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HEADER ENDOCYTOSIS/EXOCYTOSIS 09-MAR-03 1UAD TITLE CRYSTAL STRUCTURE OF THE RALA-GPPNHP-SEC5 RAL-BINDING TITLE 2 DOMAIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAL-A; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 9-183; COMPND 5 SYNONYM: RALA; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: EXOCYST COMPLEX COMPONENT SEC5; COMPND 9 CHAIN: C, D; COMPND 10 FRAGMENT: N-TERMINAL DOMAIN, SEC5 RAL-BINDING DOMAIN; COMPND 11 SYNONYM: RSEC5; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-RIL; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX2T; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 11 ORGANISM_COMMON: RAT; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21-RIL; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PGEX2T KEYWDS SMALL GTP-BINDING PROTEIN, IMMUNOGLOBLIN-LIKE FOLD, BETA- KEYWDS 2 SANDWICH EXPDTA X-RAY DIFFRACTION AUTHOR S.FUKAI,H.T.MATERN,R.H.SCHELLER,A.T.BRUNGER REVDAT 1 15-JUL-03 1UAD 0 JRNL AUTH S.FUKAI,H.T.MATERN,J.R.JAGATH,R.H.SCHELLER, JRNL AUTH 2 A.T.BRUNGER JRNL TITL STRUCTURAL BASIS OF THE INTERACTION BETWEEN RALA JRNL TITL 2 AND SEC5, A SUBUNIT OF THE SEC6/8 COMPLEX JRNL REF EMBO J. V. 22 3267 2003 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.10 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.51 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2588488.640 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 40357 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) : 0.219 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4051 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5940 REMARK 3 BIN R VALUE (WORKING SET) : 0.2790 REMARK 3 BIN FREE R VALUE : 0.3190 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 675 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4134 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 66 REMARK 3 SOLVENT ATOMS : 222 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 5.03000 REMARK 3 B22 (A**2) : 5.03000 REMARK 3 B33 (A**2) : -10.07000 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) : 0.27 REMARK 3 ESD FROM SIGMAA (A) : 0.25 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) : 0.32 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.76 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) : 1.540 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.540 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.990 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.930 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.32 REMARK 3 BSOL : 44.29 REMARK 3 REMARK 3 NCS MODEL : CONSTR 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 : GNP.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 : GNP.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UAD 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005614. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-NOV-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.50 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) : 0.979 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC Q315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40357 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 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 (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04400 REMARK 200 FOR THE DATA SET : 40.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.27400 REMARK 200 FOR SHELL : 3.750 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: PDB ENTRY 1CTQ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, SODIUM ACETATE, PH 5.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 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 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 1/2+X,1/2+Y,1/2+Z REMARK 290 6555 1/2-X,1/2-Y,1/2+Z REMARK 290 7555 1/2-Y,1/2+X,1/2+Z REMARK 290 8555 1/2+Y,1/2-X,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 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.70900 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.70900 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 51.33800 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.70900 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.70900 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 51.33800 REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 58.70900 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 58.70900 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 51.33800 REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 58.70900 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 58.70900 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 51.33800 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, 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 BIOMOLECULE: 2 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 GLN A 9 REMARK 465 ASN A 10 REMARK 465 GLN B 9 REMARK 465 ASN B 10 REMARK 465 MET C 1 REMARK 465 SER C 2 REMARK 465 ARG C 3 REMARK 465 GLU C 96 REMARK 465 LYS C 97 REMARK 465 ILE C 98 REMARK 465 GLY C 99 REMARK 465 MET D 1 REMARK 465 SER D 2 REMARK 465 ARG D 3 REMARK 465 GLU D 96 REMARK 465 LYS D 97 REMARK 465 ILE D 98 REMARK 465 GLY D 99 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 19 SD MET A 19 CE 0.035 REMARK 500 MET B 35 SD MET B 35 CE 0.036 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 TYR A 36 N - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 LYS A 47 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 ASP A 65 N - CA - C ANGL. DEV. = -6.8 DEGREES REMARK 500 LEU A 67 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 ASP A 68 N - CA - C ANGL. DEV. = -7.4 DEGREES REMARK 500 LEU A 90 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 PHE A 93 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 LEU A 124 N - CA - C ANGL. DEV. = -7.0 DEGREES REMARK 500 TYR B 36 N - CA - C ANGL. DEV. = 6.9 DEGREES REMARK 500 LYS B 47 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 LEU B 67 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 ASP B 68 N - CA - C ANGL. DEV. = -6.9 DEGREES REMARK 500 PHE B 93 N - CA - C ANGL. DEV. = -7.5 DEGREES REMARK 500 LEU B 124 N - CA - C ANGL. DEV. = -7.0 DEGREES REMARK 500 ASN B 163 N - CA - C ANGL. DEV. = 7.1 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1C1Y RELATED DB: PDB REMARK 900 RELATED ID: 1HE8 RELATED DB: PDB REMARK 900 RELATED ID: 1K8R RELATED DB: PDB REMARK 900 RELATED ID: 1LFD RELATED DB: PDB DBREF 1UAD A 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 1UAD B 9 183 UNP P11233 RALA_HUMAN 9 183 DBREF 1UAD C 1 99 UNP O54921 SEC5_RAT 1 99 DBREF 1UAD D 1 99 UNP O54921 SEC5_RAT 1 99 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 GLN 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 175 GLN ASN SER LEU ALA LEU HIS LYS VAL ILE MET VAL GLY SEQRES 2 B 175 SER GLY GLY VAL GLY LYS SER ALA LEU THR LEU GLN PHE SEQRES 3 B 175 MET TYR ASP GLU PHE VAL GLU ASP TYR GLU PRO THR LYS SEQRES 4 B 175 ALA ASP SER TYR ARG LYS LYS VAL VAL LEU ASP GLY GLU SEQRES 5 B 175 GLU VAL GLN ILE ASP ILE LEU ASP THR ALA GLY GLN GLU SEQRES 6 B 175 ASP TYR ALA ALA ILE ARG ASP ASN TYR PHE ARG SER GLY SEQRES 7 B 175 GLU GLY PHE LEU CYS VAL PHE SER ILE THR GLU MET GLU SEQRES 8 B 175 SER PHE ALA ALA THR ALA ASP PHE ARG GLU GLN ILE LEU SEQRES 9 B 175 ARG VAL LYS GLU ASP GLU ASN VAL PRO PHE LEU LEU VAL SEQRES 10 B 175 GLY ASN LYS SER ASP LEU GLU ASP LYS ARG GLN VAL SER SEQRES 11 B 175 VAL GLU GLU ALA LYS ASN ARG ALA GLU GLN TRP ASN VAL SEQRES 12 B 175 ASN TYR VAL GLU THR SER ALA LYS THR ARG ALA ASN VAL SEQRES 13 B 175 ASP LYS VAL PHE PHE ASP LEU MET ARG GLU ILE ARG ALA SEQRES 14 B 175 ARG LYS MET GLU ASP SER SEQRES 1 C 99 MET SER ARG SER ARG GLN PRO PRO LEU VAL THR GLY ILE SEQRES 2 C 99 SER PRO ASN GLU GLY ILE PRO TRP THR LYS VAL THR ILE SEQRES 3 C 99 ARG GLY GLU ASN LEU GLY THR GLY PRO THR ASP LEU ILE SEQRES 4 C 99 GLY LEU THR ILE CYS GLY HIS ASN CYS LEU LEU THR ALA SEQRES 5 C 99 GLU TRP MET SER ALA SER LYS ILE VAL CYS ARG VAL GLY SEQRES 6 C 99 GLN ALA LYS ASN ASP LYS GLY ASP ILE ILE VAL THR THR SEQRES 7 C 99 LYS SER GLY GLY ARG GLY THR SER THR VAL SER PHE LYS SEQRES 8 C 99 LEU LEU LYS PRO GLU LYS ILE GLY SEQRES 1 D 99 MET SER ARG SER ARG GLN PRO PRO LEU VAL THR GLY ILE SEQRES 2 D 99 SER PRO ASN GLU GLY ILE PRO TRP THR LYS VAL THR ILE SEQRES 3 D 99 ARG GLY GLU ASN LEU GLY THR GLY PRO THR ASP LEU ILE SEQRES 4 D 99 GLY LEU THR ILE CYS GLY HIS ASN CYS LEU LEU THR ALA SEQRES 5 D 99 GLU TRP MET SER ALA SER LYS ILE VAL CYS ARG VAL GLY SEQRES 6 D 99 GLN ALA LYS ASN ASP LYS GLY ASP ILE ILE VAL THR THR SEQRES 7 D 99 LYS SER GLY GLY ARG GLY THR SER THR VAL SER PHE LYS SEQRES 8 D 99 LEU LEU LYS PRO GLU LYS ILE GLY HET MG A 300 1 HET MG B 300 1 HET GNP A 200 32 HET GNP 1200 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 *222(H2 O) HELIX 1 1 GLY A 26 ASP A 37 1 12 HELIX 2 2 ALA A 76 GLY A 86 1 11 HELIX 3 3 GLU A 97 GLU A 116 1 20 HELIX 4 4 LEU A 131 ARG A 135 5 5 HELIX 5 5 SER A 138 ASN A 150 1 13 HELIX 6 6 ASN A 163 ASP A 182 1 20 HELIX 7 7 GLY B 26 ASP B 37 1 12 HELIX 8 8 ALA B 76 GLY B 86 1 11 HELIX 9 9 GLU B 97 GLU B 116 1 20 HELIX 10 10 LYS B 128 ARG B 135 5 8 HELIX 11 11 SER B 138 ASN B 150 1 13 HELIX 12 12 ASN B 163 MET B 180 1 18 HELIX 13 13 GLY C 34 THR C 36 5 3 HELIX 14 14 LEU C 49 ALA C 52 5 4 HELIX 15 15 GLY D 34 THR D 36 5 3 HELIX 16 16 LEU D 49 ALA D 52 5 4 SHEET 1 A10 ASN A 152 GLU A 155 0 SHEET 2 A10 PHE A 122 ASN A 127 1 N LEU A 124 O ASN A 152 SHEET 3 A10 GLY A 88 SER A 94 1 N CYS A 91 O VAL A 125 SHEET 4 A10 LEU A 14 VAL A 20 1 N VAL A 20 O VAL A 92 SHEET 5 A10 GLU A 60 THR A 69 1 O ASP A 65 N VAL A 17 SHEET 6 A10 ALA A 48 LEU A 57 -1 N TYR A 51 O ILE A 66 SHEET 7 A10 LEU C 9 SER C 14 -1 O ILE C 13 N SER A 50 SHEET 8 A10 LYS C 23 GLU C 29 -1 O THR C 25 N SER C 14 SHEET 9 A10 LYS C 59 ARG C 63 -1 O ILE C 60 N ILE C 26 SHEET 10 A10 GLU C 53 SER C 56 -1 N GLU C 53 O VAL C 61 SHEET 1 B 8 ASN A 152 GLU A 155 0 SHEET 2 B 8 PHE A 122 ASN A 127 1 N LEU A 124 O ASN A 152 SHEET 3 B 8 GLY A 88 SER A 94 1 N CYS A 91 O VAL A 125 SHEET 4 B 8 LEU A 14 VAL A 20 1 N VAL A 20 O VAL A 92 SHEET 5 B 8 GLU A 60 THR A 69 1 O ASP A 65 N VAL A 17 SHEET 6 B 8 ALA A 48 LEU A 57 -1 N TYR A 51 O ILE A 66 SHEET 7 B 8 LEU C 9 SER C 14 -1 O ILE C 13 N SER A 50 SHEET 8 B 8 THR C 85 SER C 86 1 O THR C 85 N VAL C 10 SHEET 1 C10 ASN B 152 GLU B 155 0 SHEET 2 C10 PHE B 122 ASN B 127 1 N LEU B 124 O ASN B 152 SHEET 3 C10 GLY B 88 SER B 94 1 N CYS B 91 O VAL B 125 SHEET 4 C10 LEU B 14 VAL B 20 1 N VAL B 20 O VAL B 92 SHEET 5 C10 GLU B 60 THR B 69 1 O ASP B 65 N VAL B 17 SHEET 6 C10 ALA B 48 LEU B 57 -1 N LEU B 57 O GLU B 60 SHEET 7 C10 LEU D 9 SER D 14 -1 O ILE D 13 N SER B 50 SHEET 8 C10 LYS D 23 GLU D 29 -1 O THR D 25 N SER D 14 SHEET 9 C10 LYS D 59 ARG D 63 -1 O ILE D 60 N ILE D 26 SHEET 10 C10 GLU D 53 SER D 56 -1 N GLU D 53 O VAL D 61 SHEET 1 D 8 ASN B 152 GLU B 155 0 SHEET 2 D 8 PHE B 122 ASN B 127 1 N LEU B 124 O ASN B 152 SHEET 3 D 8 GLY B 88 SER B 94 1 N CYS B 91 O VAL B 125 SHEET 4 D 8 LEU B 14 VAL B 20 1 N VAL B 20 O VAL B 92 SHEET 5 D 8 GLU B 60 THR B 69 1 O ASP B 65 N VAL B 17 SHEET 6 D 8 ALA B 48 LEU B 57 -1 N LEU B 57 O GLU B 60 SHEET 7 D 8 LEU D 9 SER D 14 -1 O ILE D 13 N SER B 50 SHEET 8 D 8 THR D 85 SER D 86 1 O THR D 85 N VAL D 10 SHEET 1 E 2 GLU C 17 GLY C 18 0 SHEET 2 E 2 LYS C 91 LEU C 92 1 O LYS C 91 N GLY C 18 SHEET 1 F 4 HIS C 46 ASN C 47 0 SHEET 2 F 4 LEU C 38 ILE C 43 -1 N ILE C 43 O HIS C 46 SHEET 3 F 4 ILE C 74 THR C 78 -1 O ILE C 75 N THR C 42 SHEET 4 F 4 GLY C 82 ARG C 83 -1 O GLY C 82 N THR C 78 SHEET 1 G 2 GLU D 17 GLY D 18 0 SHEET 2 G 2 LYS D 91 LEU D 92 1 O LYS D 91 N GLY D 18 SHEET 1 H 4 HIS D 46 ASN D 47 0 SHEET 2 H 4 LEU D 38 ILE D 43 -1 N ILE D 43 O HIS D 46 SHEET 3 H 4 ILE D 74 THR D 78 -1 O THR D 77 N GLY D 40 SHEET 4 H 4 GLY D 82 ARG D 83 -1 O GLY D 82 N THR D 78 LINK MG MG A 300 O2B GNP A 200 CISPEP 1 SER C 14 PRO C 15 0 -0.14 CISPEP 2 SER D 14 PRO D 15 0 -0.25 CRYST1 117.418 117.418 102.676 90.00 90.00 90.00 I 4 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 0.008517 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008517 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009739 0.00000