HEADER HYDROLASE/DNA 24-AUG-09 3IRQ
TITLE CRYSTAL STRUCTURE OF A Z-Z JUNCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOUBLE-STRANDED RNA-SPECIFIC ADENOSINE DEAMINASE;
COMPND 3 CHAIN: D, C, B, A;
COMPND 4 FRAGMENT: ZALPHA DOMAIN;
COMPND 5 SYNONYM: DRADA, 136 KDA DOUBLE-STRANDED RNA-BINDING PROTEIN, P136,
COMPND 6 K88DSRBP, INTERFERON-INDUCIBLE PROTEIN 4, IFI-4;
COMPND 7 EC: 3.5.4.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA (5'-D(*GP*TP*CP*GP*CP*GP*CP*GP*TP*CP*GP*CP*GP*CP*G)-
COMPND 11 3');
COMPND 12 CHAIN: G;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA (5'-D(*AP*CP*CP*GP*CP*GP*CP*GP*AP*CP*GP*CP*GP*CP*G)-
COMPND 16 3');
COMPND 17 CHAIN: F;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADAR, ADAR1, DSRAD, G1P1, IFI4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS Z-DNA, ADAR1, RNA EDITING, INNATE IMMUNITY, DNA JUNCTION, Z DOMAIN,
KEYWDS 2 ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING, CYTOPLASM, DISEASE
KEYWDS 3 MUTATION, DNA-BINDING, HYDROLASE, ISOPEPTIDE BOND, METAL-BINDING,
KEYWDS 4 MRNA PROCESSING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, RNA-BINDING,
KEYWDS 5 RNA-MEDIATED GENE SILENCING, UBL CONJUGATION, ZINC, HYDROLASE-DNA
KEYWDS 6 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ATHANASIADIS,M.DE ROSA
REVDAT 3 06-SEP-23 3IRQ 1 SEQADV
REVDAT 2 02-JUN-10 3IRQ 1 JRNL
REVDAT 1 19-MAY-10 3IRQ 0
JRNL AUTH M.DE ROSA,D.DE SANCTIS,A.L.ROSARIO,M.ARCHER,A.RICH,
JRNL AUTH 2 A.ATHANASIADIS,M.A.CARRONDO
JRNL TITL CRYSTAL STRUCTURE OF A JUNCTION BETWEEN TWO Z-DNA HELICES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 9088 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20439751
JRNL DOI 10.1073/PNAS.1003182107
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 7864
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640
REMARK 3 FREE R VALUE TEST SET COUNT : 365
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 72.8264 - 4.0382 0.94 2571 118 0.2213 0.2393
REMARK 3 2 4.0382 - 3.2052 0.97 2500 125 0.2134 0.2745
REMARK 3 3 3.2052 - 2.8001 0.95 2428 122 0.2762 0.3343
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 39.57
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 79.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 2609
REMARK 3 ANGLE : 0.692 3620
REMARK 3 CHIRALITY : 0.037 410
REMARK 3 PLANARITY : 0.002 352
REMARK 3 DIHEDRAL : 19.097 1044
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN D AND (RESSEQ 183:186 OR RESSEQ
REMARK 3 176:179 OR RESSEQ 191:195 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 183:186 OR RESSEQ
REMARK 3 176:179 OR RESSEQ 191:195 )
REMARK 3 ATOM PAIRS NUMBER : 101
REMARK 3 RMSD : 0.023
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN D AND (RESSEQ 183:186 OR RESSEQ
REMARK 3 176:179 OR RESSEQ 191:195 )
REMARK 3 SELECTION : CHAIN A AND (RESSEQ 183:186 OR RESSEQ
REMARK 3 176:179 OR RESSEQ 191:195 )
REMARK 3 ATOM PAIRS NUMBER : 103
REMARK 3 RMSD : 0.038
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN D AND (RESSEQ 183:186 OR RESSEQ
REMARK 3 176:179 OR RESSEQ 191:195 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 183:186 OR RESSEQ
REMARK 3 176:179 OR RESSEQ 191:195 )
REMARK 3 ATOM PAIRS NUMBER : 103
REMARK 3 RMSD : 0.020
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7894
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 106.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
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) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.25600
REMARK 200 R SYM FOR SHELL (I) : 0.14900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1QBJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 2000, 0.1 M TRIS-HCL, 0.2 M
REMARK 280 AMMONIUM ACETATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 -1.000000 0.000000 0.000000 14.64150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.24100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.88050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.24100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 14.64150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.88050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: BIOLOGICAL ASSEMBLY IS A DOUBLE STRANDED DNA MOLECULE BOUND
REMARK 300 BY FOUR PROTEIN MOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G, F, C, 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 SER D 200
REMARK 465 THR D 201
REMARK 465 GLN D 202
REMARK 465 DG G -1
REMARK 465 DA F -1
REMARK 465 SER C 200
REMARK 465 THR C 201
REMARK 465 GLN C 202
REMARK 465 GLY B 136
REMARK 465 VAL B 199
REMARK 465 SER B 200
REMARK 465 THR B 201
REMARK 465 GLN B 202
REMARK 465 GLY A 136
REMARK 465 ALA A 198
REMARK 465 VAL A 199
REMARK 465 SER A 200
REMARK 465 THR A 201
REMARK 465 GLN A 202
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 LYS D 145 CE NZ
REMARK 470 GLN D 186 CG CD OE1 NE2
REMARK 470 DT G 0 C2 O2 N3 C4 O4 C5 C7
REMARK 470 DT G 0 C6
REMARK 470 DC F 0 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC F 0 C6
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 LYS B 184 CE NZ
REMARK 470 GLN B 186 CG CD OE1 NE2
REMARK 470 LYS A 154 CE NZ
REMARK 470 LYS A 187 CE NZ
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 DT G 7 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT G 7 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC F 12 O4' - C1' - N1 ANGL. DEV. = 2.7 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 SER D 137 -179.22 -65.89
REMARK 500 GLU D 149 38.64 -78.97
REMARK 500 LEU B 150 -75.52 -56.99
REMARK 500 ALA B 189 166.30 -47.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QBJ RELATED DB: PDB
REMARK 900 ZALPHA/Z-DNA
REMARK 900 RELATED ID: 3IRR RELATED DB: PDB
REMARK 900 Z-Z JUNCTION (WITH HEPES INTERCALATING)
DBREF 3IRQ D 140 202 UNP P55265 DSRAD_HUMAN 140 202
DBREF 3IRQ C 140 202 UNP P55265 DSRAD_HUMAN 140 202
DBREF 3IRQ B 140 202 UNP P55265 DSRAD_HUMAN 140 202
DBREF 3IRQ A 140 202 UNP P55265 DSRAD_HUMAN 140 202
DBREF 3IRQ G -1 13 PDB 3IRQ 3IRQ -1 13
DBREF 3IRQ F -1 13 PDB 3IRQ 3IRQ -1 13
SEQADV 3IRQ GLY D 136 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ SER D 137 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ HIS D 138 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ MET D 139 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ GLY C 136 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ SER C 137 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ HIS C 138 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ MET C 139 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ GLY B 136 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ SER B 137 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ HIS B 138 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ MET B 139 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ GLY A 136 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ SER A 137 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ HIS A 138 UNP P55265 EXPRESSION TAG
SEQADV 3IRQ MET A 139 UNP P55265 EXPRESSION TAG
SEQRES 1 D 67 GLY SER HIS MET GLU GLN ARG ILE LEU LYS PHE LEU GLU
SEQRES 2 D 67 GLU LEU GLY GLU GLY LYS ALA THR THR ALA HIS ASP LEU
SEQRES 3 D 67 SER GLY LYS LEU GLY THR PRO LYS LYS GLU ILE ASN ARG
SEQRES 4 D 67 VAL LEU TYR SER LEU ALA LYS LYS GLY LYS LEU GLN LYS
SEQRES 5 D 67 GLU ALA GLY THR PRO PRO LEU TRP LYS ILE ALA VAL SER
SEQRES 6 D 67 THR GLN
SEQRES 1 G 15 DG DT DC DG DC DG DC DG DT DC DG DC DG
SEQRES 2 G 15 DC DG
SEQRES 1 F 15 DA DC DC DG DC DG DC DG DA DC DG DC DG
SEQRES 2 F 15 DC DG
SEQRES 1 C 67 GLY SER HIS MET GLU GLN ARG ILE LEU LYS PHE LEU GLU
SEQRES 2 C 67 GLU LEU GLY GLU GLY LYS ALA THR THR ALA HIS ASP LEU
SEQRES 3 C 67 SER GLY LYS LEU GLY THR PRO LYS LYS GLU ILE ASN ARG
SEQRES 4 C 67 VAL LEU TYR SER LEU ALA LYS LYS GLY LYS LEU GLN LYS
SEQRES 5 C 67 GLU ALA GLY THR PRO PRO LEU TRP LYS ILE ALA VAL SER
SEQRES 6 C 67 THR GLN
SEQRES 1 B 67 GLY SER HIS MET GLU GLN ARG ILE LEU LYS PHE LEU GLU
SEQRES 2 B 67 GLU LEU GLY GLU GLY LYS ALA THR THR ALA HIS ASP LEU
SEQRES 3 B 67 SER GLY LYS LEU GLY THR PRO LYS LYS GLU ILE ASN ARG
SEQRES 4 B 67 VAL LEU TYR SER LEU ALA LYS LYS GLY LYS LEU GLN LYS
SEQRES 5 B 67 GLU ALA GLY THR PRO PRO LEU TRP LYS ILE ALA VAL SER
SEQRES 6 B 67 THR GLN
SEQRES 1 A 67 GLY SER HIS MET GLU GLN ARG ILE LEU LYS PHE LEU GLU
SEQRES 2 A 67 GLU LEU GLY GLU GLY LYS ALA THR THR ALA HIS ASP LEU
SEQRES 3 A 67 SER GLY LYS LEU GLY THR PRO LYS LYS GLU ILE ASN ARG
SEQRES 4 A 67 VAL LEU TYR SER LEU ALA LYS LYS GLY LYS LEU GLN LYS
SEQRES 5 A 67 GLU ALA GLY THR PRO PRO LEU TRP LYS ILE ALA VAL SER
SEQRES 6 A 67 THR GLN
FORMUL 7 HOH *18(H2 O)
HELIX 1 1 SER D 137 GLU D 149 1 13
HELIX 2 2 THR D 157 LEU D 165 1 9
HELIX 3 3 PRO D 168 LYS D 181 1 14
HELIX 4 4 GLY C 136 LEU C 150 1 15
HELIX 5 5 THR C 157 LEU C 165 1 9
HELIX 6 6 PRO C 168 LYS C 182 1 15
HELIX 7 7 SER B 137 GLY B 151 1 15
HELIX 8 8 THR B 157 GLY B 166 1 10
HELIX 9 9 PRO B 168 LYS B 182 1 15
HELIX 10 10 SER A 137 GLU A 149 1 13
HELIX 11 11 THR A 157 LEU A 165 1 9
HELIX 12 12 PRO A 168 LYS A 181 1 14
SHEET 1 A 2 LEU D 185 GLU D 188 0
SHEET 2 A 2 LEU D 194 ILE D 197 -1 O LYS D 196 N GLN D 186
SHEET 1 B 2 LEU C 185 GLU C 188 0
SHEET 2 B 2 LEU C 194 ILE C 197 -1 O LEU C 194 N GLU C 188
SHEET 1 C 2 LEU B 185 GLU B 188 0
SHEET 2 C 2 LEU B 194 ILE B 197 -1 O LYS B 196 N GLN B 186
SHEET 1 D 2 GLN A 186 GLU A 188 0
SHEET 2 D 2 LEU A 194 LYS A 196 -1 O LEU A 194 N GLU A 188
CISPEP 1 THR D 191 PRO D 192 0 7.69
CISPEP 2 THR C 191 PRO C 192 0 7.63
CISPEP 3 THR B 191 PRO B 192 0 7.87
CISPEP 4 THR A 191 PRO A 192 0 5.90
CRYST1 29.283 99.761 106.482 90.00 90.00 90.00 P 21 21 21 16
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 0.034150 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010024 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009391 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
