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HEADER TRANSIT PEPTIDE 17-FEB-94 1HPC TITLE REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TITLE 2 TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN TITLE 3 OF THE GLYCINE DECARBOXYLASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: H PROTEIN OF THE GLYCINE CLEAVAGE SYSTEM; COMPND 3 CHAIN: A, B; COMPND 4 EC: 1.4.4.2; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PISUM SATIVUM KEYWDS TRANSIT PEPTIDE EXPDTA X-RAY DIFFRACTION AUTHOR S.PARES,C.COHEN-ADDAD,L.SIEKER,M.NEUBURGER,R.DOUCE REVDAT 1 08-MAY-95 1HPC 0 JRNL AUTH S.PARES,C.COHEN-ADDAD,L.C.SIEKER,M.NEUBURGER, JRNL AUTH 2 R.DOUCE JRNL TITL REFINED STRUCTURES AT 2 AND 2.2 A RESOLUTION OF JRNL TITL 2 TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING JRNL TITL 3 PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 51 1041 1995 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.COHEN-ADDAD,S.PARES,L.SIEKER,M.NEUBURGER,R.DOUCE REMARK 1 TITL THE LIPOAMIDE ARM IN THE GLYCINE DECARBOXYLASE REMARK 1 TITL 2 COMPLEX IS NOT FREELY SWINGING REMARK 1 REF NAT.STRUCT.BIOL. V. 2 1 1995 REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.PARES,C.COHEN-ADDAD,L.SIEKER,M.NEUBURGER,R.DOUCE REMARK 1 TITL X-RAY STRUCTURE DETERMINATION AT 2.6 ANGSTROMS REMARK 1 TITL 2 RESOLUTION OF A LIPOATE-CONTAINING PROTEIN: THE REMARK 1 TITL 3 H-PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX REMARK 1 TITL 4 FROM PEA LEAVES REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 4850 1994 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REFERENCE 3 REMARK 1 AUTH L.SIEKER,C.COHEN-ADDAD,M.NEUBURGER,R.DOUCE REMARK 1 TITL CRYSTALLOGRAPHIC DATA FOR H-PROTEIN FROM THE REMARK 1 TITL 2 GLYCINE DECARBOXYLASE COMPLEX REMARK 1 REF J.MOL.BIOL. V. 220 223 1991 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 4 REMARK 1 AUTH D.MACHEREL,M.LEBRUN,J.GAGNON,M.NEUBURGER,R.DOUCE REMARK 1 TITL CDNA CLONING, PRIMARY STRUCTURE AND GENE REMARK 1 TITL 2 EXPRESSION FOR H-PROTEIN, A COMPONENT OF THE REMARK 1 TITL 3 GLYCINE-CLEAVAGE SYSTEM (GLYCINE DECARBOXYLASE) OF REMARK 1 TITL 4 PEA (PISUM SATIVUM) LEAF MITOCHONDRIA REMARK 1 REF BIOCHEM.J. V. 268 783 1990 REMARK 1 REFN ASTM BIJOAK UK ISSN 0306-3275 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 16839 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2344 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 22 REMARK 3 SOLVENT ATOMS : 206 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.011 REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL 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 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: NULL REMARK 4 REMARK 4 1HPC 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 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17031 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL 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) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 -X+Y,-X,2/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,2/3-Z REMARK 290 6555 -X,-X+Y,1/3-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.60000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.20000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.20000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.60000 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 2 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 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 96 LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 NZ LYS B 63 O1 LPA B 63 2.18 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 ASN B 91 CG ASN B 91 OD1 0.095 REMARK 500 ASN B 91 CG ASN B 91 ND2 -0.099 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 ASP A 5 N - CA - C ANGL. DEV. = 16.9 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 120 DISTANCE = 10.75 ANGSTROMS REMARK 525 HOH 150 DISTANCE = 5.42 ANGSTROMS REMARK 525 HOH 173 DISTANCE = 5.34 ANGSTROMS REMARK 525 HOH 195 DISTANCE = 5.04 ANGSTROMS DBREF 1HPC A 1 131 UNP P16048 GCSH_PEA 35 165 DBREF 1HPC B 1 131 UNP P16048 GCSH_PEA 35 165 SEQRES 1 A 131 SER ASN VAL LEU ASP GLY LEU LYS TYR ALA PRO SER HIS SEQRES 2 A 131 GLU TRP VAL LYS HIS GLU GLY SER VAL ALA THR ILE GLY SEQRES 3 A 131 ILE THR ASP HIS ALA GLN ASP HIS LEU GLY GLU VAL VAL SEQRES 4 A 131 PHE VAL GLU LEU PRO GLU PRO GLY VAL SER VAL THR LYS SEQRES 5 A 131 GLY LYS GLY PHE GLY ALA VAL GLU SER VAL LYS ALA THR SEQRES 6 A 131 SER ASP VAL ASN SER PRO ILE SER GLY GLU VAL ILE GLU SEQRES 7 A 131 VAL ASN THR GLY LEU THR GLY LYS PRO GLY LEU ILE ASN SEQRES 8 A 131 SER SER PRO TYR GLU ASP GLY TRP MET ILE LYS ILE LYS SEQRES 9 A 131 PRO THR SER PRO ASP GLU LEU GLU SER LEU LEU GLY ALA SEQRES 10 A 131 LYS GLU TYR THR LYS PHE CYS GLU GLU GLU ASP ALA ALA SEQRES 11 A 131 HIS SEQRES 1 B 131 SER ASN VAL LEU ASP GLY LEU LYS TYR ALA PRO SER HIS SEQRES 2 B 131 GLU TRP VAL LYS HIS GLU GLY SER VAL ALA THR ILE GLY SEQRES 3 B 131 ILE THR ASP HIS ALA GLN ASP HIS LEU GLY GLU VAL VAL SEQRES 4 B 131 PHE VAL GLU LEU PRO GLU PRO GLY VAL SER VAL THR LYS SEQRES 5 B 131 GLY LYS GLY PHE GLY ALA VAL GLU SER VAL LYS ALA THR SEQRES 6 B 131 SER ASP VAL ASN SER PRO ILE SER GLY GLU VAL ILE GLU SEQRES 7 B 131 VAL ASN THR GLY LEU THR GLY LYS PRO GLY LEU ILE ASN SEQRES 8 B 131 SER SER PRO TYR GLU ASP GLY TRP MET ILE LYS ILE LYS SEQRES 9 B 131 PRO THR SER PRO ASP GLU LEU GLU SER LEU LEU GLY ALA SEQRES 10 B 131 LYS GLU TYR THR LYS PHE CYS GLU GLU GLU ASP ALA ALA SEQRES 11 B 131 HIS HET LPA A 63 11 HET LPA B 63 11 HETNAM LPA LIPOIC ACID FORMUL 3 LPA 2(C8 H14 O2 S2) FORMUL 5 HOH *206(H2 O) HELIX 1 H1A SER A 12 ASP A 29 1 18 HELIX 2 H2A GLU A 119 ASP A 128 1 10 HELIX 3 H1B SER B 12 ASP B 29 1 18 HELIX 4 H2B GLU B 119 ASP B 128 1 10 SHEET 1 AA 4 HIS A 13 GLU A 19 0 SHEET 2 AA 4 VAL A 22 THR A 28 -1 SHEET 3 AA 4 GLY A 74 ASN A 80 -1 SHEET 4 AA 4 ILE A 101 PRO A 105 -1 SHEET 1 AB 3 GLU A 37 LEU A 43 0 SHEET 2 AB 3 GLY A 55 SER A 61 -1 SHEET 3 AB 3 THR A 65 SER A 70 -1 SHEET 1 BA 4 HIS B 13 GLU B 19 0 SHEET 2 BA 4 VAL B 22 THR B 28 -1 SHEET 3 BA 4 GLY B 74 ASN B 80 -1 SHEET 4 BA 4 ILE B 101 PRO B 105 -1 SHEET 1 BB 3 GLU B 37 LEU B 43 0 SHEET 2 BB 3 GLY B 55 SER B 61 -1 SHEET 3 BB 3 THR B 65 SER B 70 -1 LINK NZ LYS A 63 C1 LPA A 63 LINK NZ LYS B 63 C1 LPA B 63 SITE 1 LPA 1 LYS A 63 SITE 1 LPB 1 LYS B 63 CRYST1 57.300 57.300 136.800 90.00 90.00 120.00 P 31 2 1 12 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 0.017452 0.010076 0.000000 0.00000 SCALE2 0.000000 0.020152 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007310 0.00000 MTRIX1 1 0.389500 0.566000 0.726000 7.29000 1 MTRIX2 1 0.913800 -0.300000 -0.250000 -28.70000 1 MTRIX3 1 0.071400 0.767000 -0.637000 22.17000 1