HEADER TRANSPORT PROTEIN/DNA 15-JUL-04 1U1O
TITLE CRYSTAL STRUCTURE OF UP1 COMPLEXED WITH D(TTAGGGTTAG(DI)G); A HUMAN
TITLE 2 TELOMERIC REPEAT CONTAINING INOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*TP*AP*GP*GP*GP*TP*TP*AP*GP*(OIP)*G)-3';
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1;
COMPND 7 CHAIN: A;
COMPND 8 SYNONYM: HELIX-DESTABILIZING PROTEIN, SINGLE-STRAND BINDING PROTEIN,
COMPND 9 HNRNP CORE PROTEIN A1;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: OLIGONUCLEOTIDE D(TTAGGGTTAG (DI) G) BASED ON HUMAN
SOURCE 4 TELOMERIC REPEAT D(TTAGGG)N;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 GENE: HNRPA1;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PYS45
KEYWDS PROTEIN-DNA COMPLEX, UP1, HUMAN TELOMERIC REPEAT, HTR, TR2-G(11)DI,
KEYWDS 2 RRM, RNA RECOGNITION MOTIF, DI, INOSINE, HNRNP A1, TRANSPORT
KEYWDS 3 PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.MYERS,Y.SHAMOO
REVDAT 3 23-AUG-23 1U1O 1 REMARK
REVDAT 2 24-FEB-09 1U1O 1 VERSN
REVDAT 1 21-SEP-04 1U1O 0
JRNL AUTH J.C.MYERS,Y.SHAMOO
JRNL TITL HUMAN UP1 AS A MODEL FOR UNDERSTANDING PURINE RECOGNITION IN
JRNL TITL 2 THE FAMILY OF PROTEINS CONTAINING THE RNA RECOGNITION MOTIF
JRNL TITL 3 (RRM).
JRNL REF J.MOL.BIOL. V. 342 743 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15342234
JRNL DOI 10.1016/J.JMB.2004.07.029
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 513258.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 15339
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) : 0.231
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 750
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1272
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 64
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.044
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1466
REMARK 3 NUCLEIC ACID ATOMS : 230
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.75000
REMARK 3 B22 (A**2) : 6.75000
REMARK 3 B33 (A**2) : -13.49000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.140
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) : 1.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.940 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 39.74
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 : 010304.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : 010304.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023134.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 103.0
REMARK 200 PH : 8.1
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 : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15339
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
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: PDB ENTRY 2UP1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE, GLYCEROL, TRIS,
REMARK 280 SODIUM CHLORIDE, MES, EDTA, BETA-MERCAPTOETHANOL, PH 8.1, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 283.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 86.36900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 25.34050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 25.34050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 129.55350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 25.34050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 25.34050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.18450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 25.34050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 25.34050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 129.55350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 25.34050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 25.34050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.18450
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 86.36900
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 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A
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 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 SER A 6
REMARK 465 PRO A 7
REMARK 465 SER A 191
REMARK 465 SER A 192
REMARK 465 GLN A 193
REMARK 465 ARG A 194
REMARK 465 GLY A 195
REMARK 465 ARG A 196
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2UP1 RELATED DB: PDB
REMARK 900 STRUCTURE OF UP1-TELOMERIC DNA COMPLEX
REMARK 900 RELATED ID: 1PGZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UP1 COMPLEXED WITH D(TTAGGGTTAG(6-MI) G); A
REMARK 900 HUMAN TELOMERIC REPEAT CONTAINING 6-METHYL-8-(2-DEOXY--
REMARK 900 RIBOFURANOSYL)ISOXANTHOPTERIDINE (6-MI)
REMARK 900 RELATED ID: 1PO6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UP1 COMPLEXED WITH D(TTAGG(6MI)TTAGGG); A
REMARK 900 HUMAN TELOMERIC REPEAT CONTAINING 6-METHYL-8-(2-DEOXY--
REMARK 900 RIBOFURANOSYL)ISOXANTHOPTERIDINE (6-MI)
REMARK 900 RELATED ID: 1U1K RELATED DB: PDB
REMARK 900 RELATED ID: 1U1L RELATED DB: PDB
REMARK 900 RELATED ID: 1U1M RELATED DB: PDB
REMARK 900 RELATED ID: 1U1N RELATED DB: PDB
REMARK 900 RELATED ID: 1U1P RELATED DB: PDB
REMARK 900 RELATED ID: 1U1Q RELATED DB: PDB
REMARK 900 RELATED ID: 1U1R RELATED DB: PDB
DBREF 1U1O A 1 196 UNP P09651 ROA1_HUMAN 0 195
DBREF 1U1O B 202 212 PDB 1U1O 1U1O 202 212
SEQRES 1 B 11 DT DA DG DG DG DT DT DA DG DI DG
SEQRES 1 A 196 MET SER LYS SER GLU SER PRO LYS GLU PRO GLU GLN LEU
SEQRES 2 A 196 ARG LYS LEU PHE ILE GLY GLY LEU SER PHE GLU THR THR
SEQRES 3 A 196 ASP GLU SER LEU ARG SER HIS PHE GLU GLN TRP GLY THR
SEQRES 4 A 196 LEU THR ASP CYS VAL VAL MET ARG ASP PRO ASN THR LYS
SEQRES 5 A 196 ARG SER ARG GLY PHE GLY PHE VAL THR TYR ALA THR VAL
SEQRES 6 A 196 GLU GLU VAL ASP ALA ALA MET ASN ALA ARG PRO HIS LYS
SEQRES 7 A 196 VAL ASP GLY ARG VAL VAL GLU PRO LYS ARG ALA VAL SER
SEQRES 8 A 196 ARG GLU ASP SER GLN ARG PRO GLY ALA HIS LEU THR VAL
SEQRES 9 A 196 LYS LYS ILE PHE VAL GLY GLY ILE LYS GLU ASP THR GLU
SEQRES 10 A 196 GLU HIS HIS LEU ARG ASP TYR PHE GLU GLN TYR GLY LYS
SEQRES 11 A 196 ILE GLU VAL ILE GLU ILE MET THR ASP ARG GLY SER GLY
SEQRES 12 A 196 LYS LYS ARG GLY PHE ALA PHE VAL THR PHE ASP ASP HIS
SEQRES 13 A 196 ASP SER VAL ASP LYS ILE VAL ILE GLN LYS TYR HIS THR
SEQRES 14 A 196 VAL ASN GLY HIS ASN CYS GLU VAL ARG LYS ALA LEU SER
SEQRES 15 A 196 LYS GLN GLU MET ALA SER ALA SER SER SER GLN ARG GLY
SEQRES 16 A 196 ARG
FORMUL 3 HOH *87(H2 O)
HELIX 1 1 PRO A 10 ARG A 14 1 5
HELIX 2 2 THR A 26 GLU A 35 1 10
HELIX 3 3 GLN A 36 GLY A 38 5 3
HELIX 4 4 THR A 64 ASN A 73 1 10
HELIX 5 5 GLU A 93 ARG A 97 5 5
HELIX 6 6 GLU A 117 GLU A 126 1 10
HELIX 7 7 GLN A 127 GLY A 129 5 3
HELIX 8 8 ASP A 155 ILE A 164 1 10
HELIX 9 9 SER A 182 SER A 190 1 9
SHEET 1 A 5 LEU A 40 ARG A 47 0
SHEET 2 A 5 SER A 54 TYR A 62 -1 O ARG A 55 N MET A 46
SHEET 3 A 5 LYS A 15 GLY A 19 -1 N ILE A 18 O GLY A 58
SHEET 4 A 5 ARG A 82 ARG A 88 -1 O LYS A 87 N PHE A 17
SHEET 5 A 5 HIS A 77 VAL A 79 -1 N VAL A 79 O ARG A 82
SHEET 1 B 4 ILE A 131 THR A 138 0
SHEET 2 B 4 LYS A 145 PHE A 153 -1 O THR A 152 N GLU A 132
SHEET 3 B 4 LYS A 106 GLY A 110 -1 N VAL A 109 O ALA A 149
SHEET 4 B 4 GLU A 176 LYS A 179 -1 O ARG A 178 N PHE A 108
SHEET 1 C 2 THR A 169 VAL A 170 0
SHEET 2 C 2 HIS A 173 ASN A 174 -1 O HIS A 173 N VAL A 170
CISPEP 1 ARG A 75 PRO A 76 0 0.18
CRYST1 50.681 50.681 172.738 90.00 90.00 90.00 P 43 21 2 8
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 0.019731 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019731 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005789 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
