HEADER LIGASE/RNA 20-JUL-06 2DU4
TITLE CRYSTAL STRUCTURE OF ARCHAEOGLOBUS FULGIDUS O-PHOSPHOSERYL-TRNA
TITLE 2 SYNTHETASE COMPLEXED WITH TRNACYS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA;
COMPND 3 CHAIN: C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: O-PHOSPHOSERYL-TRNA SYNTHETASE;
COMPND 7 CHAIN: A, B;
COMPND 8 EC: 6.1.1.-;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 5 ORGANISM_TAXID: 2234;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET26B
KEYWDS ALPHA4 TETRAMER, LIGASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.FUKUNAGA
REVDAT 5 25-OCT-23 2DU4 1 REMARK
REVDAT 4 09-JUN-09 2DU4 1 REVDAT
REVDAT 3 24-FEB-09 2DU4 1 VERSN
REVDAT 2 06-JAN-09 2DU4 1 JRNL
REVDAT 1 13-MAR-07 2DU4 0
JRNL AUTH R.FUKUNAGA,S.YOKOYAMA
JRNL TITL STRUCTURAL INSIGHTS INTO THE FIRST STEP OF RNA-DEPENDENT
JRNL TITL 2 CYSTEINE BIOSYNTHESIS IN ARCHAEA.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 14 272 2007
JRNL REFN ISSN 1545-9993
JRNL PMID 17351629
JRNL DOI 10.1038/NSMB1219
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2997395.230
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 47199
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) : 0.207
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 : 2362
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7345
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 368
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7540
REMARK 3 NUCLEIC ACID ATOMS : 1520
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 57
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 98.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.76000
REMARK 3 B22 (A**2) : -6.76000
REMARK 3 B33 (A**2) : 13.51000
REMARK 3 B12 (A**2) : 21.67000
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) : 0.46
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.330
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) : 8.790 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 11.520; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 12.140; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 14.230; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 51.49
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 5 : SEP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : DNA-RNA_REP.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000025845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47199
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
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 <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: CNS
REMARK 200 STARTING MODEL: 2DU3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 6000, 1.2M NACL, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 50.51067
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 101.02133
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 101.02133
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 50.51067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER OF O-PHOSPHOSERYL-
REMARK 300 TRNA SYNTHETASE WITH TWO BOUND TRNACYS MOLECULES GENERATED FROM THE
REMARK 300 DIMER O-PHOSPHOSERYL-TRNA SYNTHETASE WITH ONE BOUND TRNACYS
REMARK 300 MOLECULE IN THE ASYMMETRIC UNIT BY THE OPERATIONS: Y, X, -Z
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 PRO A 103
REMARK 465 ASN A 104
REMARK 465 VAL A 105
REMARK 465 GLY A 106
REMARK 465 ILE A 107
REMARK 465 SER A 108
REMARK 465 ALA A 109
REMARK 465 GLU A 110
REMARK 465 LYS A 111
REMARK 465 ILE A 112
REMARK 465 ARG A 113
REMARK 465 GLN A 114
REMARK 465 ILE A 115
REMARK 465 GLU A 116
REMARK 465 ALA A 117
REMARK 465 ILE A 118
REMARK 465 THR A 119
REMARK 465 LYS A 120
REMARK 465 ARG A 121
REMARK 465 GLU A 122
REMARK 465 VAL A 123
REMARK 465 ASP A 124
REMARK 465 SER A 125
REMARK 465 LYS A 126
REMARK 465 PRO A 127
REMARK 465 LEU A 128
REMARK 465 GLN A 129
REMARK 465 GLU A 130
REMARK 465 ILE A 131
REMARK 465 PHE A 132
REMARK 465 HIS A 133
REMARK 465 ARG A 134
REMARK 465 TYR A 135
REMARK 465 LYS A 136
REMARK 465 LYS A 137
REMARK 465 GLY A 138
REMARK 465 GLU A 139
REMARK 465 ILE A 140
REMARK 465 ASP A 141
REMARK 465 GLY A 142
REMARK 465 ASP A 143
REMARK 465 ASP A 144
REMARK 465 LEU A 145
REMARK 465 SER A 146
REMARK 465 TYR A 147
REMARK 465 LEU A 148
REMARK 465 ILE A 149
REMARK 465 ALA A 150
REMARK 465 GLU A 151
REMARK 465 VAL A 152
REMARK 465 LEU A 153
REMARK 465 ASP A 154
REMARK 465 VAL A 155
REMARK 465 ASP A 156
REMARK 465 ASP A 157
REMARK 465 ILE A 158
REMARK 465 THR A 159
REMARK 465 ALA A 160
REMARK 465 VAL A 161
REMARK 465 LYS A 162
REMARK 465 ILE A 163
REMARK 465 LEU A 164
REMARK 465 ASP A 165
REMARK 465 GLU A 166
REMARK 465 VAL A 167
REMARK 465 PHE A 168
REMARK 465 PRO A 169
REMARK 465 GLU A 170
REMARK 465 VAL B 105
REMARK 465 GLY B 106
REMARK 465 ILE B 107
REMARK 465 SER B 108
REMARK 465 ALA B 109
REMARK 465 GLU B 110
REMARK 465 LYS B 111
REMARK 465 ILE B 112
REMARK 465 ARG B 113
REMARK 465 GLN B 114
REMARK 465 ILE B 115
REMARK 465 GLU B 116
REMARK 465 ALA B 117
REMARK 465 ILE B 118
REMARK 465 THR B 119
REMARK 465 LYS B 120
REMARK 465 ARG B 121
REMARK 465 GLU B 122
REMARK 465 VAL B 123
REMARK 465 ASP B 124
REMARK 465 SER B 125
REMARK 465 LYS B 126
REMARK 465 PRO B 127
REMARK 465 LEU B 128
REMARK 465 GLN B 129
REMARK 465 GLU B 130
REMARK 465 ILE B 131
REMARK 465 PHE B 132
REMARK 465 HIS B 133
REMARK 465 ARG B 134
REMARK 465 TYR B 135
REMARK 465 LYS B 136
REMARK 465 LYS B 137
REMARK 465 GLY B 138
REMARK 465 GLU B 139
REMARK 465 ILE B 140
REMARK 465 ASP B 141
REMARK 465 GLY B 142
REMARK 465 ASP B 143
REMARK 465 ASP B 144
REMARK 465 LEU B 145
REMARK 465 SER B 146
REMARK 465 TYR B 147
REMARK 465 LEU B 148
REMARK 465 ILE B 149
REMARK 465 ALA B 150
REMARK 465 GLU B 151
REMARK 465 VAL B 152
REMARK 465 LEU B 153
REMARK 465 ASP B 154
REMARK 465 VAL B 155
REMARK 465 ASP B 156
REMARK 465 ASP B 157
REMARK 465 ILE B 158
REMARK 465 THR B 159
REMARK 465 ALA B 160
REMARK 465 VAL B 161
REMARK 465 LYS B 162
REMARK 465 ILE B 163
REMARK 465 LEU B 164
REMARK 465 ASP B 165
REMARK 465 GLU B 166
REMARK 465 VAL B 167
REMARK 465 PHE B 168
REMARK 465 PRO B 169
REMARK 465 GLU B 170
REMARK 465 PHE B 171
REMARK 465 LYS B 172
REMARK 465 GLU B 173
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 O SER B 185 OH TYR B 229 2.19
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 G C 901 P G C 901 OP3 -0.083
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 320 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 LEU B 56 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 LEU B 326 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 PRO B 459 C - N - CA ANGL. DEV. = 10.7 DEGREES
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 PRO A 32 -38.25 -37.63
REMARK 500 ASP A 76 -2.68 -56.66
REMARK 500 LYS A 172 -11.99 -49.35
REMARK 500 GLU A 173 -70.86 -66.87
REMARK 500 LEU A 174 147.15 -3.89
REMARK 500 SER A 178 167.75 -45.12
REMARK 500 ARG A 184 128.69 -31.90
REMARK 500 ARG A 216 109.32 -169.14
REMARK 500 ARG A 225 147.65 168.77
REMARK 500 LEU A 253 -61.47 -90.80
REMARK 500 ARG A 270 76.90 34.43
REMARK 500 ASP A 277 5.45 82.62
REMARK 500 GLN A 279 95.18 -65.18
REMARK 500 LYS A 288 -34.75 -37.45
REMARK 500 SER A 293 2.88 -55.47
REMARK 500 TYR A 296 42.33 -75.10
REMARK 500 GLU A 316 -10.33 -45.27
REMARK 500 HIS A 352 31.00 -99.65
REMARK 500 GLU A 354 56.81 -90.42
REMARK 500 LYS A 390 -70.39 -60.09
REMARK 500 GLU A 394 109.17 -59.35
REMARK 500 SER A 399 142.50 -175.18
REMARK 500 ARG A 410 147.06 -173.40
REMARK 500 ASN A 422 42.65 74.86
REMARK 500 THR A 423 -157.55 -166.76
REMARK 500 PRO A 428 23.67 -78.41
REMARK 500 ALA A 429 -0.07 -143.35
REMARK 500 LYS A 446 80.49 -65.00
REMARK 500 LYS A 448 8.72 -68.72
REMARK 500 ALA A 480 15.39 -58.93
REMARK 500 GLU A 483 -20.12 58.29
REMARK 500 GLN A 484 157.76 -30.13
REMARK 500 ARG A 492 -107.23 -96.59
REMARK 500 PHE A 526 75.04 29.51
REMARK 500 LEU B 11 -5.05 -47.77
REMARK 500 LYS B 14 -83.08 -82.87
REMARK 500 PHE B 16 -72.83 -58.15
REMARK 500 GLU B 17 -41.10 -26.82
REMARK 500 PRO B 103 105.00 -41.43
REMARK 500 GLN B 219 -62.59 72.79
REMARK 500 LYS B 269 1.17 -63.19
REMARK 500 ARG B 270 65.58 13.62
REMARK 500 ASP B 277 6.32 80.87
REMARK 500 THR B 294 -167.90 -118.98
REMARK 500 ILE B 380 -71.69 -79.20
REMARK 500 GLU B 386 -78.90 -64.53
REMARK 500 GLU B 394 153.49 -45.47
REMARK 500 GLU B 420 173.47 -38.73
REMARK 500 ASN B 422 -37.10 78.93
REMARK 500 THR B 423 -154.68 -66.05
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 G C 956 0.05 SIDE CHAIN
REMARK 500 TYR A 338 0.06 SIDE CHAIN
REMARK 500 TYR B 274 0.06 SIDE CHAIN
REMARK 500 TYR B 338 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DU3 RELATED DB: PDB
REMARK 900 RELATED ID: 2DU5 RELATED DB: PDB
REMARK 900 RELATED ID: 2DU6 RELATED DB: PDB
REMARK 900 RELATED ID: 2DU7 RELATED DB: PDB
DBREF 2DU4 A 1 534 UNP O30126 O30126_ARCFU 1 534
DBREF 2DU4 B 1 534 UNP O30126 O30126_ARCFU 1 534
DBREF 2DU4 C 901 971 PDB 2DU4 2DU4 901 971
SEQRES 1 C 71 G C C A G G G U G G C A G
SEQRES 2 C 71 A G G G G C U U U G C G G
SEQRES 3 C 71 C G G A C U G C A G A U C
SEQRES 4 C 71 C G C U U U A C C C C G G
SEQRES 5 C 71 U U C G A A U C C G G G C
SEQRES 6 C 71 C C U G G C
SEQRES 1 A 534 MET LYS PHE ASP PRO GLN LYS TYR ARG GLU LEU ALA GLU
SEQRES 2 A 534 LYS ASP PHE GLU ALA ALA TRP LYS ALA GLY LYS GLU ILE
SEQRES 3 A 534 LEU ALA GLU ARG SER PRO ASN GLU LEU TYR PRO ARG VAL
SEQRES 4 A 534 GLY PHE SER PHE GLY LYS GLU HIS PRO LEU PHE ALA THR
SEQRES 5 A 534 ILE GLN ARG LEU ARG GLU ALA TYR LEU SER ILE GLY PHE
SEQRES 6 A 534 SER GLU VAL VAL ASN PRO LEU ILE VAL GLU ASP VAL HIS
SEQRES 7 A 534 VAL LYS LYS GLN PHE GLY ARG GLU ALA LEU ALA VAL LEU
SEQRES 8 A 534 ASP ARG CYS PHE TYR LEU ALA THR LEU PRO LYS PRO ASN
SEQRES 9 A 534 VAL GLY ILE SER ALA GLU LYS ILE ARG GLN ILE GLU ALA
SEQRES 10 A 534 ILE THR LYS ARG GLU VAL ASP SER LYS PRO LEU GLN GLU
SEQRES 11 A 534 ILE PHE HIS ARG TYR LYS LYS GLY GLU ILE ASP GLY ASP
SEQRES 12 A 534 ASP LEU SER TYR LEU ILE ALA GLU VAL LEU ASP VAL ASP
SEQRES 13 A 534 ASP ILE THR ALA VAL LYS ILE LEU ASP GLU VAL PHE PRO
SEQRES 14 A 534 GLU PHE LYS GLU LEU LYS PRO ILE SER SER THR LEU THR
SEQRES 15 A 534 LEU ARG SER HIS MET THR THR GLY TRP PHE ILE THR LEU
SEQRES 16 A 534 SER HIS ILE ALA ASP LYS LEU PRO LEU PRO ILE LYS LEU
SEQRES 17 A 534 PHE SER ILE ASP ARG CYS PHE ARG ARG GLU GLN GLY GLU
SEQRES 18 A 534 ASP ALA THR ARG LEU TYR THR TYR PHE SER ALA SER CYS
SEQRES 19 A 534 VAL LEU VAL ASP GLU GLU LEU SER VAL ASP ASP GLY LYS
SEQRES 20 A 534 ALA VAL ALA GLU ALA LEU LEU ARG GLN PHE GLY PHE GLU
SEQRES 21 A 534 ASN PHE ARG PHE ARG LYS ASP GLU LYS ARG SER LYS TYR
SEQRES 22 A 534 TYR ILE PRO ASP THR GLN THR GLU VAL PHE ALA PHE HIS
SEQRES 23 A 534 PRO LYS LEU VAL GLY SER SER THR LYS TYR SER ASP GLY
SEQRES 24 A 534 TRP ILE GLU ILE ALA THR PHE GLY ILE TYR SER PRO THR
SEQRES 25 A 534 ALA LEU ALA GLU TYR ASP ILE PRO TYR PRO VAL MET ASN
SEQRES 26 A 534 LEU GLY LEU GLY VAL GLU ARG LEU ALA MET ILE LEU TYR
SEQRES 27 A 534 GLY TYR ASP ASP VAL ARG LYS MET VAL TYR PRO GLN ILE
SEQRES 28 A 534 HIS GLY GLU ILE LYS LEU SER ASP LEU ASP ILE ALA ARG
SEQRES 29 A 534 GLU ILE LYS VAL LYS GLU VAL PRO GLN THR ALA VAL GLY
SEQRES 30 A 534 LEU LYS ILE ALA GLN SER ILE VAL GLU THR ALA GLU LYS
SEQRES 31 A 534 HIS ALA SER GLU PRO SER PRO CYS SER PHE LEU ALA PHE
SEQRES 32 A 534 GLU GLY GLU MET MET GLY ARG ASN VAL ARG VAL TYR VAL
SEQRES 33 A 534 VAL GLU GLU GLU GLU ASN THR LYS LEU CYS GLY PRO ALA
SEQRES 34 A 534 TYR ALA ASN GLU VAL VAL VAL TYR LYS GLY ASP ILE TYR
SEQRES 35 A 534 GLY ILE PRO LYS THR LYS LYS TRP ARG SER PHE PHE GLU
SEQRES 36 A 534 GLU GLY VAL PRO THR GLY ILE ARG TYR ILE ASP GLY PHE
SEQRES 37 A 534 ALA TYR TYR ALA ALA ARG LYS VAL GLU GLU ALA ALA MET
SEQRES 38 A 534 ARG GLU GLN GLU GLU VAL LYS VAL LYS ALA ARG ILE VAL
SEQRES 39 A 534 GLU ASN LEU SER ASP ILE ASN LEU TYR ILE HIS GLU ASN
SEQRES 40 A 534 VAL ARG ARG TYR ILE LEU TRP LYS LYS GLY LYS ILE ASP
SEQRES 41 A 534 VAL ARG GLY PRO LEU PHE VAL THR VAL LYS ALA GLU ILE
SEQRES 42 A 534 GLU
SEQRES 1 B 534 MET LYS PHE ASP PRO GLN LYS TYR ARG GLU LEU ALA GLU
SEQRES 2 B 534 LYS ASP PHE GLU ALA ALA TRP LYS ALA GLY LYS GLU ILE
SEQRES 3 B 534 LEU ALA GLU ARG SER PRO ASN GLU LEU TYR PRO ARG VAL
SEQRES 4 B 534 GLY PHE SER PHE GLY LYS GLU HIS PRO LEU PHE ALA THR
SEQRES 5 B 534 ILE GLN ARG LEU ARG GLU ALA TYR LEU SER ILE GLY PHE
SEQRES 6 B 534 SER GLU VAL VAL ASN PRO LEU ILE VAL GLU ASP VAL HIS
SEQRES 7 B 534 VAL LYS LYS GLN PHE GLY ARG GLU ALA LEU ALA VAL LEU
SEQRES 8 B 534 ASP ARG CYS PHE TYR LEU ALA THR LEU PRO LYS PRO ASN
SEQRES 9 B 534 VAL GLY ILE SER ALA GLU LYS ILE ARG GLN ILE GLU ALA
SEQRES 10 B 534 ILE THR LYS ARG GLU VAL ASP SER LYS PRO LEU GLN GLU
SEQRES 11 B 534 ILE PHE HIS ARG TYR LYS LYS GLY GLU ILE ASP GLY ASP
SEQRES 12 B 534 ASP LEU SER TYR LEU ILE ALA GLU VAL LEU ASP VAL ASP
SEQRES 13 B 534 ASP ILE THR ALA VAL LYS ILE LEU ASP GLU VAL PHE PRO
SEQRES 14 B 534 GLU PHE LYS GLU LEU LYS PRO ILE SER SER THR LEU THR
SEQRES 15 B 534 LEU ARG SER HIS MET THR THR GLY TRP PHE ILE THR LEU
SEQRES 16 B 534 SER HIS ILE ALA ASP LYS LEU PRO LEU PRO ILE LYS LEU
SEQRES 17 B 534 PHE SER ILE ASP ARG CYS PHE ARG ARG GLU GLN GLY GLU
SEQRES 18 B 534 ASP ALA THR ARG LEU TYR THR TYR PHE SER ALA SER CYS
SEQRES 19 B 534 VAL LEU VAL ASP GLU GLU LEU SER VAL ASP ASP GLY LYS
SEQRES 20 B 534 ALA VAL ALA GLU ALA LEU LEU ARG GLN PHE GLY PHE GLU
SEQRES 21 B 534 ASN PHE ARG PHE ARG LYS ASP GLU LYS ARG SER LYS TYR
SEQRES 22 B 534 TYR ILE PRO ASP THR GLN THR GLU VAL PHE ALA PHE HIS
SEQRES 23 B 534 PRO LYS LEU VAL GLY SER SER THR LYS TYR SER ASP GLY
SEQRES 24 B 534 TRP ILE GLU ILE ALA THR PHE GLY ILE TYR SER PRO THR
SEQRES 25 B 534 ALA LEU ALA GLU TYR ASP ILE PRO TYR PRO VAL MET ASN
SEQRES 26 B 534 LEU GLY LEU GLY VAL GLU ARG LEU ALA MET ILE LEU TYR
SEQRES 27 B 534 GLY TYR ASP ASP VAL ARG LYS MET VAL TYR PRO GLN ILE
SEQRES 28 B 534 HIS GLY GLU ILE LYS LEU SER ASP LEU ASP ILE ALA ARG
SEQRES 29 B 534 GLU ILE LYS VAL LYS GLU VAL PRO GLN THR ALA VAL GLY
SEQRES 30 B 534 LEU LYS ILE ALA GLN SER ILE VAL GLU THR ALA GLU LYS
SEQRES 31 B 534 HIS ALA SER GLU PRO SER PRO CYS SER PHE LEU ALA PHE
SEQRES 32 B 534 GLU GLY GLU MET MET GLY ARG ASN VAL ARG VAL TYR VAL
SEQRES 33 B 534 VAL GLU GLU GLU GLU ASN THR LYS LEU CYS GLY PRO ALA
SEQRES 34 B 534 TYR ALA ASN GLU VAL VAL VAL TYR LYS GLY ASP ILE TYR
SEQRES 35 B 534 GLY ILE PRO LYS THR LYS LYS TRP ARG SER PHE PHE GLU
SEQRES 36 B 534 GLU GLY VAL PRO THR GLY ILE ARG TYR ILE ASP GLY PHE
SEQRES 37 B 534 ALA TYR TYR ALA ALA ARG LYS VAL GLU GLU ALA ALA MET
SEQRES 38 B 534 ARG GLU GLN GLU GLU VAL LYS VAL LYS ALA ARG ILE VAL
SEQRES 39 B 534 GLU ASN LEU SER ASP ILE ASN LEU TYR ILE HIS GLU ASN
SEQRES 40 B 534 VAL ARG ARG TYR ILE LEU TRP LYS LYS GLY LYS ILE ASP
SEQRES 41 B 534 VAL ARG GLY PRO LEU PHE VAL THR VAL LYS ALA GLU ILE
SEQRES 42 B 534 GLU
FORMUL 4 HOH *57(H2 O)
HELIX 1 1 ASP A 4 GLU A 13 1 10
HELIX 2 2 ASP A 15 GLY A 23 1 9
HELIX 3 3 LYS A 24 LEU A 27 5 4
HELIX 4 4 SER A 31 LEU A 35 5 5
HELIX 5 5 HIS A 47 ILE A 63 1 17
HELIX 6 6 ASP A 76 GLY A 84 1 9
HELIX 7 7 GLU A 86 LEU A 91 1 6
HELIX 8 8 HIS A 186 HIS A 197 1 12
HELIX 9 9 VAL A 243 ARG A 255 1 13
HELIX 10 10 PRO A 287 VAL A 290 5 4
HELIX 11 11 LYS A 295 ASP A 298 5 4
HELIX 12 12 SER A 310 GLU A 316 1 7
HELIX 13 13 VAL A 330 TYR A 338 1 9
HELIX 14 14 ASP A 342 TYR A 348 1 7
HELIX 15 15 SER A 358 GLU A 365 1 8
HELIX 16 16 THR A 374 HIS A 391 1 18
HELIX 17 17 TRP A 450 GLY A 457 1 8
HELIX 18 18 TYR A 464 ALA A 480 1 17
HELIX 19 19 ASN A 496 ILE A 500 5 5
HELIX 20 20 HIS A 505 LYS A 515 1 11
HELIX 21 21 ASP B 4 LYS B 14 1 11
HELIX 22 22 ASP B 15 GLY B 23 1 9
HELIX 23 23 LYS B 24 LEU B 27 5 4
HELIX 24 24 SER B 31 LEU B 35 5 5
HELIX 25 25 HIS B 47 SER B 62 1 16
HELIX 26 26 ASP B 76 GLY B 84 1 9
HELIX 27 27 GLU B 86 LEU B 91 1 6
HELIX 28 28 ASP B 92 CYS B 94 5 3
HELIX 29 29 MET B 187 SER B 196 1 10
HELIX 30 30 SER B 242 GLN B 256 1 15
HELIX 31 31 SER B 310 GLU B 316 1 7
HELIX 32 32 VAL B 330 GLY B 339 1 10
HELIX 33 33 ASP B 342 TYR B 348 1 7
HELIX 34 34 SER B 358 GLU B 365 1 8
HELIX 35 35 THR B 374 HIS B 391 1 18
HELIX 36 36 THR B 447 LYS B 449 5 3
HELIX 37 37 TRP B 450 GLY B 457 1 8
HELIX 38 38 TYR B 464 ARG B 482 1 19
HELIX 39 39 LEU B 497 ILE B 500 5 4
HELIX 40 40 HIS B 505 LYS B 515 1 11
SHEET 1 A 7 SER A 66 GLU A 67 0
SHEET 2 A 7 ILE A 206 PHE A 215 1 O PHE A 209 N SER A 66
SHEET 3 A 7 THR A 228 VAL A 237 -1 O SER A 233 N SER A 210
SHEET 4 A 7 VAL A 323 GLY A 329 -1 O MET A 324 N LEU A 236
SHEET 5 A 7 TRP A 300 ILE A 308 -1 N GLY A 307 O ASN A 325
SHEET 6 A 7 THR A 280 PHE A 285 -1 N VAL A 282 O ALA A 304
SHEET 7 A 7 ASN A 261 LYS A 266 -1 N ARG A 265 O GLU A 281
SHEET 1 B 2 ILE A 73 GLU A 75 0
SHEET 2 B 2 LEU A 181 LEU A 183 -1 O THR A 182 N VAL A 74
SHEET 1 C 4 TYR A 96 ALA A 98 0
SHEET 2 C 4 PHE B 95 THR B 99 -1 O ALA B 98 N TYR A 96
SHEET 3 C 4 ILE B 177 LEU B 183 -1 O ILE B 177 N THR B 99
SHEET 4 C 4 ILE B 73 GLU B 75 -1 N VAL B 74 O THR B 182
SHEET 1 D 2 ILE A 366 VAL A 368 0
SHEET 2 D 2 LEU A 502 ILE A 504 -1 O TYR A 503 N LYS A 367
SHEET 1 E 4 CYS A 398 GLU A 406 0
SHEET 2 E 4 ASN A 411 GLU A 418 -1 O VAL A 414 N PHE A 403
SHEET 3 E 4 GLY A 523 ILE A 533 -1 O LYS A 530 N TYR A 415
SHEET 4 E 4 GLU A 486 VAL A 494 -1 N VAL A 494 O GLY A 523
SHEET 1 F 4 VAL A 458 ARG A 463 0
SHEET 2 F 4 GLU A 433 TYR A 437 -1 N VAL A 434 O ILE A 462
SHEET 3 F 4 ASP A 440 ILE A 444 -1 O ILE A 444 N GLU A 433
SHEET 4 F 4 ILE A 519 ASP A 520 1 O ASP A 520 N GLY A 443
SHEET 1 G 7 SER B 66 GLU B 67 0
SHEET 2 G 7 ILE B 206 PHE B 215 1 O LYS B 207 N SER B 66
SHEET 3 G 7 THR B 228 VAL B 237 -1 O TYR B 229 N CYS B 214
SHEET 4 G 7 VAL B 323 GLY B 329 -1 O LEU B 326 N CYS B 234
SHEET 5 G 7 ASP B 298 ILE B 308 -1 N GLY B 307 O ASN B 325
SHEET 6 G 7 THR B 280 VAL B 290 -1 N HIS B 286 O GLY B 299
SHEET 7 G 7 ASN B 261 LYS B 266 -1 N ARG B 265 O GLU B 281
SHEET 1 H 2 LYS B 367 VAL B 368 0
SHEET 2 H 2 LEU B 502 TYR B 503 -1 O TYR B 503 N LYS B 367
SHEET 1 I 4 CYS B 398 MET B 407 0
SHEET 2 I 4 ARG B 410 GLU B 418 -1 O VAL B 414 N ALA B 402
SHEET 3 I 4 THR B 528 ILE B 533 -1 O LYS B 530 N TYR B 415
SHEET 4 I 4 GLU B 486 VAL B 489 -1 N VAL B 489 O VAL B 529
SHEET 1 J 4 VAL B 458 ARG B 463 0
SHEET 2 J 4 GLU B 433 TYR B 437 -1 N VAL B 436 O VAL B 458
SHEET 3 J 4 ASP B 440 ILE B 444 -1 O TYR B 442 N VAL B 435
SHEET 4 J 4 ILE B 519 ASP B 520 1 O ASP B 520 N ILE B 441
SHEET 1 K 2 ILE B 493 VAL B 494 0
SHEET 2 K 2 GLY B 523 PRO B 524 -1 O GLY B 523 N VAL B 494
CISPEP 1 TYR A 36 PRO A 37 0 0.20
CISPEP 2 LEU A 204 PRO A 205 0 0.31
CISPEP 3 SER A 396 PRO A 397 0 -0.21
CISPEP 4 TYR B 36 PRO B 37 0 0.60
CISPEP 5 LEU B 204 PRO B 205 0 -0.69
CISPEP 6 SER B 396 PRO B 397 0 -0.03
CRYST1 148.433 148.433 151.532 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 0.006737 0.003890 0.000000 0.00000
SCALE2 0.000000 0.007779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006599 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
