HEADER RNA BINDING PROTEIN 21-APR-18 6GD2
TITLE STRUCTURE OF HUR RRM3 IN COMPLEX WITH RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELAV-LIKE PROTEIN 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: HU-ANTIGEN R,HUR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RNA (5'-R(P*UP*UP*UP*AP*UP*UP*U)-3');
COMPND 8 CHAIN: D;
COMPND 9 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 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PABIS,M.SATTLER
REVDAT 2 15-MAY-19 6GD2 1 JRNL
REVDAT 1 31-OCT-18 6GD2 0
JRNL AUTH M.PABIS,G.M.POPOWICZ,R.STEHLE,D.FERNANDEZ-RAMOS,S.ASAMI,
JRNL AUTH 2 L.WARNER,S.M.GARCIA-MAURINO,A.SCHLUNDT,M.L.MARTINEZ-CHANTAR,
JRNL AUTH 3 I.DIAZ-MORENO,M.SATTLER
JRNL TITL HUR BIOLOGICAL FUNCTION INVOLVES RRM3-MEDIATED DIMERIZATION
JRNL TITL 2 AND RNA BINDING BY ALL THREE RRMS.
JRNL REF NUCLEIC ACIDS RES. V. 47 1011 2019
JRNL REFN ESSN 1362-4962
JRNL PMID 30418581
JRNL DOI 10.1093/NAR/GKY1138
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 21702
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1159
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1528
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1900
REMARK 3 NUCLEIC ACID ATOMS : 142
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.129
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.520
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2167 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1878 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2965 ; 1.823 ; 1.874
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4369 ; 1.145 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 261 ; 6.128 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 98 ;39.496 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 335 ;16.339 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ; 9.887 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2370 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 479 ; 0.001 ; 0.020
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): 996 ; 2.310 ; 2.467
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 995 ; 2.303 ; 2.465
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1246 ; 3.433 ; 3.674
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1247 ; 3.433 ; 3.676
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1171 ; 3.164 ; 3.031
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1170 ; 3.150 ; 3.028
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1710 ; 4.852 ; 4.408
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2455 ; 6.927 ;30.293
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2454 ; 6.921 ;30.289
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6GD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009552.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23114
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 8.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.060
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 : 2.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, MOLREP
REMARK 200 STARTING MODEL: 6GD1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 10% (W/V) PEG
REMARK 280 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.24000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 A 324
REMARK 465 HIS A 325
REMARK 465 LYS A 326
REMARK 465 GLY B 240
REMARK 465 ALA B 241
REMARK 465 LYS B 323
REMARK 465 SER B 324
REMARK 465 HIS B 325
REMARK 465 LYS B 326
REMARK 465 GLY C 240
REMARK 465 ALA C 241
REMARK 465 THR C 321
REMARK 465 ASN C 322
REMARK 465 LYS C 323
REMARK 465 SER C 324
REMARK 465 HIS C 325
REMARK 465 LYS C 326
REMARK 465 A D -2
REMARK 465 U D -1
REMARK 465 U D 0
REMARK 465 U D 8
REMARK 465 A D 9
REMARK 465 U D 10
REMARK 465 U D 11
REMARK 465 U D 12
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 A 323 CG CD CE NZ
REMARK 470 MET C 242 CG SD CE
REMARK 470 GLU C 296 CD OE1 OE2
REMARK 470 LYS C 320 CG CD CE NZ
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 ND2 ASN B 294 O HOH B 401 2.11
REMARK 500 O HOH C 407 O HOH C 469 2.13
REMARK 500 OE1 GLN C 253 O HOH C 401 2.18
REMARK 500 O MET B 242 O HOH B 402 2.19
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 ASN A 250 23.55 95.18
REMARK 500 ASN B 250 25.75 87.64
REMARK 500 ASN B 280 -73.77 -73.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 470 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B 464 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH C 480 DISTANCE = 6.14 ANGSTROMS
DBREF 6GD2 A 243 326 UNP Q15717 ELAV1_HUMAN 243 326
DBREF 6GD2 B 243 326 UNP Q15717 ELAV1_HUMAN 243 326
DBREF 6GD2 C 243 326 UNP Q15717 ELAV1_HUMAN 243 326
DBREF 6GD2 D -2 12 PDB 6GD2 6GD2 -2 12
SEQADV 6GD2 GLY A 240 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 ALA A 241 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 MET A 242 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 GLY B 240 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 ALA B 241 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 MET B 242 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 GLY C 240 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 ALA C 241 UNP Q15717 EXPRESSION TAG
SEQADV 6GD2 MET C 242 UNP Q15717 EXPRESSION TAG
SEQRES 1 A 87 GLY ALA MET GLY TRP CYS ILE PHE ILE TYR ASN LEU GLY
SEQRES 2 A 87 GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY
SEQRES 3 A 87 PRO PHE GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP
SEQRES 4 A 87 PHE ASN THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR
SEQRES 5 A 87 MET THR ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER
SEQRES 6 A 87 LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL
SEQRES 7 A 87 SER PHE LYS THR ASN LYS SER HIS LYS
SEQRES 1 B 87 GLY ALA MET GLY TRP CYS ILE PHE ILE TYR ASN LEU GLY
SEQRES 2 B 87 GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY
SEQRES 3 B 87 PRO PHE GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP
SEQRES 4 B 87 PHE ASN THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR
SEQRES 5 B 87 MET THR ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER
SEQRES 6 B 87 LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL
SEQRES 7 B 87 SER PHE LYS THR ASN LYS SER HIS LYS
SEQRES 1 C 87 GLY ALA MET GLY TRP CYS ILE PHE ILE TYR ASN LEU GLY
SEQRES 2 C 87 GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY
SEQRES 3 C 87 PRO PHE GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP
SEQRES 4 C 87 PHE ASN THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR
SEQRES 5 C 87 MET THR ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER
SEQRES 6 C 87 LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL
SEQRES 7 C 87 SER PHE LYS THR ASN LYS SER HIS LYS
SEQRES 1 D 15 A U U U U U A U U U U A U
SEQRES 2 D 15 U U
FORMUL 5 HOH *230(H2 O)
HELIX 1 AA1 ASP A 256 GLY A 265 1 10
HELIX 2 AA2 PRO A 266 GLY A 268 5 3
HELIX 3 AA3 ASN A 294 ASN A 306 1 13
HELIX 4 AA4 ASP B 256 GLY B 265 1 10
HELIX 5 AA5 PRO B 266 GLY B 268 5 3
HELIX 6 AA6 ASN B 294 ASN B 306 1 13
HELIX 7 AA7 ASP C 256 GLY C 265 1 10
HELIX 8 AA8 PRO C 266 GLY C 268 5 3
HELIX 9 AA9 ASN C 294 ASN C 306 1 13
SHEET 1 AA1 4 VAL A 270 ARG A 277 0
SHEET 2 AA1 4 CYS A 284 MET A 292 -1 O THR A 291 N ASN A 272
SHEET 3 AA1 4 TRP A 244 TYR A 249 -1 N ILE A 246 O VAL A 290
SHEET 4 AA1 4 GLN A 316 PHE A 319 -1 O SER A 318 N PHE A 247
SHEET 1 AA2 2 ARG A 309 LEU A 310 0
SHEET 2 AA2 2 LYS A 313 ILE A 314 -1 O LYS A 313 N LEU A 310
SHEET 1 AA3 4 VAL B 270 ARG B 277 0
SHEET 2 AA3 4 CYS B 284 MET B 292 -1 O PHE B 289 N LYS B 274
SHEET 3 AA3 4 TRP B 244 TYR B 249 -1 N TRP B 244 O MET B 292
SHEET 4 AA3 4 GLN B 316 PHE B 319 -1 O SER B 318 N PHE B 247
SHEET 1 AA4 2 ARG B 309 LEU B 310 0
SHEET 2 AA4 2 LYS B 313 ILE B 314 -1 O LYS B 313 N LEU B 310
SHEET 1 AA5 4 VAL C 270 ARG C 277 0
SHEET 2 AA5 4 CYS C 284 MET C 292 -1 O LYS C 285 N ILE C 276
SHEET 3 AA5 4 TRP C 244 TYR C 249 -1 N TRP C 244 O MET C 292
SHEET 4 AA5 4 GLN C 316 PHE C 319 -1 O SER C 318 N PHE C 247
SHEET 1 AA6 2 ARG C 309 LEU C 310 0
SHEET 2 AA6 2 LYS C 313 ILE C 314 -1 O LYS C 313 N LEU C 310
CISPEP 1 ASN A 322 LYS A 323 0 19.31
CRYST1 34.120 80.480 54.440 90.00 90.69 90.00 P 1 21 1 6
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 0.029308 0.000000 0.000351 0.00000
SCALE2 0.000000 0.012425 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018370 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
