HEADER TRANSCRIPTION 19-MAY-09 3HI9
TITLE THE X-RAY CRYSTAL STRUCTURE OF THE FIRST RNA RECOGNITION
TITLE 2 MOTIF (RRM1) OF THE AU-RICH ELEMENT (ARE) BINDING PROTEIN
TITLE 3 HUR AT 2.0 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELAV-LIKE PROTEIN 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RRM1 DOMAIN: UNP RESIDUES 18-99;
COMPND 5 SYNONYM: HU-ANTIGEN R, HUR;
COMPND 6 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: ELAVL1, HUR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BETA1-ALPHA1-BETA2-BETA3-ALPHA2-BETA4 TOPOLOGY, METHYLATION,
KEYWDS 2 PHOSPHOPROTEIN, RNA-BINDING, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.BENOIT,J.KALLEN
REVDAT 2 07-APR-10 3HI9 1 JRNL
REVDAT 1 31-MAR-10 3HI9 0
JRNL AUTH R.M.BENOIT,N.C.MEISNER,J.KALLEN,P.GRAFF,R.HEMMIG,
JRNL AUTH 2 R.CEBE,C.OSTERMEIER,H.WIDMER,M.AUER
JRNL TITL THE X-RAY CRYSTAL STRUCTURE OF THE FIRST RNA
JRNL TITL 2 RECOGNITION MOTIF AND SITE-DIRECTED MUTAGENESIS
JRNL TITL 3 SUGGEST A POSSIBLE HUR REDOX SENSING MECHANISM.
JRNL REF J.MOL.BIOL. V. 397 1231 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20219472
JRNL DOI 10.1016/J.JMB.2010.02.043
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0063
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 32762
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 + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1639
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2239
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2504
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.01000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.147
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.764
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2539 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3430 ; 1.361 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 5.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;36.591 ;23.529
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 470 ;14.225 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;15.798 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 398 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1887 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1574 ; 0.942 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2536 ; 1.818 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 965 ; 2.769 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 887 ; 4.815 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. U VALUES: REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 3HI9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB053166.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00778
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32767
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
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) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.48400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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 1FXL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M DI-AMMONIUM CITRATE, 20% W/V
REMARK 280 PEG 3350, 5% GLYCEROL, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 49.12033
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 98.24067
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 98.24067
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 49.12033
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY A 16
REMARK 465 PRO A 17
REMARK 465 ARG A 97
REMARK 465 PRO A 98
REMARK 465 SER A 99
REMARK 465 GLY B 16
REMARK 465 PRO B 17
REMARK 465 ASP B 54
REMARK 465 LYS B 55
REMARK 465 VAL B 56
REMARK 465 ALA B 57
REMARK 465 GLY B 58
REMARK 465 HIS B 59
REMARK 465 SER B 99
REMARK 465 GLY C 16
REMARK 465 PRO C 17
REMARK 465 ARG C 97
REMARK 465 PRO C 98
REMARK 465 SER C 99
REMARK 465 GLY D 16
REMARK 465 PRO D 17
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 TYR A 26 41.64 72.32
REMARK 500 GLN A 87 -122.43 45.21
REMARK 500 TYR B 26 44.85 70.32
REMARK 500 GLN B 87 -116.70 56.65
REMARK 500 GLN C 87 61.92 34.86
REMARK 500 SER C 88 -1.12 71.74
REMARK 500 VAL D 56 -73.79 -95.88
REMARK 500 ALA D 57 -1.13 -58.75
REMARK 500 GLN D 87 -113.17 51.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FXL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUD AND AU-RICH ELEMENT OF THE C-FOS
REMARK 900 RNA
DBREF 3HI9 A 18 99 UNP Q15717 ELAV1_HUMAN 18 99
DBREF 3HI9 B 18 99 UNP Q15717 ELAV1_HUMAN 18 99
DBREF 3HI9 C 18 99 UNP Q15717 ELAV1_HUMAN 18 99
DBREF 3HI9 D 18 99 UNP Q15717 ELAV1_HUMAN 18 99
SEQADV 3HI9 GLY A 16 UNP Q15717 EXPRESSION TAG
SEQADV 3HI9 PRO A 17 UNP Q15717 EXPRESSION TAG
SEQADV 3HI9 GLY B 16 UNP Q15717 EXPRESSION TAG
SEQADV 3HI9 PRO B 17 UNP Q15717 EXPRESSION TAG
SEQADV 3HI9 GLY C 16 UNP Q15717 EXPRESSION TAG
SEQADV 3HI9 PRO C 17 UNP Q15717 EXPRESSION TAG
SEQADV 3HI9 GLY D 16 UNP Q15717 EXPRESSION TAG
SEQADV 3HI9 PRO D 17 UNP Q15717 EXPRESSION TAG
SEQRES 1 A 84 GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO
SEQRES 2 A 84 GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER
SEQRES 3 A 84 SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP
SEQRES 4 A 84 LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN
SEQRES 5 A 84 TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR
SEQRES 6 A 84 LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL
SEQRES 7 A 84 SER TYR ALA ARG PRO SER
SEQRES 1 B 84 GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO
SEQRES 2 B 84 GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER
SEQRES 3 B 84 SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP
SEQRES 4 B 84 LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN
SEQRES 5 B 84 TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR
SEQRES 6 B 84 LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL
SEQRES 7 B 84 SER TYR ALA ARG PRO SER
SEQRES 1 C 84 GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO
SEQRES 2 C 84 GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER
SEQRES 3 C 84 SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP
SEQRES 4 C 84 LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN
SEQRES 5 C 84 TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR
SEQRES 6 C 84 LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL
SEQRES 7 C 84 SER TYR ALA ARG PRO SER
SEQRES 1 D 84 GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO
SEQRES 2 D 84 GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER
SEQRES 3 D 84 SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP
SEQRES 4 D 84 LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN
SEQRES 5 D 84 TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR
SEQRES 6 D 84 LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL
SEQRES 7 D 84 SER TYR ALA ARG PRO SER
FORMUL 5 HOH *197(H2 O)
HELIX 1 1 THR A 32 SER A 42 1 11
HELIX 2 2 THR A 70 ASN A 82 1 13
HELIX 3 3 THR B 32 SER B 42 1 11
HELIX 4 4 THR B 70 ASN B 82 1 13
HELIX 5 5 THR C 32 SER C 42 1 11
HELIX 6 6 THR C 70 ASN C 82 1 13
HELIX 7 7 THR D 32 SER D 42 1 11
HELIX 8 8 THR D 70 ASN D 82 1 13
SHEET 1 A 4 VAL A 46 ARG A 53 0
SHEET 2 A 4 SER A 60 TYR A 68 -1 O ASN A 67 N SER A 48
SHEET 3 A 4 ASN A 21 ASN A 25 -1 N LEU A 22 O VAL A 66
SHEET 4 A 4 LYS A 92 TYR A 95 -1 O LYS A 92 N ASN A 25
SHEET 1 B 2 ARG A 85 LEU A 86 0
SHEET 2 B 2 LYS A 89 THR A 90 -1 O LYS A 89 N LEU A 86
SHEET 1 C 4 VAL B 46 LEU B 51 0
SHEET 2 C 4 TYR B 63 TYR B 68 -1 O ASN B 67 N GLU B 47
SHEET 3 C 4 ASN B 21 ASN B 25 -1 N VAL B 24 O GLY B 64
SHEET 4 C 4 LYS B 92 TYR B 95 -1 O SER B 94 N ILE B 23
SHEET 1 D 2 ARG B 85 LEU B 86 0
SHEET 2 D 2 LYS B 89 THR B 90 -1 O LYS B 89 N LEU B 86
SHEET 1 E 4 VAL C 46 ARG C 53 0
SHEET 2 E 4 SER C 60 TYR C 68 -1 O LEU C 61 N ILE C 52
SHEET 3 E 4 ASN C 21 ASN C 25 -1 N LEU C 22 O VAL C 66
SHEET 4 E 4 LYS C 92 TYR C 95 -1 O SER C 94 N ILE C 23
SHEET 1 F 2 ARG C 85 LEU C 86 0
SHEET 2 F 2 LYS C 89 THR C 90 -1 O LYS C 89 N LEU C 86
SHEET 1 G 4 VAL D 46 ARG D 53 0
SHEET 2 G 4 SER D 60 TYR D 68 -1 O TYR D 63 N ILE D 52
SHEET 3 G 4 ASN D 21 ASN D 25 -1 N LEU D 22 O VAL D 66
SHEET 4 G 4 LYS D 92 TYR D 95 -1 O SER D 94 N ILE D 23
SHEET 1 H 2 ARG D 85 LEU D 86 0
SHEET 2 H 2 LYS D 89 THR D 90 -1 O LYS D 89 N LEU D 86
CRYST1 74.804 74.804 147.361 90.00 90.00 120.00 P 31 2 1 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 0.013368 0.007718 0.000000 0.00000
SCALE2 0.000000 0.015436 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
