HEADER LYASE 15-OCT-05 2C45
TITLE NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE 1-DECARBOXYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: ASPARTATE ALPHA-DECARBOXYLASE;
COMPND 5 EC: 4.1.1.11;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: PAND, RV3601C, MTCY07H7B.21;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DOUBLE-PSI BETA BARREL, LYASE, CARBOXYLASE, ZYMOGEN, PANTOTHENATE
KEYWDS 2 BIOSYNTHESIS, DECARBOXYLASE, PYRUVATE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.GOPALAN,S.CHOPRA,A.RANGANATHAN,K.SWAMINATHAN
REVDAT 6 13-DEC-23 2C45 1 REMARK
REVDAT 5 08-MAY-19 2C45 1 REMARK
REVDAT 4 12-DEC-18 2C45 1 COMPND SOURCE JRNL DBREF
REVDAT 3 24-JAN-18 2C45 1 JRNL
REVDAT 2 24-FEB-09 2C45 1 VERSN
REVDAT 1 06-MAR-07 2C45 0
JRNL AUTH G.GOPALAN,S.CHOPRA,A.RANGANATHAN,K.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF UNCLEAVED
JRNL TITL 2 L-ASPARTATE-ALPHA-DECARBOXYLASE FROM MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS.
JRNL REF PROTEINS V. 65 796 2006
JRNL REFN ESSN 1097-0134
JRNL PMID 17001646
JRNL DOI 10.1002/PROT.21126
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.ALBERT,V.DHANARAJ,U.GENSCHEL,G.KHAN,M.K.RAMJEE,R.PULIDO,
REMARK 1 AUTH 2 B.L.SIBANDA,F.VON DELFT,M.WITTY,T.L.BLUNDELL,A.G.SMITH,
REMARK 1 AUTH 3 C.ABELL
REMARK 1 TITL CRYSTAL STRUCTURE OF ASPARTATE DECARBOXYLASE AT 2.2A
REMARK 1 TITL 2 RESOLUTION PROVIDES EVIDENCE FOR AN ESTER IN PROTEIN
REMARK 1 TITL 3 SELF-PROCESSING
REMARK 1 REF NAT.STRUCT.BIOL. V. 5 289 1998
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 9546220
REMARK 1 DOI 10.1038/NSB0498-289
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.SCHMITZBERGER,M.L.KILKENNY,C.M.LOBLEY,M.E.WEBB,M.VINKOVIC,
REMARK 1 AUTH 2 D.MATAK-VINKOVIC,M.WITTY,D.Y.CHIRGADZE,A.G.SMITH,C.ABELL,
REMARK 1 AUTH 3 T.L.BLUNDELL
REMARK 1 TITL STRUCTURAL CONSTRAINTS ON PROTEIN SELF-PROCESSING IN
REMARK 1 TITL 2 L-ASPARTATE-ALPHA-DECARBOXYLASE
REMARK 1 REF EMBO J. V. 22 6193 2003
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 14633979
REMARK 1 DOI 10.1093/EMBOJ/CDG575
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.I.LEE,S.W.SUH
REMARK 1 TITL CRYSTAL STRUCTURE OF THE SCHIFF BASE INTERMEDIATE PRIOR TO
REMARK 1 TITL 2 DECARBOXYLATION IN THE CATALYTIC CYCLE OF ASPARTATE
REMARK 1 TITL 3 ALPHA-DECARBOXYLASE
REMARK 1 REF J.MOL.BIOL. V. 340 1 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 15184017
REMARK 1 DOI 10.1016/J.JMB.2004.04.049
REMARK 2
REMARK 2 RESOLUTION. 2.99 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) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 105724.320
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.3
REMARK 3 NUMBER OF REFLECTIONS : 22764
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) : 0.265
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1959
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.12
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 36.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1202
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 118
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.035
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6832
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 1.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.31000
REMARK 3 B22 (A**2) : 2.31000
REMARK 3 B33 (A**2) : -4.62000
REMARK 3 B12 (A**2) : 6.82000
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) : 0.59
REMARK 3 ESD FROM SIGMAA (A) : 0.75
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) : 0.66
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.66
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
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 : 0.39
REMARK 3 BSOL : 49.93
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THERE ARE EIGHT MOLECULES IN THE
REMARK 3 ASYMMETRIC UNIT, FORMING TWO TETRAMERS. HEMIHEDRAL TWINNING WITH
REMARK 3 TWIN FRACTION 0.437 AND TWIN OPERATOR H,-H-K,-L. RESTRAINED NCS
REMARK 3 MODE WAS USED FOR REFINEMENT.
REMARK 4
REMARK 4 2C45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290025995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30363
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.990
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1PPY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE (PH 6.5), 1.5 M
REMARK 280 MAGNESIUM SULPHATE AND 20% PEG2000, HANGING DROP, TEMPERATURE
REMARK 280 292K, PH 7.50, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 20.06333
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 40.12667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 ILE A 115
REMARK 465 ASP A 116
REMARK 465 MET A 117
REMARK 465 GLY A 118
REMARK 465 HIS A 119
REMARK 465 ASP A 120
REMARK 465 PRO A 121
REMARK 465 ALA A 122
REMARK 465 PHE A 123
REMARK 465 VAL A 124
REMARK 465 PRO A 125
REMARK 465 GLU A 126
REMARK 465 ASN A 127
REMARK 465 ALA A 128
REMARK 465 GLY A 129
REMARK 465 GLU A 130
REMARK 465 LEU A 131
REMARK 465 LEU A 132
REMARK 465 ASP A 133
REMARK 465 PRO A 134
REMARK 465 ARG A 135
REMARK 465 LEU A 136
REMARK 465 GLY A 137
REMARK 465 VAL A 138
REMARK 465 GLY A 139
REMARK 465 ILE B 115
REMARK 465 ASP B 116
REMARK 465 MET B 117
REMARK 465 GLY B 118
REMARK 465 HIS B 119
REMARK 465 ASP B 120
REMARK 465 PRO B 121
REMARK 465 ALA B 122
REMARK 465 PHE B 123
REMARK 465 VAL B 124
REMARK 465 PRO B 125
REMARK 465 GLU B 126
REMARK 465 ASN B 127
REMARK 465 ALA B 128
REMARK 465 GLY B 129
REMARK 465 GLU B 130
REMARK 465 LEU B 131
REMARK 465 LEU B 132
REMARK 465 ASP B 133
REMARK 465 PRO B 134
REMARK 465 ARG B 135
REMARK 465 LEU B 136
REMARK 465 GLY B 137
REMARK 465 VAL B 138
REMARK 465 GLY B 139
REMARK 465 ILE C 115
REMARK 465 ASP C 116
REMARK 465 MET C 117
REMARK 465 GLY C 118
REMARK 465 HIS C 119
REMARK 465 ASP C 120
REMARK 465 PRO C 121
REMARK 465 ALA C 122
REMARK 465 PHE C 123
REMARK 465 VAL C 124
REMARK 465 PRO C 125
REMARK 465 GLU C 126
REMARK 465 ASN C 127
REMARK 465 ALA C 128
REMARK 465 GLY C 129
REMARK 465 GLU C 130
REMARK 465 LEU C 131
REMARK 465 LEU C 132
REMARK 465 ASP C 133
REMARK 465 PRO C 134
REMARK 465 ARG C 135
REMARK 465 LEU C 136
REMARK 465 GLY C 137
REMARK 465 VAL C 138
REMARK 465 GLY C 139
REMARK 465 ILE D 115
REMARK 465 ASP D 116
REMARK 465 MET D 117
REMARK 465 GLY D 118
REMARK 465 HIS D 119
REMARK 465 ASP D 120
REMARK 465 PRO D 121
REMARK 465 ALA D 122
REMARK 465 PHE D 123
REMARK 465 VAL D 124
REMARK 465 PRO D 125
REMARK 465 GLU D 126
REMARK 465 ASN D 127
REMARK 465 ALA D 128
REMARK 465 GLY D 129
REMARK 465 GLU D 130
REMARK 465 LEU D 131
REMARK 465 LEU D 132
REMARK 465 ASP D 133
REMARK 465 PRO D 134
REMARK 465 ARG D 135
REMARK 465 LEU D 136
REMARK 465 GLY D 137
REMARK 465 VAL D 138
REMARK 465 GLY D 139
REMARK 465 ILE E 115
REMARK 465 ASP E 116
REMARK 465 MET E 117
REMARK 465 GLY E 118
REMARK 465 HIS E 119
REMARK 465 ASP E 120
REMARK 465 PRO E 121
REMARK 465 ALA E 122
REMARK 465 PHE E 123
REMARK 465 VAL E 124
REMARK 465 PRO E 125
REMARK 465 GLU E 126
REMARK 465 ASN E 127
REMARK 465 ALA E 128
REMARK 465 GLY E 129
REMARK 465 GLU E 130
REMARK 465 LEU E 131
REMARK 465 LEU E 132
REMARK 465 ASP E 133
REMARK 465 PRO E 134
REMARK 465 ARG E 135
REMARK 465 LEU E 136
REMARK 465 GLY E 137
REMARK 465 VAL E 138
REMARK 465 GLY E 139
REMARK 465 ILE F 115
REMARK 465 ASP F 116
REMARK 465 MET F 117
REMARK 465 GLY F 118
REMARK 465 HIS F 119
REMARK 465 ASP F 120
REMARK 465 PRO F 121
REMARK 465 ALA F 122
REMARK 465 PHE F 123
REMARK 465 VAL F 124
REMARK 465 PRO F 125
REMARK 465 GLU F 126
REMARK 465 ASN F 127
REMARK 465 ALA F 128
REMARK 465 GLY F 129
REMARK 465 GLU F 130
REMARK 465 LEU F 131
REMARK 465 LEU F 132
REMARK 465 ASP F 133
REMARK 465 PRO F 134
REMARK 465 ARG F 135
REMARK 465 LEU F 136
REMARK 465 GLY F 137
REMARK 465 VAL F 138
REMARK 465 GLY F 139
REMARK 465 ILE G 115
REMARK 465 ASP G 116
REMARK 465 MET G 117
REMARK 465 GLY G 118
REMARK 465 HIS G 119
REMARK 465 ASP G 120
REMARK 465 PRO G 121
REMARK 465 ALA G 122
REMARK 465 PHE G 123
REMARK 465 VAL G 124
REMARK 465 PRO G 125
REMARK 465 GLU G 126
REMARK 465 ASN G 127
REMARK 465 ALA G 128
REMARK 465 GLY G 129
REMARK 465 GLU G 130
REMARK 465 LEU G 131
REMARK 465 LEU G 132
REMARK 465 ASP G 133
REMARK 465 PRO G 134
REMARK 465 ARG G 135
REMARK 465 LEU G 136
REMARK 465 GLY G 137
REMARK 465 VAL G 138
REMARK 465 GLY G 139
REMARK 465 ILE H 115
REMARK 465 ASP H 116
REMARK 465 MET H 117
REMARK 465 GLY H 118
REMARK 465 HIS H 119
REMARK 465 ASP H 120
REMARK 465 PRO H 121
REMARK 465 ALA H 122
REMARK 465 PHE H 123
REMARK 465 VAL H 124
REMARK 465 PRO H 125
REMARK 465 GLU H 126
REMARK 465 ASN H 127
REMARK 465 ALA H 128
REMARK 465 GLY H 129
REMARK 465 GLU H 130
REMARK 465 LEU H 131
REMARK 465 LEU H 132
REMARK 465 ASP H 133
REMARK 465 PRO H 134
REMARK 465 ARG H 135
REMARK 465 LEU H 136
REMARK 465 GLY H 137
REMARK 465 VAL H 138
REMARK 465 GLY H 139
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO A 114 CA C O CB CG CD
REMARK 470 PRO B 114 CA C O CB CG CD
REMARK 470 PRO C 114 CA C O CB CG CD
REMARK 470 PRO D 114 CA C O CB CG CD
REMARK 470 PRO E 114 CA C O CB CG CD
REMARK 470 PRO F 114 CA C O CB CG CD
REMARK 470 PRO G 114 CA C O CB CG CD
REMARK 470 PRO H 114 CA C O CB CG CD
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 DISTANCE
REMARK 500 NH2 ARG H 12 O HOH H 2003 2.16
REMARK 500 O ALA E 75 O HIS E 77 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 99 OD2 ASP E 95 3564 1.87
REMARK 500 NE ARG B 99 NH2 ARG E 99 3564 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 6 105.69 -55.81
REMARK 500 ARG A 12 37.52 71.05
REMARK 500 CYS A 17 -169.20 -128.94
REMARK 500 ALA A 18 132.36 -178.11
REMARK 500 TYR A 22 128.55 65.21
REMARK 500 SER A 25 -109.28 44.40
REMARK 500 ASP A 37 83.71 48.82
REMARK 500 GLU A 42 129.78 -173.69
REMARK 500 ILE A 69 79.83 -159.73
REMARK 500 ALA A 74 -69.79 69.69
REMARK 500 ALA A 75 -8.16 -59.81
REMARK 500 LEU A 78 -65.00 58.93
REMARK 500 TYR A 90 -154.45 -88.11
REMARK 500 ALA A 91 130.56 167.09
REMARK 500 ASP A 95 -19.75 -46.00
REMARK 500 ARG A 104 92.50 -69.88
REMARK 500 ASN A 112 88.07 68.11
REMARK 500 LYS A 113 -61.79 -145.93
REMARK 500 LEU B 6 107.09 -58.92
REMARK 500 THR B 16 -72.59 -55.10
REMARK 500 ALA B 18 130.17 -175.53
REMARK 500 TYR B 22 129.24 64.49
REMARK 500 SER B 25 -106.02 43.71
REMARK 500 ASP B 37 89.17 45.79
REMARK 500 ASN B 51 25.82 -142.21
REMARK 500 SER B 66 -9.51 -59.43
REMARK 500 ILE B 69 83.22 -154.83
REMARK 500 ALA B 74 -66.96 67.90
REMARK 500 LEU B 78 -65.16 57.19
REMARK 500 TYR B 90 -155.10 -85.11
REMARK 500 ALA B 91 126.04 167.41
REMARK 500 ARG B 104 91.36 -69.54
REMARK 500 ALA B 110 -7.41 -58.83
REMARK 500 ASN B 112 86.30 67.70
REMARK 500 LYS B 113 -59.49 -148.15
REMARK 500 LEU C 6 108.97 -57.87
REMARK 500 ALA C 18 128.89 -172.60
REMARK 500 TYR C 22 125.34 64.31
REMARK 500 SER C 25 -107.80 42.86
REMARK 500 ASP C 37 83.98 49.61
REMARK 500 ASN C 51 27.29 -141.10
REMARK 500 ILE C 69 80.17 -157.03
REMARK 500 ALA C 74 -66.41 66.28
REMARK 500 LEU C 78 -65.47 56.48
REMARK 500 TYR C 90 -153.30 -91.69
REMARK 500 ALA C 91 122.84 164.39
REMARK 500 ASP C 95 -17.87 -43.18
REMARK 500 ARG C 104 86.00 -68.29
REMARK 500 ASN C 112 86.40 66.81
REMARK 500 LYS C 113 -59.61 -147.59
REMARK 500
REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2C45 A 1 139 UNP P9WIL3 PAND_MYCTU 1 139
DBREF 2C45 B 1 139 UNP P9WIL3 PAND_MYCTU 1 139
DBREF 2C45 C 1 139 UNP P9WIL3 PAND_MYCTU 1 139
DBREF 2C45 D 1 139 UNP P9WIL3 PAND_MYCTU 1 139
DBREF 2C45 E 1 139 UNP P9WIL3 PAND_MYCTU 1 139
DBREF 2C45 F 1 139 UNP P9WIL3 PAND_MYCTU 1 139
DBREF 2C45 G 1 139 UNP P9WIL3 PAND_MYCTU 1 139
DBREF 2C45 H 1 139 UNP P9WIL3 PAND_MYCTU 1 139
SEQRES 1 A 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 A 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 A 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 A 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 A 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 A 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 A 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 A 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 A 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 A 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 A 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
SEQRES 1 B 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 B 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 B 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 B 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 B 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 B 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 B 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 B 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 B 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 B 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 B 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
SEQRES 1 C 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 C 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 C 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 C 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 C 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 C 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 C 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 C 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 C 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 C 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 C 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
SEQRES 1 D 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 D 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 D 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 D 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 D 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 D 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 D 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 D 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 D 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 D 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 D 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
SEQRES 1 E 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 E 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 E 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 E 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 E 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 E 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 E 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 E 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 E 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 E 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 E 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
SEQRES 1 F 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 F 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 F 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 F 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 F 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 F 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 F 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 F 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 F 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 F 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 F 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
SEQRES 1 G 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 G 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 G 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 G 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 G 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 G 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 G 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 G 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 G 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 G 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 G 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
SEQRES 1 H 139 MET LEU ARG THR MET LEU LYS SER LYS ILE HIS ARG ALA
SEQRES 2 H 139 THR VAL THR CYS ALA ASP LEU HIS TYR VAL GLY SER VAL
SEQRES 3 H 139 THR ILE ASP ALA ASP LEU MET ASP ALA ALA ASP LEU LEU
SEQRES 4 H 139 GLU GLY GLU GLN VAL THR ILE VAL ASP ILE ASP ASN GLY
SEQRES 5 H 139 ALA ARG LEU VAL THR TYR ALA ILE THR GLY GLU ARG GLY
SEQRES 6 H 139 SER GLY VAL ILE GLY ILE ASN GLY ALA ALA ALA HIS LEU
SEQRES 7 H 139 VAL HIS PRO GLY ASP LEU VAL ILE LEU ILE ALA TYR ALA
SEQRES 8 H 139 THR MET ASP ASP ALA ARG ALA ARG THR TYR GLN PRO ARG
SEQRES 9 H 139 ILE VAL PHE VAL ASP ALA TYR ASN LYS PRO ILE ASP MET
SEQRES 10 H 139 GLY HIS ASP PRO ALA PHE VAL PRO GLU ASN ALA GLY GLU
SEQRES 11 H 139 LEU LEU ASP PRO ARG LEU GLY VAL GLY
FORMUL 9 HOH *49(H2 O)
HELIX 1 1 ALA A 30 ALA A 36 1 7
HELIX 2 2 ASP A 95 THR A 100 1 6
HELIX 3 3 ALA B 30 ALA B 36 1 7
HELIX 4 4 ASP B 95 THR B 100 1 6
HELIX 5 5 ALA C 30 ALA C 36 1 7
HELIX 6 6 ASP C 95 THR C 100 1 6
HELIX 7 7 ALA D 30 ALA D 36 1 7
HELIX 8 8 ASP D 95 THR D 100 1 6
HELIX 9 9 ALA E 30 ALA E 36 1 7
HELIX 10 10 ASP E 95 THR E 100 1 6
HELIX 11 11 ALA F 30 ALA F 36 1 7
HELIX 12 12 ASP F 95 THR F 100 1 6
HELIX 13 13 ALA G 30 ALA G 36 1 7
HELIX 14 14 ASP G 95 THR G 100 1 6
HELIX 15 15 ALA H 30 ALA H 36 1 7
HELIX 16 16 ASP H 95 THR H 100 1 6
SHEET 1 AA 2 LEU A 2 THR A 4 0
SHEET 2 AA 2 THR A 92 ASP A 94 -1 O MET A 93 N ARG A 3
SHEET 1 AB 5 ARG A 54 THR A 57 0
SHEET 2 AB 5 VAL A 44 ASP A 48 -1 O VAL A 44 N THR A 57
SHEET 3 AB 5 LEU A 84 ALA A 89 -1 O ILE A 86 N VAL A 47
SHEET 4 AB 5 SER A 8 THR A 14 -1 O SER A 8 N ALA A 89
SHEET 5 AB 5 ARG A 104 PHE A 107 1 O ARG A 104 N LYS A 9
SHEET 1 AC 4 ALA A 18 ASP A 19 0
SHEET 2 AC 4 ILE A 69 ASN A 72 1 O ILE A 71 N ASP A 19
SHEET 3 AC 4 SER A 25 ASP A 29 -1 O SER A 25 N ASN A 72
SHEET 4 AC 4 ALA A 59 GLY A 62 1 O ILE A 60 N ILE A 28
SHEET 1 BA 2 LEU B 2 THR B 4 0
SHEET 2 BA 2 THR B 92 ASP B 94 -1 O MET B 93 N ARG B 3
SHEET 1 BB 5 ARG B 54 THR B 57 0
SHEET 2 BB 5 VAL B 44 ASP B 48 -1 O VAL B 44 N THR B 57
SHEET 3 BB 5 LEU B 84 ALA B 89 -1 O ILE B 86 N VAL B 47
SHEET 4 BB 5 SER B 8 THR B 14 -1 O SER B 8 N ALA B 89
SHEET 5 BB 5 ARG B 104 PHE B 107 1 O ARG B 104 N LYS B 9
SHEET 1 BC 4 ALA B 18 ASP B 19 0
SHEET 2 BC 4 ILE B 69 ASN B 72 1 O ILE B 71 N ASP B 19
SHEET 3 BC 4 SER B 25 ASP B 29 -1 O SER B 25 N ASN B 72
SHEET 4 BC 4 ALA B 59 GLY B 62 1 O ILE B 60 N ILE B 28
SHEET 1 CA 2 LEU C 2 THR C 4 0
SHEET 2 CA 2 THR C 92 ASP C 94 -1 O MET C 93 N ARG C 3
SHEET 1 CB 5 ARG C 54 THR C 57 0
SHEET 2 CB 5 VAL C 44 ASP C 48 -1 O VAL C 44 N THR C 57
SHEET 3 CB 5 LEU C 84 ALA C 89 -1 O ILE C 86 N VAL C 47
SHEET 4 CB 5 SER C 8 THR C 14 -1 O SER C 8 N ALA C 89
SHEET 5 CB 5 ARG C 104 PHE C 107 1 O ARG C 104 N LYS C 9
SHEET 1 CC 4 ALA C 18 ASP C 19 0
SHEET 2 CC 4 ILE C 69 ASN C 72 1 O ILE C 71 N ASP C 19
SHEET 3 CC 4 SER C 25 ASP C 29 -1 O SER C 25 N ASN C 72
SHEET 4 CC 4 ALA C 59 GLY C 62 1 O ILE C 60 N ILE C 28
SHEET 1 DA 2 LEU D 2 THR D 4 0
SHEET 2 DA 2 THR D 92 ASP D 94 -1 O MET D 93 N ARG D 3
SHEET 1 DB 5 ARG D 54 THR D 57 0
SHEET 2 DB 5 VAL D 44 ASP D 48 -1 O VAL D 44 N THR D 57
SHEET 3 DB 5 LEU D 84 ALA D 89 -1 O ILE D 86 N VAL D 47
SHEET 4 DB 5 SER D 8 THR D 14 -1 O SER D 8 N ALA D 89
SHEET 5 DB 5 ARG D 104 PHE D 107 1 O ARG D 104 N LYS D 9
SHEET 1 DC 4 ALA D 18 ASP D 19 0
SHEET 2 DC 4 ILE D 69 ASN D 72 1 O ILE D 71 N ASP D 19
SHEET 3 DC 4 SER D 25 ASP D 29 -1 O SER D 25 N ASN D 72
SHEET 4 DC 4 ALA D 59 GLY D 62 1 O ILE D 60 N ILE D 28
SHEET 1 EA 2 LEU E 2 THR E 4 0
SHEET 2 EA 2 THR E 92 ASP E 94 -1 O MET E 93 N ARG E 3
SHEET 1 EB 5 ARG E 54 THR E 57 0
SHEET 2 EB 5 VAL E 44 ASP E 48 -1 O VAL E 44 N THR E 57
SHEET 3 EB 5 LEU E 84 ALA E 89 -1 O ILE E 86 N VAL E 47
SHEET 4 EB 5 SER E 8 THR E 14 -1 O SER E 8 N ALA E 89
SHEET 5 EB 5 ARG E 104 PHE E 107 1 O ARG E 104 N LYS E 9
SHEET 1 EC 4 ALA E 18 ASP E 19 0
SHEET 2 EC 4 ILE E 69 ASN E 72 1 O ILE E 71 N ASP E 19
SHEET 3 EC 4 SER E 25 ASP E 29 -1 O SER E 25 N ASN E 72
SHEET 4 EC 4 ALA E 59 GLY E 62 1 O ILE E 60 N ILE E 28
SHEET 1 FA 2 LEU F 2 THR F 4 0
SHEET 2 FA 2 THR F 92 ASP F 94 -1 O MET F 93 N ARG F 3
SHEET 1 FB 5 ARG F 54 THR F 57 0
SHEET 2 FB 5 VAL F 44 ASP F 48 -1 O VAL F 44 N THR F 57
SHEET 3 FB 5 LEU F 84 ALA F 89 -1 O ILE F 86 N VAL F 47
SHEET 4 FB 5 SER F 8 THR F 14 -1 O SER F 8 N ALA F 89
SHEET 5 FB 5 ARG F 104 PHE F 107 1 O ARG F 104 N LYS F 9
SHEET 1 FC 4 CYS F 17 ASP F 19 0
SHEET 2 FC 4 ILE F 69 ASN F 72 1 O ILE F 71 N ASP F 19
SHEET 3 FC 4 SER F 25 ASP F 29 -1 O SER F 25 N ASN F 72
SHEET 4 FC 4 ALA F 59 GLY F 62 1 O ILE F 60 N ILE F 28
SHEET 1 GA 2 LEU G 2 THR G 4 0
SHEET 2 GA 2 THR G 92 ASP G 94 -1 O MET G 93 N ARG G 3
SHEET 1 GB 8 ALA G 18 ASP G 19 0
SHEET 2 GB 8 ILE G 69 ASN G 72 1 O ILE G 71 N ASP G 19
SHEET 3 GB 8 SER G 25 ASP G 29 -1 O SER G 25 N ASN G 72
SHEET 4 GB 8 ARG G 54 GLY G 62 1 O TYR G 58 N VAL G 26
SHEET 5 GB 8 GLN G 43 ASP G 48 -1 O VAL G 44 N THR G 57
SHEET 6 GB 8 LEU G 84 ALA G 89 -1 O ILE G 86 N VAL G 47
SHEET 7 GB 8 SER G 8 THR G 14 -1 O SER G 8 N ALA G 89
SHEET 8 GB 8 ARG G 104 PHE G 107 1 O ARG G 104 N LYS G 9
SHEET 1 HA 2 LEU H 2 THR H 4 0
SHEET 2 HA 2 THR H 92 ASP H 94 -1 O MET H 93 N ARG H 3
SHEET 1 HB 5 ARG H 54 THR H 57 0
SHEET 2 HB 5 VAL H 44 ASP H 48 -1 O VAL H 44 N THR H 57
SHEET 3 HB 5 LEU H 84 ALA H 89 -1 O ILE H 86 N VAL H 47
SHEET 4 HB 5 SER H 8 THR H 14 -1 O SER H 8 N ALA H 89
SHEET 5 HB 5 ARG H 104 PHE H 107 1 O ARG H 104 N LYS H 9
SHEET 1 HC 4 ALA H 18 ASP H 19 0
SHEET 2 HC 4 ILE H 69 ASN H 72 1 O ILE H 71 N ASP H 19
SHEET 3 HC 4 SER H 25 ASP H 29 -1 O SER H 25 N ASN H 72
SHEET 4 HC 4 ALA H 59 GLY H 62 1 O ILE H 60 N ILE H 28
CRYST1 150.100 150.100 60.190 90.00 90.00 120.00 P 31 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 0.006662 0.003846 0.000000 0.00000
SCALE2 0.000000 0.007693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016614 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
