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HEADER OXIDOREDUCTASES(ACTING ON CH-NH2 DONOR) 10-JAN-00 1DXM TITLE REDUCED FORM OF THE H PROTEIN FROM GLYCINE DECARBOXYLASE TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: H PROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: GLYCINE CLEAVAGE SYSTEM H PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PISUM SATIVUM; SOURCE 3 ORGANISM_COMMON: GARDEN PEA; SOURCE 4 ORGAN: LEAF; SOURCE 5 ORGANELLE: MITOCHONDRIA; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-HM KEYWDS GLYCINE DECARBOXYLASE, MITOCHONDRIA, EXPDTA X-RAY DIFFRACTION AUTHOR M.FAURE,C.COHEN-ADDAD,M.NEUBURGER,R.DOUCE REVDAT 2 01-APR-03 1DXM 1 JRNL REVDAT 1 04-JUL-00 1DXM 0 JRNL AUTH M.FAURE,J.BOURGUIGNON,M.NEUBURGER,D.MACHEREL, JRNL AUTH 2 L.SIEKER,R.OBER,R.KAHN,C.COHEN-ADDAD,R.DOUCE JRNL TITL INTERACTION BETWEEN THE LIPOAMIDE-CONTAINING JRNL TITL 2 H-PROTEIN AND THE LIPOAMIDE DEHYDROGENASE JRNL TITL 3 (L-PROTEIN) OF THE GLYCINE DECARBOXYLASE JRNL TITL 4 MULTIENZYME SYSTEM 2. CRYSTAL STRUCTURES OF H- AND JRNL TITL 5 L-PROTEINS. JRNL REF EUR.J.BIOCHEM. V. 267 2890 2000 JRNL REFN ASTM EJBCAI IX ISSN 0014-2956 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.COHEN-ADDAD,M.FAURE,M.NEUBURGER,R.OBER,L.SIEKER, REMARK 1 AUTH 2 J.BOURGUIGNON,D.MACHEREL,R.DOUCE REMARK 1 TITL STRUCTURAL STUDIES OF THE GLYCINE DECARBOXYLASE REMARK 1 TITL 2 COMPLEX FROM PEA LEAF MITOCHONDRIA REMARK 1 REF BIOCHIMIE V. 79 637 1997 REMARK 1 REFN ASTM BICMBE FR ISSN 0300-9084 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.COHEN-ADDAD,S.PARES,L.SIEKER,M.NEUBURGER,R.DOUCE REMARK 1 TITL THE LIPOAMIDE ARM IN THE GLYCINE DECARBOXYLASE IS REMARK 1 TITL 2 NOT FREELY SWINGING REMARK 1 REF NAT.STRUCT.BIOL. V. 2 63 1995 REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REFERENCE 3 REMARK 1 AUTH S.PARES,C.COHEN-ADDAD,L.SIEKER,M.NEUBURGER,R.DOUCE REMARK 1 TITL REFINED STRUCTURES AT 2 AND 2.2 A RESOLUTION OF REMARK 1 TITL 2 TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING REMARK 1 TITL 3 PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. D51 1041 1995 REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.5 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.8 REMARK 3 NUMBER OF REFLECTIONS : 7740 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) : 0.204 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT : 410 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.013 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) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1217 REMARK 3 BIN R VALUE (WORKING SET) : 0.2830 REMARK 3 BIN FREE R VALUE : 0.3600 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 60 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.046 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1948 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 40 REMARK 3 SOLVENT ATOMS : 151 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 47.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.41000 REMARK 3 B22 (A**2) : 3.41000 REMARK 3 B33 (A**2) : -6.82000 REMARK 3 B12 (A**2) : -2.07000 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) : 0.30 REMARK 3 ESD FROM SIGMAA (A) : 0.38 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) : 0.43 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.63 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.17 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) : 1.430 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.440 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.980 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.090 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.36 REMARK 3 BSOL : 48.00 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 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED REMARK 4 REMARK 4 1DXM 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 3.102 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-2184 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-DEC-1998 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.20 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7808 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11000 REMARK 200 FOR THE DATA SET : 4.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.24000 REMARK 200 FOR SHELL : 3.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMEN REMARK 200 SOFTWARE USED: CNS 0.5 REMARK 200 STARTING MODEL: 1HPC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.2 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 45.05667 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 90.11333 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 90.11333 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 45.05667 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, Y, Z 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 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. = 8.6 DEGREES REMARK 500 HIS A 13 N - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 ALA A 64 N - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 500 LYS A 104 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 HIS B 13 N - CA - C ANGL. DEV. = 8.4 DEGREES REMARK 500 LYS B 63 CD - CE - NZ ANGL. DEV. = -9.6 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 Z 15 DISTANCE = 5.58 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: LP1 REMARK 800 SITE_DESCRIPTION: LIPOATE COFACTOR OF PROTEIN COVALENTLY BOUND REMARK 800 TO LYSINE 63 CHAIN A REMARK 800 SITE_IDENTIFIER: LP2 REMARK 800 SITE_DESCRIPTION: LIPOATE COFACTOR OF PROTEIN COVALENTLY BOUND REMARK 800 TO LYSINE 63 CHAIN B DBREF 1DXM A 1 131 UNP P16048 GCSH_PEA 35 165 DBREF 1DXM 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 MODRES 1DXM LYS A 63 LYS DIHYDROLIPOATE SITE MODRES 1DXM LYS B 63 LYS DIHYDROLIPOATE SITE HET RED A 163 11 HET RED B 163 11 HETNAM RED DIHYDROLIPOIC ACID FORMUL 3 RED 2(C8 H16 O2 S2) FORMUL 5 HOH *145(H2 O) HELIX 1 1 THR A 28 GLY A 36 1 9 HELIX 2 2 THR A 81 LYS A 86 1 6 HELIX 3 3 GLY A 88 SER A 93 1 6 HELIX 4 4 SER A 107 SER A 113 5 7 HELIX 5 5 GLY A 116 ALA A 130 1 15 HELIX 6 6 THR B 28 GLY B 36 1 9 HELIX 7 7 THR B 81 THR B 84 5 4 HELIX 8 8 GLY B 88 SER B 93 1 6 HELIX 9 9 SER B 107 SER B 113 5 7 HELIX 10 10 GLY B 116 ALA B 129 1 14 SHEET 1 AA 4 GLU A 14 GLU A 19 0 SHEET 2 AA 4 VAL A 22 ILE A 27 -1 N GLY A 26 O TRP A 15 SHEET 3 AA 4 ILE A 101 PRO A 105 -1 N ILE A 103 O ALA A 23 SHEET 4 AA 4 GLY A 74 VAL A 79 -1 N GLU A 78 O LYS A 102 SHEET 1 AB 3 VAL A 38 GLU A 42 0 SHEET 2 AB 3 GLY A 55 SER A 61 -1 N GLU A 60 O VAL A 39 SHEET 3 AB 3 THR A 65 ASN A 69 -1 N VAL A 68 O PHE A 56 SHEET 1 BA 5 LYS B 8 ALA B 10 0 SHEET 2 BA 5 GLU B 14 GLU B 19 -1 N VAL B 16 O LYS B 8 SHEET 3 BA 5 VAL B 22 ILE B 27 -1 N GLY B 26 O TRP B 15 SHEET 4 BA 5 ILE B 101 PRO B 105 -1 N ILE B 103 O ALA B 23 SHEET 5 BA 5 GLY B 74 VAL B 79 -1 N GLU B 78 O LYS B 102 SHEET 1 BB 3 VAL B 38 GLU B 42 0 SHEET 2 BB 3 GLY B 55 SER B 61 -1 N GLU B 60 O VAL B 39 SHEET 3 BB 3 THR B 65 ASN B 69 -1 N VAL B 68 O PHE B 56 LINK NZ LYS A 63 C1 RED A 163 LINK NZ LYS B 63 C1 RED B 163 SITE 1 LP1 2 RED A 163 LYS A 63 SITE 1 LP2 2 RED B 163 LYS B 63 CRYST1 56.410 56.410 135.170 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 0.017727 0.010235 0.000000 0.00000 SCALE2 0.000000 0.020470 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007398 0.00000 MTRIX1 1 0.394430 0.547610 0.737940 -0.16918 1 MTRIX2 1 0.913690 -0.319300 -0.251430 -0.57433 1 MTRIX3 1 0.097940 0.773420 -0.626290 0.15324 1