
REMARK 500 ALA D 127 40.27 -92.37
REMARK 500 ARG D 128 -10.22 -168.24
REMARK 500
REMARK 500 REMARK: NULL
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 A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 23 OG1
REMARK 620 2 THR A 41 OG1 65.1
REMARK 620 3 GTP A 203 O1G 119.0 65.1
REMARK 620 4 GTP A 203 O2B 94.1 117.4 79.5
REMARK 620 5 GTP A 203 O3B 155.5 123.6 59.3 61.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 64 SG
REMARK 620 2 CYS C 67 SG 115.2
REMARK 620 3 CYS C 89 SG 120.7 109.5
REMARK 620 4 CYS C 92 SG 109.0 108.8 90.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 81 SG
REMARK 620 2 CYS C 84 SG 135.9
REMARK 620 3 CYS C 104 SG 94.8 113.4
REMARK 620 4 CYS C 107 SG 95.7 118.4 86.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 23 OG1
REMARK 620 2 THR B 41 OG1 73.4
REMARK 620 3 GTP B 203 O1G 121.2 65.6
REMARK 620 4 GTP B 203 O2B 87.2 127.9 86.5
REMARK 620 5 GTP B 203 O3B 147.6 123.6 59.3 60.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 64 SG
REMARK 620 2 CYS D 67 SG 116.3
REMARK 620 3 CYS D 89 SG 118.8 110.8
REMARK 620 4 CYS D 92 SG 107.7 110.8 88.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 81 SG
REMARK 620 2 CYS D 84 SG 138.2
REMARK 620 3 CYS D 104 SG 110.6 96.4
REMARK 620 4 CYS D 107 SG 126.9 86.1 83.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP B 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: AR_001000757.1 RELATED DB: TARGETDB
DBREF 2ZET A 1 201 UNP Q99P58 RB27B_MOUSE 1 201
DBREF 2ZET C 1 146 UNP Q91V27 MELPH_MOUSE 1 146
DBREF 2ZET B 1 201 UNP Q99P58 RB27B_MOUSE 1 201
DBREF 2ZET D 1 146 UNP Q91V27 MELPH_MOUSE 1 146
SEQADV 2ZET GLY A -1 UNP Q99P58 EXPRESSION TAG
SEQADV 2ZET SER A 0 UNP Q99P58 EXPRESSION TAG
SEQADV 2ZET LEU A 78 UNP Q99P58 GLN 78 ENGINEERED MUTATION
SEQADV 2ZET GLY C -6 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER C -5 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER C -4 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET GLY C -3 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER C -2 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER C -1 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET GLY C 0 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET GLY B -1 UNP Q99P58 EXPRESSION TAG
SEQADV 2ZET SER B 0 UNP Q99P58 EXPRESSION TAG
SEQADV 2ZET LEU B 78 UNP Q99P58 GLN 78 ENGINEERED MUTATION
SEQADV 2ZET GLY D -6 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER D -5 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER D -4 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET GLY D -3 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER D -2 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET SER D -1 UNP Q91V27 EXPRESSION TAG
SEQADV 2ZET GLY D 0 UNP Q91V27 EXPRESSION TAG
SEQRES 1 A 203 GLY SER MSE THR ASP GLY ASP TYR ASP TYR LEU ILE LYS
SEQRES 2 A 203 LEU LEU ALA LEU GLY ASP SER GLY VAL GLY LYS THR THR
SEQRES 3 A 203 PHE LEU TYR ARG TYR THR ASP ASN LYS PHE ASN PRO LYS
SEQRES 4 A 203 PHE ILE THR THR VAL GLY ILE ASP PHE ARG GLU LYS ARG
SEQRES 5 A 203 VAL VAL TYR ASP THR GLN GLY ALA ASP GLY ALA SER GLY
SEQRES 6 A 203 LYS ALA PHE LYS VAL HIS LEU GLN LEU TRP ASP THR ALA
SEQRES 7 A 203 GLY LEU GLU ARG PHE ARG SER LEU THR THR ALA PHE PHE
SEQRES 8 A 203 ARG ASP ALA MSE GLY PHE LEU LEU MSE PHE ASP LEU THR
SEQRES 9 A 203 SER GLN GLN SER PHE LEU ASN VAL ARG ASN TRP MSE SER
SEQRES 10 A 203 GLN LEU GLN ALA ASN ALA TYR CYS GLU ASN PRO ASP ILE
SEQRES 11 A 203 VAL LEU ILE GLY ASN LYS ALA ASP LEU PRO ASP GLN ARG
SEQRES 12 A 203 GLU VAL ASN GLU ARG GLN ALA ARG GLU LEU ALA GLU LYS
SEQRES 13 A 203 TYR GLY ILE PRO TYR PHE GLU THR SER ALA ALA THR GLY
SEQRES 14 A 203 GLN ASN VAL GLU LYS SER VAL GLU THR LEU LEU ASP LEU
SEQRES 15 A 203 ILE MSE LYS ARG MSE GLU LYS CYS VAL GLU LYS THR GLN
SEQRES 16 A 203 VAL PRO ASP THR VAL ASN GLY GLY
SEQRES 1 C 153 GLY SER SER GLY SER SER GLY MSE GLY LYS ARG LEU ASP
SEQRES 2 C 153 LEU SER THR LEU THR ASP GLU GLU ALA GLU HIS VAL TRP
SEQRES 3 C 153 ALA VAL VAL GLN ARG ASP PHE ASP LEU ARG ARG ARG GLU
SEQRES 4 C 153 GLU GLU ARG LEU GLN GLY LEU LYS GLY LYS ILE GLN LYS
SEQRES 5 C 153 GLU SER SER LYS ARG GLU LEU LEU SER ASP THR ALA HIS
SEQRES 6 C 153 LEU ASN GLU THR HIS CYS ALA ARG CYS LEU GLN PRO TYR
SEQRES 7 C 153 ARG LEU LEU LEU ASN SER ARG ARG GLN CYS LEU GLU CYS
SEQRES 8 C 153 SER LEU PHE VAL CYS LYS SER CYS SER HIS ALA HIS PRO
SEQRES 9 C 153 GLU GLU GLN GLY TRP LEU CYS ASP PRO CYS HIS LEU ALA
SEQRES 10 C 153 ARG VAL VAL LYS ILE GLY SER LEU GLU TRP TYR TYR GLN
SEQRES 11 C 153 HIS VAL ARG ALA ARG PHE LYS ARG PHE GLY SER ALA LYS
SEQRES 12 C 153 VAL ILE ARG SER LEU CYS GLY ARG LEU GLN
SEQRES 1 B 203 GLY SER MSE THR ASP GLY ASP TYR ASP TYR LEU ILE LYS
SEQRES 2 B 203 LEU LEU ALA LEU GLY ASP SER GLY VAL GLY LYS THR THR
SEQRES 3 B 203 PHE LEU TYR ARG TYR THR ASP ASN LYS PHE ASN PRO LYS
SEQRES 4 B 203 PHE ILE THR THR VAL GLY ILE ASP PHE ARG GLU LYS ARG
SEQRES 5 B 203 VAL VAL TYR ASP THR GLN GLY ALA ASP GLY ALA SER GLY
SEQRES 6 B 203 LYS ALA PHE LYS VAL HIS LEU GLN LEU TRP ASP THR ALA
SEQRES 7 B 203 GLY LEU GLU ARG PHE ARG SER LEU THR THR ALA PHE PHE
SEQRES 8 B 203 ARG ASP ALA MSE GLY PHE LEU LEU MSE PHE ASP LEU THR
SEQRES 9 B 203 SER GLN GLN SER PHE LEU ASN VAL ARG ASN TRP MSE SER
SEQRES 10 B 203 GLN LEU GLN ALA ASN ALA TYR CYS GLU ASN PRO ASP ILE
SEQRES 11 B 203 VAL LEU ILE GLY ASN LYS ALA ASP LEU PRO ASP GLN ARG
SEQRES 12 B 203 GLU VAL ASN GLU ARG GLN ALA ARG GLU LEU ALA GLU LYS
SEQRES 13 B 203 TYR GLY ILE PRO TYR PHE GLU THR SER ALA ALA THR GLY
SEQRES 14 B 203 GLN ASN VAL GLU LYS SER VAL GLU THR LEU LEU ASP LEU
SEQRES 15 B 203 ILE MSE LYS ARG MSE GLU LYS CYS VAL GLU LYS THR GLN
SEQRES 16 B 203 VAL PRO ASP THR VAL ASN GLY GLY
SEQRES 1 D 153 GLY SER SER GLY SER SER GLY MSE GLY LYS ARG LEU ASP
SEQRES 2 D 153 LEU SER THR LEU THR ASP GLU GLU ALA GLU HIS VAL TRP
SEQRES 3 D 153 ALA VAL VAL GLN ARG ASP PHE ASP LEU ARG ARG ARG GLU
SEQRES 4 D 153 GLU GLU ARG LEU GLN GLY LEU LYS GLY LYS ILE GLN LYS
SEQRES 5 D 153 GLU SER SER LYS ARG GLU LEU LEU SER ASP THR ALA HIS
SEQRES 6 D 153 LEU ASN GLU THR HIS CYS ALA ARG CYS LEU GLN PRO TYR
SEQRES 7 D 153 ARG LEU LEU LEU ASN SER ARG ARG GLN CYS LEU GLU CYS
SEQRES 8 D 153 SER LEU PHE VAL CYS LYS SER CYS SER HIS ALA HIS PRO
SEQRES 9 D 153 GLU GLU GLN GLY TRP LEU CYS ASP PRO CYS HIS LEU ALA
SEQRES 10 D 153 ARG VAL VAL LYS ILE GLY SER LEU GLU TRP TYR TYR GLN
SEQRES 11 D 153 HIS VAL ARG ALA ARG PHE LYS ARG PHE GLY SER ALA LYS
SEQRES 12 D 153 VAL ILE ARG SER LEU CYS GLY ARG LEU GLN
MODRES 2ZET MSE A 93 MET SELENOMETHIONINE
MODRES 2ZET MSE A 98 MET SELENOMETHIONINE
MODRES 2ZET MSE A 114 MET SELENOMETHIONINE
MODRES 2ZET MSE A 182 MET SELENOMETHIONINE
MODRES 2ZET MSE A 185 MET SELENOMETHIONINE
MODRES 2ZET MSE B 93 MET SELENOMETHIONINE
MODRES 2ZET MSE B 98 MET SELENOMETHIONINE
MODRES 2ZET MSE B 114 MET SELENOMETHIONINE
MODRES 2ZET MSE B 182 MET SELENOMETHIONINE
MODRES 2ZET MSE B 185 MET SELENOMETHIONINE
HET MSE A 93 8
HET MSE A 98 8
HET MSE A 114 8
HET MSE A 182 8
HET MSE A 185 8
HET MSE B 93 8
HET MSE B 98 8
HET MSE B 114 8
HET MSE B 182 8
HET MSE B 185 8
HET MG A 202 1
HET GTP A 203 32
HET ZN C 301 1
HET ZN C 302 1
HET SO4 C 303 5
HET MG B 202 1
HET GTP B 203 32
HET ZN D 301 1
HET ZN D 302 1
HET SO4 D 303 5
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 5 MG 2(MG 2+)
FORMUL 6 GTP 2(C10 H16 N5 O14 P3)
FORMUL 7 ZN 4(ZN 2+)
FORMUL 9 SO4 2(O4 S 2-)
FORMUL 15 HOH *9(H2 O)
HELIX 1 1 GLY A 21 ASN A 32 1 12
HELIX 2 2 PHE A 81 PHE A 88 1 8
HELIX 3 3 PHE A 89 ALA A 92 5 4
HELIX 4 4 SER A 103 ALA A 121 1 19
HELIX 5 5 LEU A 137 ARG A 141 5 5
HELIX 6 6 ASN A 144 TYR A 155 1 12
HELIX 7 7 ASN A 169 GLU A 186 1 18
HELIX 8 8 THR C 11 SER C 54 1 44
HELIX 9 9 HIS C 58 THR C 62 5 5
HELIX 10 10 PRO C 70 LEU C 74 5 5
HELIX 11 11 CYS C 89 SER C 91 5 3
HELIX 12 12 ASP C 105 LEU C 118 1 14
HELIX 13 13 LEU C 118 ALA C 127 1 10
HELIX 14 14 PHE C 132 LEU C 141 1 10
HELIX 15 15 GLY B 21 ASN B 32 1 12
HELIX 16 16 PHE B 81 ALA B 87 1 7
HELIX 17 17 PHE B 88 ALA B 92 5 5
HELIX 18 18 SER B 103 ALA B 121 1 19
HELIX 19 19 LEU B 137 ARG B 141 5 5
HELIX 20 20 ASN B 144 GLY B 156 1 13
HELIX 21 21 ASN B 169 GLU B 186 1 18
HELIX 22 22 THR D 11 LEU D 53 1 43
HELIX 23 23 SER D 54 THR D 56 5 3
HELIX 24 24 HIS D 58 HIS D 63 1 6
HELIX 25 25 PRO D 70 LEU D 74 5 5
HELIX 26 26 CYS D 89 SER D 91 5 3
HELIX 27 27 ASP D 105 SER D 117 1 13
HELIX 28 28 LEU D 118 ALA D 127 1 10
HELIX 29 29 PHE D 132 LEU D 141 1 10
SHEET 1 A 6 ILE A 44 ASP A 54 0
SHEET 2 A 6 ALA A 65 THR A 75 -1 O LEU A 72 N ARG A 47
SHEET 3 A 6 TYR A 8 LEU A 15 1 N LEU A 12 O TRP A 73
SHEET 4 A 6 GLY A 94 ASP A 100 1 O LEU A 96 N LEU A 13
SHEET 5 A 6 ASP A 127 ASN A 133 1 O ILE A 131 N PHE A 99
SHEET 6 A 6 TYR A 159 THR A 162 1 O THR A 162 N GLY A 132
SHEET 1 B 2 ARG C 79 GLN C 80 0
SHEET 2 B 2 PHE C 87 VAL C 88 -1 O VAL C 88 N ARG C 79
SHEET 1 C 2 SER C 93 HIS C 94 0
SHEET 2 C 2 LEU C 103 CYS C 104 -1 O LEU C 103 N HIS C 94
SHEET 1 D 5 PHE B 46 VAL B 52 0
SHEET 2 D 5 LYS B 67 ASP B 74 -1 O VAL B 68 N VAL B 51
SHEET 3 D 5 TYR B 8 LEU B 15 1 N LEU B 12 O TRP B 73
SHEET 4 D 5 GLY B 94 ASP B 100 1 O LEU B 96 N LEU B 13
SHEET 5 D 5 ASP B 127 ILE B 128 1 O ASP B 127 N PHE B 95
SHEET 1 E 6 PHE B 46 VAL B 52 0
SHEET 2 E 6 LYS B 67 ASP B 74 -1 O VAL B 68 N VAL B 51
SHEET 3 E 6 TYR B 8 LEU B 15 1 N LEU B 12 O TRP B 73
SHEET 4 E 6 GLY B 94 ASP B 100 1 O LEU B 96 N LEU B 13
SHEET 5 E 6 LEU B 130 ASN B 133 1 O ASN B 133 N PHE B 99
SHEET 6 E 6 TYR B 159 THR B 162 1 O PHE B 160 N GLY B 132
SHEET 1 F 2 ARG D 79 GLN D 80 0
SHEET 2 F 2 PHE D 87 VAL D 88 -1 O VAL D 88 N ARG D 79
SHEET 1 G 2 SER D 93 HIS D 94 0
SHEET 2 G 2 LEU D 103 CYS D 104 -1 O LEU D 103 N HIS D 94
LINK C ALA A 92 N MSE A 93 1555 1555 1.33
LINK C MSE A 93 N GLY A 94 1555 1555 1.33
LINK C LEU A 97 N MSE A 98 1555 1555 1.33
LINK C MSE A 98 N PHE A 99 1555 1555 1.33
LINK C TRP A 113 N MSE A 114 1555 1555 1.33
LINK C MSE A 114 N SER A 115 1555 1555 1.33
LINK C ILE A 181 N MSE A 182 1555 1555 1.33
LINK C MSE A 182 N LYS A 183 1555 1555 1.33
LINK C ARG A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N GLU A 186 1555 1555 1.33
LINK C ALA B 92 N MSE B 93 1555 1555 1.33
LINK C MSE B 93 N GLY B 94 1555 1555 1.32
LINK C LEU B 97 N MSE B 98 1555 1555 1.33
LINK C MSE B 98 N PHE B 99 1555 1555 1.33
LINK C TRP B 113 N MSE B 114 1555 1555 1.33
LINK C MSE B 114 N SER B 115 1555 1555 1.33
LINK C ILE B 181 N MSE B 182 1555 1555 1.32
LINK C MSE B 182 N LYS B 183 1555 1555 1.33
LINK C ARG B 184 N MSE B 185 1555 1555 1.33
LINK C MSE B 185 N GLU B 186 1555 1555 1.33
LINK OG1 THR A 23 MG MG A 202 1555 1555 2.61
LINK OG1 THR A 41 MG MG A 202 1555 1555 2.52
LINK MG MG A 202 O1G GTP A 203 1555 1555 2.45
LINK MG MG A 202 O2B GTP A 203 1555 1555 2.46
LINK MG MG A 202 O3B GTP A 203 1555 1555 2.67
LINK SG CYS C 64 ZN ZN C 302 1555 1555 2.39
LINK SG CYS C 67 ZN ZN C 302 1555 1555 2.33
LINK SG CYS C 81 ZN ZN C 301 1555 1555 2.52
LINK SG CYS C 84 ZN ZN C 301 1555 1555 2.26
LINK SG CYS C 89 ZN ZN C 302 1555 1555 2.54
LINK SG CYS C 92 ZN ZN C 302 1555 1555 2.46
LINK SG CYS C 104 ZN ZN C 301 1555 1555 2.40
LINK SG CYS C 107 ZN ZN C 301 1555 1555 2.39
LINK OG1 THR B 23 MG MG B 202 1555 1555 2.20
LINK OG1 THR B 41 MG MG B 202 1555 1555 2.46
LINK MG MG B 202 O1G GTP B 203 1555 1555 2.36
LINK MG MG B 202 O2B GTP B 203 1555 1555 2.39
LINK MG MG B 202 O3B GTP B 203 1555 1555 2.79
LINK SG CYS D 64 ZN ZN D 302 1555 1555 2.43
LINK SG CYS D 67 ZN ZN D 302 1555 1555 2.48
LINK SG CYS D 81 ZN ZN D 301 1555 1555 2.38
LINK SG CYS D 84 ZN ZN D 301 1555 1555 2.38
LINK SG CYS D 89 ZN ZN D 302 1555 1555 2.46
LINK SG CYS D 92 ZN ZN D 302 1555 1555 2.42
LINK SG CYS D 104 ZN ZN D 301 1555 1555 2.50
LINK SG CYS D 107 ZN ZN D 301 1555 1555 2.52
SITE 1 AC1 4 CYS C 81 CYS C 84 CYS C 104 CYS C 107
SITE 1 AC2 4 CYS C 64 CYS C 67 CYS C 89 CYS C 92
SITE 1 AC3 5 ARG A 90 PHE C 129 LYS C 130 ARG C 131
SITE 2 AC3 5 LYS C 136
SITE 1 AC4 3 THR A 23 THR A 41 GTP A 203
SITE 1 AC5 4 CYS D 81 CYS D 84 CYS D 104 CYS D 107
SITE 1 AC6 4 CYS D 64 CYS D 67 CYS D 89 CYS D 92
SITE 1 AC7 4 ARG B 90 LYS D 130 ARG D 131 LYS D 136
SITE 1 AC8 3 THR B 23 THR B 41 GTP B 203
SITE 1 AC9 22 ASP A 17 SER A 18 GLY A 19 VAL A 20
SITE 2 AC9 22 GLY A 21 LYS A 22 THR A 23 THR A 24
SITE 3 AC9 22 PRO A 36 LYS A 37 PHE A 38 THR A 40
SITE 4 AC9 22 THR A 41 GLY A 77 ASN A 133 LYS A 134
SITE 5 AC9 22 ASP A 136 LEU A 137 SER A 163 ALA A 164
SITE 6 AC9 22 ALA A 165 MG A 202
SITE 1 BC1 22 ASP B 17 SER B 18 GLY B 19 VAL B 20
SITE 2 BC1 22 GLY B 21 LYS B 22 THR B 23 THR B 24
SITE 3 BC1 22 PRO B 36 LYS B 37 PHE B 38 THR B 40
SITE 4 BC1 22 THR B 41 GLY B 77 ASN B 133 LYS B 134
SITE 5 BC1 22 ASP B 136 LEU B 137 SER B 163 ALA B 164
SITE 6 BC1 22 ALA B 165 MG B 202
CRYST1 82.208 82.208 325.484 90.00 90.00 90.00 P 41 21 2 16
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 0.012164 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003072 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
