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HEADER SIGNALING PROTEIN 10-APR-05 1ZC3 TITLE CRYSTAL STRUCTURE OF THE RAL-BINDING DOMAIN OF EXO84 IN TITLE 2 COMPLEX WITH THE ACTIVE RALA COMPND MOL_ID: 1; COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAL-A; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: EXOCYST COMPLEX PROTEIN EXO84; COMPND 8 CHAIN: B, D; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: RALA, RAL; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 12 ORGANISM_COMMON: RAT; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PGEX-2T KEYWDS EXOCYTOSIS, SMALL GTPASE, GTP-BINDING PROTEIN, EXPDTA X-RAY DIFFRACTION AUTHOR R.JIN,J.R.JUNUTULA,H.T.MATERN,K.E.ERVIN,R.H.SCHELLER, AUTHOR 2 A.T.BRUNGER REVDAT 2 28-JUN-05 1ZC3 1 JRNL REVDAT 1 14-JUN-05 1ZC3 0 JRNL AUTH R.JIN,J.R.JUNUTULA,H.T.MATERN,K.E.ERVIN, JRNL AUTH 2 R.H.SCHELLER,A.T.BRUNGER JRNL TITL EXO84 AND SEC5 ARE COMPETITIVE REGULATORY SEC6/8 JRNL TITL 2 EFFECTORS TO THE RALA GTPASE. JRNL REF EMBO J. V. 24 2064 2005 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 267842.630 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.2 REMARK 3 NUMBER OF REFLECTIONS : 52234 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) : 0.206 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200 REMARK 3 FREE R VALUE TEST SET COUNT : 5333 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003 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) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.60 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6769 REMARK 3 BIN R VALUE (WORKING SET) : 0.2760 REMARK 3 BIN FREE R VALUE : 0.3040 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 755 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4598 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 66 REMARK 3 SOLVENT ATOMS : 413 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.79000 REMARK 3 B22 (A**2) : -4.25000 REMARK 3 B33 (A**2) : 3.46000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.98000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24 REMARK 3 ESD FROM SIGMAA (A) : 0.23 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) : 0.27 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.87 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) : 2.250 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.430 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.470 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.090 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.34 REMARK 3 BSOL : 42.47 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 : GNP.PAR REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : WATER_REP.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 : GNP.TOP REMARK 3 TOPOLOGY FILE 4 : ION.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ZC3 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB032552. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : SI(111) 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 : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57036 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.08500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02 REMARK 200 COMPLETENESS FOR SHELL (%) : 70.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.46900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 18-22% PEG3350, 0.1-0.2 M AMMONIUM REMARK 280 SULFATE, 0.1 M BIS-TRIS, PH 6.5, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,1/2+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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 56.89750 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 GLN A 9 REMARK 465 ASN A 10 REMARK 465 LEU B 167 REMARK 465 GLU B 168 REMARK 465 THR B 169 REMARK 465 PRO B 170 REMARK 465 GLN C 9 REMARK 465 ASN C 10 REMARK 465 LEU D 167 REMARK 465 GLU D 168 REMARK 465 THR D 169 REMARK 465 PRO D 170 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 172 SD MET A 172 CE -0.070 REMARK 500 MET B 199 SD MET B 199 CE -0.086 REMARK 500 PRO B 236 CG PRO B 236 CD 0.059 REMARK 500 MET D 199 CG MET D 199 SD -0.059 REMARK 500 MET D 246 SD MET D 246 CE -0.067 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LYS A 47 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 LEU A 90 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 PRO B 236 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 SER B 250 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 TYR C 36 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 LYS C 47 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 LEU C 90 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 LEU C 124 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 ALA D 185 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 ASN D 235 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 PRO D 236 N - CA - C ANGL. DEV. = 12.7 DEGREES REMARK 500 PRO D 237 C - N - CA ANGL. DEV. =-10.9 DEGREES REMARK 500 PRO D 237 C - N - CD ANGL. DEV. = 11.7 DEGREES REMARK 500 GLU D 249 N - CA - C ANGL. DEV. = 9.3 DEGREES REMARK 500 SER D 250 N - CA - C ANGL. DEV. =-11.2 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ZC4 RELATED DB: PDB DBREF 1ZC3 A 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 1ZC3 C 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 1ZC3 B 167 279 UNP O54924 O54924_RAT 167 279 DBREF 1ZC3 D 167 279 UNP O54924 O54924_RAT 167 279 SEQADV 1ZC3 LEU A 72 UNP P11233 GLN 72 ENGINEERED SEQADV 1ZC3 LEU C 72 UNP P11233 GLN 72 ENGINEERED SEQRES 1 A 175 GLN ASN SER LEU ALA LEU HIS LYS VAL ILE MET VAL GLY SEQRES 2 A 175 SER GLY GLY VAL GLY LYS SER ALA LEU THR LEU GLN PHE SEQRES 3 A 175 MET TYR ASP GLU PHE VAL GLU ASP TYR GLU PRO THR LYS SEQRES 4 A 175 ALA ASP SER TYR ARG LYS LYS VAL VAL LEU ASP GLY GLU SEQRES 5 A 175 GLU VAL GLN ILE ASP ILE LEU ASP THR ALA GLY LEU GLU SEQRES 6 A 175 ASP TYR ALA ALA ILE ARG ASP ASN TYR PHE ARG SER GLY SEQRES 7 A 175 GLU GLY PHE LEU CYS VAL PHE SER ILE THR GLU MET GLU SEQRES 8 A 175 SER PHE ALA ALA THR ALA ASP PHE ARG GLU GLN ILE LEU SEQRES 9 A 175 ARG VAL LYS GLU ASP GLU ASN VAL PRO PHE LEU LEU VAL SEQRES 10 A 175 GLY ASN LYS SER ASP LEU GLU ASP LYS ARG GLN VAL SER SEQRES 11 A 175 VAL GLU GLU ALA LYS ASN ARG ALA GLU GLN TRP ASN VAL SEQRES 12 A 175 ASN TYR VAL GLU THR SER ALA LYS THR ARG ALA ASN VAL SEQRES 13 A 175 ASP LYS VAL PHE PHE ASP LEU MET ARG GLU ILE ARG ALA SEQRES 14 A 175 ARG LYS MET GLU ASP SER SEQRES 1 B 113 LEU GLU THR PRO GLY GLN TYR LEU VAL TYR ASN GLY ASP SEQRES 2 B 113 LEU VAL GLU TYR GLU ALA ASP HIS MET ALA GLN LEU GLN SEQRES 3 B 113 ARG VAL HIS GLY PHE LEU MET ASN ASP CYS LEU LEU VAL SEQRES 4 B 113 ALA THR TRP LEU PRO GLN ARG ARG GLY MET TYR ARG TYR SEQRES 5 B 113 ASN ALA LEU TYR PRO LEU ASP ARG LEU ALA VAL VAL ASN SEQRES 6 B 113 VAL LYS ASP ASN PRO PRO MET LYS ASP MET PHE LYS LEU SEQRES 7 B 113 LEU MET PHE PRO GLU SER ARG ILE PHE GLN ALA GLU ASN SEQRES 8 B 113 ALA LYS ILE LYS ARG GLU TRP LEU GLU VAL LEU GLU GLU SEQRES 9 B 113 THR LYS ARG ALA LEU SER ASP LYS ARG SEQRES 1 C 175 GLN ASN SER LEU ALA LEU HIS LYS VAL ILE MET VAL GLY SEQRES 2 C 175 SER GLY GLY VAL GLY LYS SER ALA LEU THR LEU GLN PHE SEQRES 3 C 175 MET TYR ASP GLU PHE VAL GLU ASP TYR GLU PRO THR LYS SEQRES 4 C 175 ALA ASP SER TYR ARG LYS LYS VAL VAL LEU ASP GLY GLU SEQRES 5 C 175 GLU VAL GLN ILE ASP ILE LEU ASP THR ALA GLY LEU GLU SEQRES 6 C 175 ASP TYR ALA ALA ILE ARG ASP ASN TYR PHE ARG SER GLY SEQRES 7 C 175 GLU GLY PHE LEU CYS VAL PHE SER ILE THR GLU MET GLU SEQRES 8 C 175 SER PHE ALA ALA THR ALA ASP PHE ARG GLU GLN ILE LEU SEQRES 9 C 175 ARG VAL LYS GLU ASP GLU ASN VAL PRO PHE LEU LEU VAL SEQRES 10 C 175 GLY ASN LYS SER ASP LEU GLU ASP LYS ARG GLN VAL SER SEQRES 11 C 175 VAL GLU GLU ALA LYS ASN ARG ALA GLU GLN TRP ASN VAL SEQRES 12 C 175 ASN TYR VAL GLU THR SER ALA LYS THR ARG ALA ASN VAL SEQRES 13 C 175 ASP LYS VAL PHE PHE ASP LEU MET ARG GLU ILE ARG ALA SEQRES 14 C 175 ARG LYS MET GLU ASP SER SEQRES 1 D 113 LEU GLU THR PRO GLY GLN TYR LEU VAL TYR ASN GLY ASP SEQRES 2 D 113 LEU VAL GLU TYR GLU ALA ASP HIS MET ALA GLN LEU GLN SEQRES 3 D 113 ARG VAL HIS GLY PHE LEU MET ASN ASP CYS LEU LEU VAL SEQRES 4 D 113 ALA THR TRP LEU PRO GLN ARG ARG GLY MET TYR ARG TYR SEQRES 5 D 113 ASN ALA LEU TYR PRO LEU ASP ARG LEU ALA VAL VAL ASN SEQRES 6 D 113 VAL LYS ASP ASN PRO PRO MET LYS ASP MET PHE LYS LEU SEQRES 7 D 113 LEU MET PHE PRO GLU SER ARG ILE PHE GLN ALA GLU ASN SEQRES 8 D 113 ALA LYS ILE LYS ARG GLU TRP LEU GLU VAL LEU GLU GLU SEQRES 9 D 113 THR LYS ARG ALA LEU SER ASP LYS ARG HET MG 500 1 HET MG 600 1 HET GNP 700 32 HET GNP 800 32 HETNAM MG MAGNESIUM ION HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER FORMUL 5 MG 2(MG 2+) FORMUL 7 GNP 2(C10 H17 N6 O13 P3) FORMUL 9 HOH *413(H2 O) HELIX 1 1 GLY A 26 ASP A 37 1 12 HELIX 2 2 TYR A 75 SER A 85 1 11 HELIX 3 3 GLU A 97 GLU A 116 1 20 HELIX 4 4 LYS A 128 ARG A 135 5 8 HELIX 5 5 SER A 138 TRP A 149 1 12 HELIX 6 6 ASN A 163 ASP A 182 1 20 HELIX 7 7 ASN B 257 ARG B 279 1 23 HELIX 8 8 GLY C 26 ASP C 37 1 12 HELIX 9 9 TYR C 75 SER C 85 1 11 HELIX 10 10 GLU C 97 ALA C 103 1 7 HELIX 11 11 ALA C 103 GLU C 116 1 14 HELIX 12 12 LEU C 131 ARG C 135 5 5 HELIX 13 13 SER C 138 ASN C 150 1 13 HELIX 14 14 ASN C 163 SER C 183 1 21 HELIX 15 15 ASN D 257 ASP D 277 1 21 SHEET 1 A13 TYR A 153 GLU A 155 0 SHEET 2 A13 PHE A 122 ASN A 127 1 N GLY A 126 O VAL A 154 SHEET 3 A13 GLY A 88 SER A 94 1 N CYS A 91 O VAL A 125 SHEET 4 A13 LEU A 14 VAL A 20 1 N VAL A 20 O VAL A 92 SHEET 5 A13 GLU A 60 THR A 69 1 O ASP A 65 N VAL A 17 SHEET 6 A13 ALA A 48 LEU A 57 -1 N LEU A 57 O GLU A 60 SHEET 7 A13 ALA D 228 VAL D 232 1 O ASN D 231 N ALA A 48 SHEET 8 A13 MET D 241 MET D 246 -1 O LYS D 243 N VAL D 230 SHEET 9 A13 GLU D 249 GLN D 254 -1 O GLU D 249 N MET D 246 SHEET 10 A13 LEU D 174 TYR D 183 -1 N VAL D 181 O GLN D 254 SHEET 11 A13 GLN D 190 MET D 199 -1 O LEU D 198 N TYR D 176 SHEET 12 A13 CYS D 202 LEU D 209 -1 O ALA D 206 N HIS D 195 SHEET 13 A13 TYR D 216 PRO D 223 -1 O TYR D 222 N LEU D 203 SHEET 1 B13 TYR B 216 PRO B 223 0 SHEET 2 B13 CYS B 202 LEU B 209 -1 N LEU B 209 O TYR B 216 SHEET 3 B13 GLN B 190 MET B 199 -1 N PHE B 197 O LEU B 204 SHEET 4 B13 LEU B 174 GLU B 184 -1 N TYR B 176 O LEU B 198 SHEET 5 B13 GLU B 249 GLN B 254 -1 O GLN B 254 N VAL B 181 SHEET 6 B13 MET B 241 MET B 246 -1 N LEU B 244 O ARG B 251 SHEET 7 B13 ALA B 228 VAL B 232 -1 N VAL B 230 O LYS B 243 SHEET 8 B13 ALA C 48 LEU C 57 1 O ALA C 48 N ASN B 231 SHEET 9 B13 GLU C 60 THR C 69 -1 O GLU C 60 N LEU C 57 SHEET 10 B13 LEU C 14 VAL C 20 1 N VAL C 17 O ASP C 65 SHEET 11 B13 GLY C 88 SER C 94 1 O VAL C 92 N VAL C 20 SHEET 12 B13 PHE C 122 ASN C 127 1 O VAL C 125 N CYS C 91 SHEET 13 B13 ASN C 152 GLU C 155 1 O ASN C 152 N LEU C 124 CISPEP 1 PHE B 247 PRO B 248 0 -0.07 CISPEP 2 PHE D 247 PRO D 248 0 0.15 CRYST1 52.469 113.795 71.012 90.00 102.86 90.00 P 1 21 1 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 0.019059 0.000000 0.004350 0.00000 SCALE2 0.000000 0.008788 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014444 0.00000