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HEADER SIGNALING PROTEIN 10-APR-05 1ZC4 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 1ZC4 1 JRNL REVDAT 1 14-JUN-05 1ZC4 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. 2.50 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.79 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 499774.250 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5 REMARK 3 NUMBER OF REFLECTIONS : 27186 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) : 0.208 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2732 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.30 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3837 REMARK 3 BIN R VALUE (WORKING SET) : 0.2650 REMARK 3 BIN FREE R VALUE : 0.3010 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 419 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4678 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 66 REMARK 3 SOLVENT ATOMS : 153 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 31.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.31000 REMARK 3 B22 (A**2) : -6.66000 REMARK 3 B33 (A**2) : 5.35000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.85000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29 REMARK 3 ESD FROM SIGMAA (A) : 0.28 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) : 0.36 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.36 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.89 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) : 2.310 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.850 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.500 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.270 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 29.94 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 1ZC4 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 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB032553. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-JUN-2004; 15-JUL-2004 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : SSRL; SSRL REMARK 200 BEAMLINE : BL11-1; BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945; 0.97927, 0.97900, REMARK 200 0.89194 REMARK 200 MONOCHROMATOR : SI(111); SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC REMARK 200 QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28917 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 4.900 REMARK 200 R MERGE (I) : 0.09000 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) : 2.48 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.44400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD 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 (%): 60.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11 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 56.69450 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 GLU B 284 REMARK 465 GLU B 285 REMARK 465 ALA B 286 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 465 GLU D 284 REMARK 465 GLU D 285 REMARK 465 ALA D 286 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 35 SD MET A 35 CE -0.054 REMARK 500 MET A 172 SD MET A 172 CE -0.089 REMARK 500 MET B 199 SD MET B 199 CE -0.134 REMARK 500 PRO B 236 CG PRO B 236 CD 0.050 REMARK 500 MET B 241 SD MET B 241 CE -0.142 REMARK 500 MET C 172 SD MET C 172 CE -0.054 REMARK 500 MET D 199 SD MET D 199 CE -0.054 REMARK 500 PRO D 236 CG PRO D 236 CD 0.050 REMARK 500 MET D 241 SD MET D 241 CE -0.099 REMARK 500 MET D 246 SD MET D 246 CE -0.075 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. = -9.0 DEGREES REMARK 500 LEU A 90 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 PHE A 93 N - CA - C ANGL. DEV. = -7.5 DEGREES REMARK 500 ALA B 185 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 PRO B 236 N - CA - C ANGL. DEV. = 7.6 DEGREES REMARK 500 PRO B 236 C - N - CD ANGL. DEV. = -8.1 DEGREES REMARK 500 GLU B 249 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 SER B 250 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 LYS C 47 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 LEU C 90 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 LEU C 124 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ALA D 185 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 ASN D 200 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 PRO D 236 C - N - CD ANGL. DEV. = -9.4 DEGREES REMARK 500 GLU D 249 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 SER D 250 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 52 DISTANCE = 5.08 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ZC3 RELATED DB: PDB DBREF 1ZC4 A 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 1ZC4 C 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 1ZC4 B 167 286 UNP O54924 O54924_RAT 167 286 DBREF 1ZC4 D 167 286 UNP O54924 O54924_RAT 167 286 SEQADV 1ZC4 LEU A 72 UNP P11233 GLN 72 ENGINEERED SEQADV 1ZC4 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 120 LEU GLU THR PRO GLY GLN TYR LEU VAL TYR ASN GLY ASP SEQRES 2 B 120 LEU VAL GLU TYR GLU ALA ASP HIS MET ALA GLN LEU GLN SEQRES 3 B 120 ARG VAL HIS GLY PHE LEU MET ASN ASP CYS LEU LEU VAL SEQRES 4 B 120 ALA THR TRP LEU PRO GLN ARG ARG GLY MET TYR ARG TYR SEQRES 5 B 120 ASN ALA LEU TYR PRO LEU ASP ARG LEU ALA VAL VAL ASN SEQRES 6 B 120 VAL LYS ASP ASN PRO PRO MET LYS ASP MET PHE LYS LEU SEQRES 7 B 120 LEU MET PHE PRO GLU SER ARG ILE PHE GLN ALA GLU ASN SEQRES 8 B 120 ALA LYS ILE LYS ARG GLU TRP LEU GLU VAL LEU GLU GLU SEQRES 9 B 120 THR LYS ARG ALA LEU SER ASP LYS ARG ARG ARG GLU GLN SEQRES 10 B 120 GLU GLU ALA 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 120 LEU GLU THR PRO GLY GLN TYR LEU VAL TYR ASN GLY ASP SEQRES 2 D 120 LEU VAL GLU TYR GLU ALA ASP HIS MET ALA GLN LEU GLN SEQRES 3 D 120 ARG VAL HIS GLY PHE LEU MET ASN ASP CYS LEU LEU VAL SEQRES 4 D 120 ALA THR TRP LEU PRO GLN ARG ARG GLY MET TYR ARG TYR SEQRES 5 D 120 ASN ALA LEU TYR PRO LEU ASP ARG LEU ALA VAL VAL ASN SEQRES 6 D 120 VAL LYS ASP ASN PRO PRO MET LYS ASP MET PHE LYS LEU SEQRES 7 D 120 LEU MET PHE PRO GLU SER ARG ILE PHE GLN ALA GLU ASN SEQRES 8 D 120 ALA LYS ILE LYS ARG GLU TRP LEU GLU VAL LEU GLU GLU SEQRES 9 D 120 THR LYS ARG ALA LEU SER ASP LYS ARG ARG ARG GLU GLN SEQRES 10 D 120 GLU GLU ALA HET MG 200 1 HET MG 300 1 HET GNP 400 32 HET GNP 500 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 *153(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 ALA A 103 1 7 HELIX 4 4 ALA A 103 GLU A 116 1 14 HELIX 5 5 LYS A 128 ARG A 135 5 8 HELIX 6 6 SER A 138 ASN A 150 1 13 HELIX 7 7 ASN A 163 ASP A 182 1 20 HELIX 8 8 ASN B 257 ARG B 281 1 25 HELIX 9 9 GLY C 26 ASP C 37 1 12 HELIX 10 10 TYR C 75 SER C 85 1 11 HELIX 11 11 GLU C 97 ALA C 103 1 7 HELIX 12 12 ALA C 103 GLU C 116 1 14 HELIX 13 13 LEU C 131 ARG C 135 5 5 HELIX 14 14 SER C 138 ASN C 150 1 13 HELIX 15 15 ASN C 163 SER C 183 1 21 HELIX 16 16 ASN D 257 GLN D 283 1 27 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 VAL A 55 O VAL A 62 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 ARG D 251 N LEU D 244 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 LEU D 204 N PHE D 197 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 203 O TYR B 222 SHEET 3 B13 ALA B 189 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 ILE B 252 N TYR B 183 SHEET 6 B13 MET B 241 MET B 246 -1 N PHE B 242 O PHE B 253 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 ASN C 127 N PHE C 93 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 0.22 CISPEP 2 PHE D 247 PRO D 248 0 0.17 CRYST1 52.912 113.389 70.680 90.00 102.77 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 0.018899 0.000000 0.004285 0.00000 SCALE2 0.000000 0.008819 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014507 0.00000