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HEADER APOPTOSIS 09-JUL-04 1WMG TITLE CRYSTAL STRUCTURE OF THE UNC5H2 DEATH DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NETRIN RECEPTOR UNC5H2; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 FRAGMENT: DEATH DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS SIX HELIX BUNDLE, DEATH DOMAIN, APOPTOSIS, STRUCTURAL KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI EXPDTA X-RAY DIFFRACTION AUTHOR N.HANDA,K.MURAYAMA,M.SHIROUZU,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 2 19-DEC-06 1WMG 1 JRNL REVDAT 1 09-JAN-05 1WMG 0 JRNL AUTH N.HANDA,M.KUKIMOTO-NIINO,R.AKASAKA,K.MURAYAMA, JRNL AUTH 2 T.TERADA,M.INOUE,T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA, JRNL AUTH 3 E.NUNOKAWA,A.TANAKA,Y.HAYASHIZAKI,T.KIGAWA, JRNL AUTH 4 M.SHIROUZU,S.YOKOYAMA JRNL TITL STRUCTURE OF THE UNC5H2 DEATH DOMAIN JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 62 1502 2006 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.78 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 824690.650 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 65800 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) : 0.229 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3282 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.30 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9301 REMARK 3 BIN R VALUE (WORKING SET) : 0.3030 REMARK 3 BIN FREE R VALUE : 0.3130 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 495 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4070 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 43 REMARK 3 SOLVENT ATOMS : 185 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 12.14000 REMARK 3 B22 (A**2) : -9.32000 REMARK 3 B33 (A**2) : -2.83000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 9.07000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28 REMARK 3 ESD FROM SIGMAA (A) : 0.30 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) : 0.33 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.50 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) : 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 : 0.40 REMARK 3 BSOL : 59.50 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS REFINED ALSO WITH REMARK 3 ARP/WARP. THE FILE CONTAINS FRIEDEL PAIRS. REMARK 4 REMARK 4 1WMG 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB023742. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-APR-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 : SPRING-8 REMARK 200 BEAMLINE : BL26B1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979006, 0.979363, 0.964000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : JUPITER REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71778 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 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 (%) : 99.6 REMARK 200 DATA REDUNDANCY : 3.590 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06900 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.24100 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: 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: THE FILE CONTAINS FRIEDEL PAIRS. REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MES, MAGNESIUM SULFATE, PH 6.5, REMARK 280 LIQUID DIFFUSION, TEMPERATURE 285K 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 1/2+X,1/2+Y,Z REMARK 290 4555 1/2-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 62.43900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.60350 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 62.43900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.60350 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 6 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, B, C, D, E, F 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH 7 LIES ON A SPECIAL POSITION. 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 847 REMARK 465 SER A 848 REMARK 465 SER A 849 REMARK 465 GLY A 850 REMARK 465 SER A 851 REMARK 465 SER A 852 REMARK 465 GLY A 853 REMARK 465 SER A 944 REMARK 465 GLY A 945 REMARK 465 PRO A 946 REMARK 465 SER A 947 REMARK 465 SER A 948 REMARK 465 GLY A 949 REMARK 465 GLY B 847 REMARK 465 SER B 848 REMARK 465 SER B 849 REMARK 465 GLY B 850 REMARK 465 SER B 851 REMARK 465 SER B 852 REMARK 465 GLY B 853 REMARK 465 TYR B 854 REMARK 465 GLN B 915 REMARK 465 ASP B 916 REMARK 465 ASP B 917 REMARK 465 GLY B 918 REMARK 465 ASP B 942 REMARK 465 GLY B 943 REMARK 465 SER B 944 REMARK 465 GLY B 945 REMARK 465 PRO B 946 REMARK 465 SER B 947 REMARK 465 SER B 948 REMARK 465 GLY B 949 REMARK 465 GLY C 847 REMARK 465 SER C 848 REMARK 465 SER C 849 REMARK 465 GLY C 850 REMARK 465 SER C 851 REMARK 465 SER C 852 REMARK 465 GLY C 853 REMARK 465 ASP C 917 REMARK 465 GLY C 943 REMARK 465 SER C 944 REMARK 465 GLY C 945 REMARK 465 PRO C 946 REMARK 465 SER C 947 REMARK 465 SER C 948 REMARK 465 GLY C 949 REMARK 465 GLY D 847 REMARK 465 SER D 848 REMARK 465 SER D 849 REMARK 465 GLY D 850 REMARK 465 SER D 851 REMARK 465 SER D 852 REMARK 465 GLY D 853 REMARK 465 GLN D 915 REMARK 465 ASP D 916 REMARK 465 ASP D 917 REMARK 465 GLY D 943 REMARK 465 SER D 944 REMARK 465 GLY D 945 REMARK 465 PRO D 946 REMARK 465 SER D 947 REMARK 465 SER D 948 REMARK 465 GLY D 949 REMARK 465 GLY E 847 REMARK 465 SER E 848 REMARK 465 SER E 849 REMARK 465 GLY E 850 REMARK 465 SER E 851 REMARK 465 SER E 852 REMARK 465 GLY E 853 REMARK 465 ASP E 942 REMARK 465 GLY E 943 REMARK 465 SER E 944 REMARK 465 GLY E 945 REMARK 465 PRO E 946 REMARK 465 SER E 947 REMARK 465 SER E 948 REMARK 465 GLY E 949 REMARK 465 GLY F 847 REMARK 465 SER F 848 REMARK 465 SER F 849 REMARK 465 GLY F 850 REMARK 465 SER F 851 REMARK 465 SER F 852 REMARK 465 GLY F 853 REMARK 465 TYR F 854 REMARK 465 ASP F 942 REMARK 465 GLY F 943 REMARK 465 SER F 944 REMARK 465 GLY F 945 REMARK 465 PRO F 946 REMARK 465 SER F 947 REMARK 465 SER F 948 REMARK 465 GLY F 949 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 PRO A 902 CB PRO A 902 CG 0.053 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 PRO A 859 C - N - CA ANGL. DEV. = -7.6 DEGREES REMARK 500 LEU B 870 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 LEU C 860 N - CA - C ANGL. DEV. = 7.5 DEGREES REMARK 500 LEU C 870 N - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 500 GLN C 915 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 ASN C 921 N - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 500 PRO D 859 C - N - CA ANGL. DEV. = -7.5 DEGREES REMARK 500 PRO D 859 C - N - CD ANGL. DEV. = 8.4 DEGREES REMARK 500 LEU D 870 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 ASP D 890 N - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007015810.1 RELATED DB: TARGETDB DBREF 1WMG A 854 943 UNP Q8K1S3 UNC5B_MOUSE 854 943 DBREF 1WMG B 854 943 UNP Q8K1S3 UNC5B_MOUSE 854 943 DBREF 1WMG C 854 943 UNP Q8K1S3 UNC5B_MOUSE 854 943 DBREF 1WMG D 854 943 UNP Q8K1S3 UNC5B_MOUSE 854 943 DBREF 1WMG E 854 943 UNP Q8K1S3 UNC5B_MOUSE 854 943 DBREF 1WMG F 854 943 UNP Q8K1S3 UNC5B_MOUSE 854 943 SEQADV 1WMG GLY A 847 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER A 848 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER A 849 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY A 850 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER A 851 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER A 852 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY A 853 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG MSE A 889 UNP Q8K1S3 MET 889 MODIFIED RESIDUE SEQADV 1WMG MSE A 930 UNP Q8K1S3 MET 930 MODIFIED RESIDUE SEQADV 1WMG MSE A 935 UNP Q8K1S3 MET 935 MODIFIED RESIDUE SEQADV 1WMG MSE A 939 UNP Q8K1S3 MET 939 MODIFIED RESIDUE SEQADV 1WMG SER A 944 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY A 945 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG PRO A 946 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER A 947 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER A 948 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY A 949 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY B 847 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER B 848 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER B 849 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY B 850 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER B 851 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER B 852 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY B 853 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG MSE B 889 UNP Q8K1S3 MET 889 MODIFIED RESIDUE SEQADV 1WMG MSE B 930 UNP Q8K1S3 MET 930 MODIFIED RESIDUE SEQADV 1WMG MSE B 935 UNP Q8K1S3 MET 935 MODIFIED RESIDUE SEQADV 1WMG MSE B 939 UNP Q8K1S3 MET 939 MODIFIED RESIDUE SEQADV 1WMG SER B 944 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY B 945 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG PRO B 946 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER B 947 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER B 948 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY B 949 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY C 847 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER C 848 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER C 849 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY C 850 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER C 851 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER C 852 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY C 853 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG MSE C 889 UNP Q8K1S3 MET 889 MODIFIED RESIDUE SEQADV 1WMG MSE C 930 UNP Q8K1S3 MET 930 MODIFIED RESIDUE SEQADV 1WMG MSE C 935 UNP Q8K1S3 MET 935 MODIFIED RESIDUE SEQADV 1WMG MSE C 939 UNP Q8K1S3 MET 939 MODIFIED RESIDUE SEQADV 1WMG SER C 944 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY C 945 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG PRO C 946 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER C 947 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER C 948 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY C 949 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY D 847 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER D 848 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER D 849 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY D 850 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER D 851 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER D 852 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY D 853 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG MSE D 889 UNP Q8K1S3 MET 889 MODIFIED RESIDUE SEQADV 1WMG MSE D 930 UNP Q8K1S3 MET 930 MODIFIED RESIDUE SEQADV 1WMG MSE D 935 UNP Q8K1S3 MET 935 MODIFIED RESIDUE SEQADV 1WMG MSE D 939 UNP Q8K1S3 MET 939 MODIFIED RESIDUE SEQADV 1WMG SER D 944 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY D 945 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG PRO D 946 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER D 947 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER D 948 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY D 949 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY E 847 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER E 848 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER E 849 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY E 850 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER E 851 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER E 852 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY E 853 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG MSE E 889 UNP Q8K1S3 MET 889 MODIFIED RESIDUE SEQADV 1WMG MSE E 930 UNP Q8K1S3 MET 930 MODIFIED RESIDUE SEQADV 1WMG MSE E 935 UNP Q8K1S3 MET 935 MODIFIED RESIDUE SEQADV 1WMG MSE E 939 UNP Q8K1S3 MET 939 MODIFIED RESIDUE SEQADV 1WMG SER E 944 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY E 945 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG PRO E 946 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER E 947 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER E 948 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY E 949 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY F 847 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER F 848 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER F 849 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY F 850 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER F 851 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER F 852 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY F 853 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG MSE F 889 UNP Q8K1S3 MET 889 MODIFIED RESIDUE SEQADV 1WMG MSE F 930 UNP Q8K1S3 MET 930 MODIFIED RESIDUE SEQADV 1WMG MSE F 935 UNP Q8K1S3 MET 935 MODIFIED RESIDUE SEQADV 1WMG MSE F 939 UNP Q8K1S3 MET 939 MODIFIED RESIDUE SEQADV 1WMG SER F 944 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY F 945 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG PRO F 946 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER F 947 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG SER F 948 UNP Q8K1S3 CLONING ARTIFACT SEQADV 1WMG GLY F 949 UNP Q8K1S3 CLONING ARTIFACT SEQRES 1 A 103 GLY SER SER GLY SER SER GLY TYR ALA PHE LYS ILE PRO SEQRES 2 A 103 LEU SER ILE ARG GLN LYS ILE CYS SER SER LEU ASP ALA SEQRES 3 A 103 PRO ASN SER ARG GLY ASN ASP TRP ARG LEU LEU ALA GLN SEQRES 4 A 103 LYS LEU SER MSE ASP ARG TYR LEU ASN TYR PHE ALA THR SEQRES 5 A 103 LYS ALA SER PRO THR GLY VAL ILE LEU ASP LEU TRP GLU SEQRES 6 A 103 ALA ARG GLN GLN ASP ASP GLY ASP LEU ASN SER LEU ALA SEQRES 7 A 103 SER ALA LEU GLU GLU MSE GLY LYS SER GLU MSE LEU VAL SEQRES 8 A 103 ALA MSE ALA THR ASP GLY SER GLY PRO SER SER GLY SEQRES 1 B 103 GLY SER SER GLY SER SER GLY TYR ALA PHE LYS ILE PRO SEQRES 2 B 103 LEU SER ILE ARG GLN LYS ILE CYS SER SER LEU ASP ALA SEQRES 3 B 103 PRO ASN SER ARG GLY ASN ASP TRP ARG LEU LEU ALA GLN SEQRES 4 B 103 LYS LEU SER MSE ASP ARG TYR LEU ASN TYR PHE ALA THR SEQRES 5 B 103 LYS ALA SER PRO THR GLY VAL ILE LEU ASP LEU TRP GLU SEQRES 6 B 103 ALA ARG GLN GLN ASP ASP GLY ASP LEU ASN SER LEU ALA SEQRES 7 B 103 SER ALA LEU GLU GLU MSE GLY LYS SER GLU MSE LEU VAL SEQRES 8 B 103 ALA MSE ALA THR ASP GLY SER GLY PRO SER SER GLY SEQRES 1 C 103 GLY SER SER GLY SER SER GLY TYR ALA PHE LYS ILE PRO SEQRES 2 C 103 LEU SER ILE ARG GLN LYS ILE CYS SER SER LEU ASP ALA SEQRES 3 C 103 PRO ASN SER ARG GLY ASN ASP TRP ARG LEU LEU ALA GLN SEQRES 4 C 103 LYS LEU SER MSE ASP ARG TYR LEU ASN TYR PHE ALA THR SEQRES 5 C 103 LYS ALA SER PRO THR GLY VAL ILE LEU ASP LEU TRP GLU SEQRES 6 C 103 ALA ARG GLN GLN ASP ASP GLY ASP LEU ASN SER LEU ALA SEQRES 7 C 103 SER ALA LEU GLU GLU MSE GLY LYS SER GLU MSE LEU VAL SEQRES 8 C 103 ALA MSE ALA THR ASP GLY SER GLY PRO SER SER GLY SEQRES 1 D 103 GLY SER SER GLY SER SER GLY TYR ALA PHE LYS ILE PRO SEQRES 2 D 103 LEU SER ILE ARG GLN LYS ILE CYS SER SER LEU ASP ALA SEQRES 3 D 103 PRO ASN SER ARG GLY ASN ASP TRP ARG LEU LEU ALA GLN SEQRES 4 D 103 LYS LEU SER MSE ASP ARG TYR LEU ASN TYR PHE ALA THR SEQRES 5 D 103 LYS ALA SER PRO THR GLY VAL ILE LEU ASP LEU TRP GLU SEQRES 6 D 103 ALA ARG GLN GLN ASP ASP GLY ASP LEU ASN SER LEU ALA SEQRES 7 D 103 SER ALA LEU GLU GLU MSE GLY LYS SER GLU MSE LEU VAL SEQRES 8 D 103 ALA MSE ALA THR ASP GLY SER GLY PRO SER SER GLY SEQRES 1 E 103 GLY SER SER GLY SER SER GLY TYR ALA PHE LYS ILE PRO SEQRES 2 E 103 LEU SER ILE ARG GLN LYS ILE CYS SER SER LEU ASP ALA SEQRES 3 E 103 PRO ASN SER ARG GLY ASN ASP TRP ARG LEU LEU ALA GLN SEQRES 4 E 103 LYS LEU SER MSE ASP ARG TYR LEU ASN TYR PHE ALA THR SEQRES 5 E 103 LYS ALA SER PRO THR GLY VAL ILE LEU ASP LEU TRP GLU SEQRES 6 E 103 ALA ARG GLN GLN ASP ASP GLY ASP LEU ASN SER LEU ALA SEQRES 7 E 103 SER ALA LEU GLU GLU MSE GLY LYS SER GLU MSE LEU VAL SEQRES 8 E 103 ALA MSE ALA THR ASP GLY SER GLY PRO SER SER GLY SEQRES 1 F 103 GLY SER SER GLY SER SER GLY TYR ALA PHE LYS ILE PRO SEQRES 2 F 103 LEU SER ILE ARG GLN LYS ILE CYS SER SER LEU ASP ALA SEQRES 3 F 103 PRO ASN SER ARG GLY ASN ASP TRP ARG LEU LEU ALA GLN SEQRES 4 F 103 LYS LEU SER MSE ASP ARG TYR LEU ASN TYR PHE ALA THR SEQRES 5 F 103 LYS ALA SER PRO THR GLY VAL ILE LEU ASP LEU TRP GLU SEQRES 6 F 103 ALA ARG GLN GLN ASP ASP GLY ASP LEU ASN SER LEU ALA SEQRES 7 F 103 SER ALA LEU GLU GLU MSE GLY LYS SER GLU MSE LEU VAL SEQRES 8 F 103 ALA MSE ALA THR ASP GLY SER GLY PRO SER SER GLY MODRES 1WMG MSE A 889 MET SELENOMETHIONINE MODRES 1WMG MSE A 930 MET SELENOMETHIONINE MODRES 1WMG MSE A 935 MET SELENOMETHIONINE MODRES 1WMG MSE A 939 MET SELENOMETHIONINE MODRES 1WMG MSE B 889 MET SELENOMETHIONINE MODRES 1WMG MSE B 930 MET SELENOMETHIONINE MODRES 1WMG MSE B 935 MET SELENOMETHIONINE MODRES 1WMG MSE B 939 MET SELENOMETHIONINE MODRES 1WMG MSE C 889 MET SELENOMETHIONINE MODRES 1WMG MSE C 930 MET SELENOMETHIONINE MODRES 1WMG MSE C 935 MET SELENOMETHIONINE MODRES 1WMG MSE C 939 MET SELENOMETHIONINE MODRES 1WMG MSE D 889 MET SELENOMETHIONINE MODRES 1WMG MSE D 930 MET SELENOMETHIONINE MODRES 1WMG MSE D 935 MET SELENOMETHIONINE MODRES 1WMG MSE D 939 MET SELENOMETHIONINE MODRES 1WMG MSE E 889 MET SELENOMETHIONINE MODRES 1WMG MSE E 930 MET SELENOMETHIONINE MODRES 1WMG MSE E 935 MET SELENOMETHIONINE MODRES 1WMG MSE E 939 MET SELENOMETHIONINE MODRES 1WMG MSE F 889 MET SELENOMETHIONINE MODRES 1WMG MSE F 930 MET SELENOMETHIONINE MODRES 1WMG MSE F 935 MET SELENOMETHIONINE MODRES 1WMG MSE F 939 MET SELENOMETHIONINE HET MSE A 889 8 HET MSE A 930 8 HET MSE A 935 8 HET MSE A 939 8 HET MSE B 889 8 HET MSE B 930 8 HET MSE B 935 8 HET MSE B 939 8 HET MSE C 889 8 HET MSE C 930 8 HET MSE C 935 8 HET MSE C 939 8 HET MSE D 889 8 HET MSE D 930 8 HET MSE D 935 8 HET MSE D 939 8 HET MSE E 889 8 HET MSE E 930 8 HET MSE E 935 8 HET MSE E 939 8 HET MSE F 889 8 HET MSE F 930 8 HET MSE F 935 8 HET MSE F 939 8 HET SO3 1001 4 HET SO3 1002 4 HET SO3 1003 4 HET SO3 1004 4 HET SO3 1005 4 HET SO3 1006 4 HET SO3 1007 4 HET SO4 2001 5 HET SO4 2002 5 HET SO4 2003 5 HETNAM MSE SELENOMETHIONINE HETNAM SO3 SULFITE ION HETNAM SO4 SULFATE ION FORMUL 1 MSE 24(C5 H11 N O2 SE) FORMUL 7 SO3 7(O3 S 2-) FORMUL 14 SO4 3(O4 S 2-) FORMUL 17 HOH *185(H2 O) HELIX 1 1 PRO A 859 ALA A 872 1 14 HELIX 2 2 PRO A 873 ARG A 876 5 4 HELIX 3 3 ASP A 879 LEU A 887 1 9 HELIX 4 4 MSE A 889 ARG A 891 5 3 HELIX 5 5 TYR A 892 THR A 898 1 7 HELIX 6 6 SER A 901 GLN A 914 1 14 HELIX 7 7 ASP A 919 MSE A 930 1 12 HELIX 8 8 LYS A 932 ASP A 942 1 11 HELIX 9 9 PRO B 859 ALA B 872 1 14 HELIX 10 10 PRO B 873 ARG B 876 5 4 HELIX 11 11 ASP B 879 LEU B 887 1 9 HELIX 12 12 MSE B 889 ARG B 891 5 3 HELIX 13 13 TYR B 892 ALA B 897 1 6 HELIX 14 14 SER B 901 ARG B 913 1 13 HELIX 15 15 ASP B 919 MSE B 930 1 12 HELIX 16 16 LYS B 932 THR B 941 1 10 HELIX 17 17 PRO C 859 ALA C 872 1 14 HELIX 18 18 ASP C 879 LEU C 887 1 9 HELIX 19 19 MSE C 889 ARG C 891 5 3 HELIX 20 20 TYR C 892 ALA C 897 1 6 HELIX 21 21 SER C 901 ARG C 913 1 13 HELIX 22 22 LEU C 920 MSE C 930 1 11 HELIX 23 23 LYS C 932 ASP C 942 1 11 HELIX 24 24 PRO D 859 ALA D 872 1 14 HELIX 25 25 ASP D 879 LEU D 887 1 9 HELIX 26 26 MSE D 889 ARG D 891 5 3 HELIX 27 27 TYR D 892 THR D 898 1 7 HELIX 28 28 SER D 901 ARG D 913 1 13 HELIX 29 29 LEU D 920 MSE D 930 1 11 HELIX 30 30 LYS D 932 ASP D 942 1 11 HELIX 31 31 PRO E 859 ALA E 872 1 14 HELIX 32 32 ASP E 879 LEU E 887 1 9 HELIX 33 33 MSE E 889 ARG E 891 5 3 HELIX 34 34 TYR E 892 ALA E 897 1 6 HELIX 35 35 SER E 901 ARG E 913 1 13 HELIX 36 36 LEU E 920 MSE E 930 1 11 HELIX 37 37 LYS E 932 THR E 941 1 10 HELIX 38 38 PRO F 859 ASP F 871 1 13 HELIX 39 39 ASP F 879 LEU F 887 1 9 HELIX 40 40 MSE F 889 ARG F 891 5 3 HELIX 41 41 TYR F 892 ALA F 897 1 6 HELIX 42 42 SER F 901 GLN F 914 1 14 HELIX 43 43 LEU F 920 MSE F 930 1 11 HELIX 44 44 GLU F 934 MSE F 939 1 6 CRYST1 124.878 47.207 121.177 90.00 119.56 90.00 C 1 2 1 24 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 0.008008 0.000000 0.004542 0.00000 SCALE2 0.000000 0.021183 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009487 0.00000