HEADER RNA BINDING PROTEIN 21-APR-18 6GD3
TITLE STRUCTURE OF HUR RRM3 IN COMPLEX WITH RNA (UAUUUA)
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*AP*UP*UP*UP*A)-3');
COMPND 8 CHAIN: P;
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 6GD3 1 JRNL
REVDAT 1 31-OCT-18 6GD3 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. 1.35 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 59206
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3025
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4086
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 228
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1946
REMARK 3 NUCLEIC ACID ATOMS : 124
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.053
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.932
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2198 ; 0.027 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1917 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3008 ; 2.330 ; 1.877
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4465 ; 1.160 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 271 ; 6.250 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 99 ;39.563 ;24.848
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 346 ;13.565 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ; 8.315 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 320 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2424 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 492 ; 0.002 ; 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): 1021 ; 2.306 ; 1.963
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1020 ; 2.296 ; 1.961
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1277 ; 3.293 ; 2.937
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1278 ; 3.292 ; 2.940
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1177 ; 3.600 ; 2.497
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1178 ; 3.599 ; 2.498
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1719 ; 5.169 ; 3.595
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2555 ; 6.702 ;24.917
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2491 ; 6.572 ;24.263
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 : NULL
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 6GD3 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_1200009547.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.007
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62913
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 6.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.360
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
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 : 2.180
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 (%): 48.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.01 M CALCIUM
REMARK 280 CHLORIDE, 0.05 M SODIUM CACODYLATE PH 6.5 AND 10 % (W/V) PEG
REMARK 280 4000, 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 39.96500
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: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, P
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 240
REMARK 465 ALA A 241
REMARK 465 MET A 242
REMARK 465 LYS A 326
REMARK 465 LYS B 323
REMARK 465 SER B 324
REMARK 465 HIS B 325
REMARK 465 LYS B 326
REMARK 465 SER C 324
REMARK 465 HIS C 325
REMARK 465 LYS C 326
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 LYS C 283 CE NZ
REMARK 470 ASP C 312 CG OD1 OD2
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 HOH A 560 O HOH A 592 1.47
REMARK 500 O HOH C 413 O HOH C 454 1.51
REMARK 500 OD1 ASN B 272 O HOH B 401 1.63
REMARK 500 OE2 GLU B 257 O HOH B 402 1.71
REMARK 500 O HOH A 620 O HOH A 628 1.78
REMARK 500 O HOH C 428 O HOH C 449 1.84
REMARK 500 ND2 ASN B 272 O HOH B 403 1.91
REMARK 500 O HOH A 519 O HOH A 582 1.98
REMARK 500 O HOH A 547 O HOH A 592 2.00
REMARK 500 OH TYR A 308 O HOH A 501 2.01
REMARK 500 O SER A 324 O HOH A 502 2.11
REMARK 500 O HOH A 624 O HOH A 633 2.16
REMARK 500 O HOH B 469 O HOH B 476 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 577 O HOH B 458 2756 1.27
REMARK 500 O HOH A 567 O HOH C 401 2655 1.47
REMARK 500 O HOH A 617 O HOH C 474 1655 2.16
REMARK 500 O HOH A 632 O HOH A 633 1455 2.16
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 TYR A 295 CG TYR A 295 CD1 -0.080
REMARK 500 GLU A 296 CG GLU A 296 CD 0.099
REMARK 500 GLU A 296 CD GLU A 296 OE1 0.077
REMARK 500 TRP B 244 CE3 TRP B 244 CZ3 0.103
REMARK 500 GLU B 297 CD GLU B 297 OE1 -0.078
REMARK 500 GLY B 307 N GLY B 307 CA 0.091
REMARK 500 TYR C 249 CE1 TYR C 249 CZ -0.102
REMARK 500 TYR C 295 CZ TYR C 295 CE2 -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 MET A 263 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG A 277 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 277 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET C 263 CG - SD - CE ANGL. DEV. = -10.7 DEGREES
REMARK 500 CYS C 284 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 U P 4 O5' - P - OP2 ANGL. DEV. = -11.1 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 ASN A 282 16.15 58.58
REMARK 500 ASN B 250 28.72 84.28
REMARK 500 ASN C 250 31.21 87.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 279 O
REMARK 620 2 HOH C 442 O 92.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 401
DBREF 6GD3 A 243 326 UNP Q15717 ELAV1_HUMAN 243 326
DBREF 6GD3 B 243 326 UNP Q15717 ELAV1_HUMAN 243 326
DBREF 6GD3 C 243 326 UNP Q15717 ELAV1_HUMAN 243 326
DBREF 6GD3 P 1 6 PDB 6GD3 6GD3 1 6
SEQADV 6GD3 GLY A 240 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 ALA A 241 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 MET A 242 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 GLY B 240 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 ALA B 241 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 MET B 242 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 GLY C 240 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 ALA C 241 UNP Q15717 EXPRESSION TAG
SEQADV 6GD3 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 P 6 U A U U U A
HET NA A 401 1
HETNAM NA SODIUM ION
FORMUL 5 NA NA 1+
FORMUL 6 HOH *297(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 LYS A 285 N ILE A 276
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 SER A 318 -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 LYS B 285 N ILE B 276
SHEET 3 AA3 4 TRP B 244 TYR B 249 -1 N ILE B 246 O VAL B 290
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 THR C 291 N ASN C 272
SHEET 3 AA5 4 TRP C 244 TYR C 249 -1 N ILE C 246 O VAL C 290
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
LINK O PHE A 279 NA NA A 401 1555 1555 2.98
LINK NA NA A 401 O HOH C 442 1555 2555 2.76
CISPEP 1 ASN C 322 LYS C 323 0 2.11
SITE 1 AC1 2 PHE A 279 ASN A 280
CRYST1 33.740 79.930 54.870 90.00 90.63 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 0.029638 0.000000 0.000327 0.00000
SCALE2 0.000000 0.012511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018226 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
