Header list of 2hgn.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 27-JUN-06 2HGN
TITLE NMR STRUCTURE OF THE THIRD QRRM DOMAIN OF HUMAN HNRNP F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN F;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: QUASI RNA RECOGNITION MOTIF 3 (QRRM3);
COMPND 5 SYNONYM: HNRNP F, NUCLEOLIN-LIKE PROTEIN MCS94-1;
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: HNRPF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B(+)
KEYWDS RNA RECOGNITION MOTIF, G-TRACT, G-QUADRUPLEX, ALTERNATIVE SPLICING,
KEYWDS 2 RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.DOMINGUEZ,F.H.-T.ALLAIN
REVDAT 4 09-MAR-22 2HGN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2HGN 1 VERSN
REVDAT 2 08-AUG-06 2HGN 1 JRNL
REVDAT 1 11-JUL-06 2HGN 0
JRNL AUTH C.DOMINGUEZ,F.H.ALLAIN
JRNL TITL NMR STRUCTURE OF THE THREE QUASI RNA RECOGNITION MOTIFS
JRNL TITL 2 (QRRMS) OF HUMAN HNRNP F AND INTERACTION STUDIES WITH BCL-X
JRNL TITL 3 G-TRACT RNA: A NOVEL MODE OF RNA RECOGNITION.
JRNL REF NUCLEIC ACIDS RES. V. 34 3634 2006
JRNL REFN ISSN 0305-1048
JRNL PMID 16885237
JRNL DOI 10.1093/NAR/GKL488
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ATNOSCANDID 1.1, AMBER 7.0
REMARK 3 AUTHORS : HERRMANN (ATNOSCANDID), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HGN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038326.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 25MM NAH2PO4, 50 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3 MM HNRNP F QRRM3 U-15N, 25MM
REMARK 210 NAH2PO4 (PH 6.2), 50MM NACL 10
REMARK 210 MM BETA-MERCAPTOETHANOL; 0.3 MM
REMARK 210 HNRNP F QRRM3 U-15N,13C, 25MM
REMARK 210 NAH2PO4 (PH 6.2), 50MM NACL, 10
REMARK 210 MM BETA-MERCAPTOETHANOL; 0.3 MM
REMARK 210 HNRNP F QRRM3 U-15N, 25MM
REMARK 210 NAH2PO4 (PH 6.2), 50MM NACL, 10
REMARK 210 MM BETA-MERCAPTOETHANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 MET A 243
REMARK 465 GLY A 244
REMARK 465 SER A 245
REMARK 465 SER A 246
REMARK 465 HIS A 247
REMARK 465 HIS A 248
REMARK 465 HIS A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 SER A 253
REMARK 465 SER A 254
REMARK 465 GLY A 255
REMARK 465 LEU A 256
REMARK 465 VAL A 257
REMARK 465 PRO A 258
REMARK 465 ARG A 259
REMARK 465 GLY A 260
REMARK 465 SER A 261
REMARK 465 HIS A 262
REMARK 465 MET A 263
REMARK 465 ALA A 264
REMARK 465 SER A 265
REMARK 465 MET A 266
REMARK 465 THR A 267
REMARK 465 GLY A 268
REMARK 465 GLY A 269
REMARK 465 GLN A 270
REMARK 465 GLN A 271
REMARK 465 MET A 272
REMARK 465 GLY A 273
REMARK 465 ARG A 274
REMARK 465 GLY A 275
REMARK 465 SER A 276
REMARK 465 GLY A 277
REMARK 465 ASP A 278
REMARK 465 SER A 279
REMARK 465 GLU A 280
REMARK 465 PHE A 281
REMARK 465 THR A 282
REMARK 465 VAL A 283
REMARK 465 GLN A 284
REMARK 465 SER A 285
REMARK 465 THR A 286
REMARK 465 SER A 368
REMARK 465 ASN A 369
REMARK 465 GLY A 370
REMARK 465 ALA A 371
REMARK 465 TYR A 372
REMARK 465 SER A 373
REMARK 465 SER A 374
REMARK 465 GLN A 375
REMARK 465 VAL A 376
REMARK 465 MET A 377
REMARK 465 GLN A 378
REMARK 465 GLY A 379
REMARK 465 MET A 380
REMARK 465 GLY A 381
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 ALA A 336 HG1 THR A 337 1.57
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 1 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 MET A 352 CA - CB - CG ANGL. DEV. = 10.3 DEGREES
REMARK 500 2 ARG A 316 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 4 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 349 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 ARG A 316 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 7 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 8 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 PHE A 308 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 8 ARG A 316 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 9 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 11 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 12 ARG A 316 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG A 349 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 12 MET A 352 CA - CB - CG ANGL. DEV. = 11.0 DEGREES
REMARK 500 13 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 14 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 15 ARG A 316 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 15 LEU A 361 CB - CG - CD1 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 1 HIS A 289 175.34 -50.12
REMARK 500 1 SER A 310 -172.15 -177.45
REMARK 500 1 PRO A 311 31.35 -58.23
REMARK 500 1 ASP A 324 6.32 -152.36
REMARK 500 1 THR A 328 -0.68 48.04
REMARK 500 1 GLU A 330 37.09 -152.55
REMARK 500 1 THR A 337 175.37 114.21
REMARK 500 1 MET A 345 47.10 -75.50
REMARK 500 1 LYS A 347 -9.48 -155.25
REMARK 500 1 ASP A 348 -70.79 20.15
REMARK 500 1 ARG A 349 23.45 -52.69
REMARK 500 1 ASN A 351 -57.52 -124.52
REMARK 500 1 HIS A 354 93.86 51.06
REMARK 500 1 ARG A 355 175.25 158.21
REMARK 500 1 GLU A 358 76.43 -69.64
REMARK 500 1 ASN A 362 26.16 -149.30
REMARK 500 2 SER A 310 -169.47 174.08
REMARK 500 2 PRO A 311 62.77 -46.96
REMARK 500 2 ASP A 324 -39.54 -179.64
REMARK 500 2 VAL A 327 -91.05 -138.44
REMARK 500 2 GLU A 330 59.73 -153.93
REMARK 500 2 THR A 337 176.30 117.32
REMARK 500 2 MET A 345 48.26 -72.32
REMARK 500 2 LYS A 347 5.32 -160.68
REMARK 500 2 ASP A 348 -39.60 11.11
REMARK 500 2 HIS A 354 72.09 126.44
REMARK 500 2 ARG A 355 -88.54 -149.44
REMARK 500 2 GLU A 358 74.96 -67.96
REMARK 500 2 ASN A 362 13.48 -149.55
REMARK 500 3 PRO A 311 31.39 -58.20
REMARK 500 3 PRO A 314 105.46 -57.63
REMARK 500 3 ILE A 319 58.90 -143.37
REMARK 500 3 ASP A 324 23.97 -161.55
REMARK 500 3 VAL A 327 -70.27 -135.65
REMARK 500 3 THR A 328 -8.13 -145.00
REMARK 500 3 THR A 337 172.91 121.87
REMARK 500 3 SER A 346 22.87 -73.28
REMARK 500 3 ASP A 348 -30.70 23.42
REMARK 500 3 ASN A 351 -67.36 -128.41
REMARK 500 3 HIS A 354 113.64 44.45
REMARK 500 3 ARG A 355 142.26 68.15
REMARK 500 3 GLU A 358 74.84 -67.69
REMARK 500 3 ASN A 362 6.37 -153.16
REMARK 500 4 HIS A 289 176.19 -57.65
REMARK 500 4 PHE A 309 -71.75 -38.69
REMARK 500 4 PRO A 311 30.62 -58.92
REMARK 500 4 ILE A 321 -175.81 172.13
REMARK 500 4 ASP A 324 16.83 -157.69
REMARK 500 4 VAL A 327 -66.67 -133.51
REMARK 500 4 THR A 328 16.19 -143.93
REMARK 500
REMARK 500 THIS ENTRY HAS 207 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 288 HIS A 289 1 149.80
REMARK 500 PHE A 309 SER A 310 1 149.01
REMARK 500 GLY A 329 GLU A 330 1 -134.21
REMARK 500 ALA A 336 THR A 337 1 145.69
REMARK 500 ARG A 349 ALA A 350 1 -139.10
REMARK 500 ARG A 355 TYR A 356 1 -132.01
REMARK 500 SER A 363 THR A 364 1 -139.72
REMARK 500 PHE A 309 SER A 310 2 146.09
REMARK 500 GLY A 329 GLU A 330 2 -139.06
REMARK 500 ALA A 336 THR A 337 2 147.15
REMARK 500 ARG A 349 ALA A 350 2 -99.25
REMARK 500 GLU A 330 ALA A 331 3 -142.07
REMARK 500 ALA A 336 THR A 337 3 143.76
REMARK 500 ARG A 349 ALA A 350 3 -97.91
REMARK 500 ASN A 351 MET A 352 3 -138.51
REMARK 500 GLN A 353 HIS A 354 3 -149.11
REMARK 500 HIS A 354 ARG A 355 3 -140.47
REMARK 500 GLY A 288 HIS A 289 4 143.91
REMARK 500 HIS A 289 CYS A 290 4 149.92
REMARK 500 ALA A 336 THR A 337 4 145.07
REMARK 500 ARG A 349 ALA A 350 4 -132.47
REMARK 500 ASN A 351 MET A 352 4 -146.80
REMARK 500 VAL A 333 GLU A 334 5 -149.57
REMARK 500 ALA A 336 THR A 337 5 147.87
REMARK 500 ARG A 349 ALA A 350 5 -131.27
REMARK 500 GLN A 353 HIS A 354 5 -126.33
REMARK 500 ASN A 362 SER A 363 5 -146.71
REMARK 500 GLY A 366 ALA A 367 5 149.77
REMARK 500 ALA A 336 THR A 337 6 145.85
REMARK 500 ARG A 349 ALA A 350 6 -55.03
REMARK 500 ARG A 355 TYR A 356 6 -121.05
REMARK 500 PHE A 309 SER A 310 7 145.69
REMARK 500 GLU A 330 ALA A 331 7 -145.58
REMARK 500 ALA A 336 THR A 337 7 148.22
REMARK 500 ARG A 349 ALA A 350 7 -105.15
REMARK 500 ASN A 362 SER A 363 7 -147.04
REMARK 500 PHE A 309 SER A 310 8 145.47
REMARK 500 GLY A 325 ARG A 326 8 -146.47
REMARK 500 THR A 328 GLY A 329 8 144.43
REMARK 500 ALA A 336 THR A 337 8 143.63
REMARK 500 ARG A 349 ALA A 350 8 -127.63
REMARK 500 ALA A 336 THR A 337 9 145.26
REMARK 500 ARG A 349 ALA A 350 9 -128.01
REMARK 500 ASN A 362 SER A 363 9 -145.27
REMARK 500 PHE A 309 SER A 310 10 148.89
REMARK 500 ALA A 336 THR A 337 10 147.34
REMARK 500 ARG A 349 ALA A 350 10 -132.06
REMARK 500 MET A 352 GLN A 353 10 -35.47
REMARK 500 GLN A 353 HIS A 354 10 -138.57
REMARK 500 PHE A 309 SER A 310 11 141.83
REMARK 500
REMARK 500 THIS ENTRY HAS 74 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 PHE A 308 0.11 SIDE CHAIN
REMARK 500 3 ARG A 326 0.08 SIDE CHAIN
REMARK 500 4 ARG A 316 0.10 SIDE CHAIN
REMARK 500 5 PHE A 309 0.09 SIDE CHAIN
REMARK 500 5 ARG A 349 0.14 SIDE CHAIN
REMARK 500 6 ARG A 349 0.18 SIDE CHAIN
REMARK 500 7 PHE A 309 0.08 SIDE CHAIN
REMARK 500 8 TYR A 298 0.06 SIDE CHAIN
REMARK 500 8 PHE A 308 0.09 SIDE CHAIN
REMARK 500 8 ARG A 349 0.16 SIDE CHAIN
REMARK 500 9 ARG A 294 0.13 SIDE CHAIN
REMARK 500 9 PHE A 309 0.10 SIDE CHAIN
REMARK 500 9 ARG A 349 0.14 SIDE CHAIN
REMARK 500 10 PHE A 308 0.11 SIDE CHAIN
REMARK 500 11 PHE A 309 0.07 SIDE CHAIN
REMARK 500 11 ARG A 349 0.18 SIDE CHAIN
REMARK 500 12 PHE A 309 0.07 SIDE CHAIN
REMARK 500 13 PHE A 309 0.08 SIDE CHAIN
REMARK 500 15 ARG A 326 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HGL RELATED DB: PDB
REMARK 900 RELATED ID: 2HGM RELATED DB: PDB
DBREF 2HGN A 277 381 UNP P52597 HNRPF_HUMAN 277 381
SEQADV 2HGN MET A 243 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLY A 244 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN SER A 245 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN SER A 246 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN HIS A 247 UNP P52597 EXPRESSION TAG
SEQADV 2HGN HIS A 248 UNP P52597 EXPRESSION TAG
SEQADV 2HGN HIS A 249 UNP P52597 EXPRESSION TAG
SEQADV 2HGN HIS A 250 UNP P52597 EXPRESSION TAG
SEQADV 2HGN HIS A 251 UNP P52597 EXPRESSION TAG
SEQADV 2HGN HIS A 252 UNP P52597 EXPRESSION TAG
SEQADV 2HGN SER A 253 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN SER A 254 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLY A 255 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN LEU A 256 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN VAL A 257 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN PRO A 258 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN ARG A 259 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLY A 260 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN SER A 261 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN HIS A 262 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN MET A 263 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN ALA A 264 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN SER A 265 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN MET A 266 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN THR A 267 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLY A 268 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLY A 269 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLN A 270 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLN A 271 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN MET A 272 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLY A 273 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN ARG A 274 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN GLY A 275 UNP P52597 CLONING ARTIFACT
SEQADV 2HGN SER A 276 UNP P52597 CLONING ARTIFACT
SEQRES 1 A 139 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 139 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 139 GLY GLN GLN MET GLY ARG GLY SER GLY ASP SER GLU PHE
SEQRES 4 A 139 THR VAL GLN SER THR THR GLY HIS CYS VAL HIS MET ARG
SEQRES 5 A 139 GLY LEU PRO TYR LYS ALA THR GLU ASN ASP ILE TYR ASN
SEQRES 6 A 139 PHE PHE SER PRO LEU ASN PRO VAL ARG VAL HIS ILE GLU
SEQRES 7 A 139 ILE GLY PRO ASP GLY ARG VAL THR GLY GLU ALA ASP VAL
SEQRES 8 A 139 GLU PHE ALA THR HIS GLU GLU ALA VAL ALA ALA MET SER
SEQRES 9 A 139 LYS ASP ARG ALA ASN MET GLN HIS ARG TYR ILE GLU LEU
SEQRES 10 A 139 PHE LEU ASN SER THR THR GLY ALA SER ASN GLY ALA TYR
SEQRES 11 A 139 SER SER GLN VAL MET GLN GLY MET GLY
HELIX 1 1 THR A 301 SER A 310 1 10
HELIX 2 2 ALA A 336 MET A 345 1 10
SHEET 1 A 4 ARG A 316 HIS A 318 0
SHEET 2 A 4 ASP A 332 GLU A 334 -1 O GLU A 334 N ARG A 316
SHEET 3 A 4 VAL A 291 HIS A 292 -1 N VAL A 291 O VAL A 333
SHEET 4 A 4 PHE A 360 LEU A 361 -1 O PHE A 360 N HIS A 292
CISPEP 1 GLY A 366 ALA A 367 1 2.06
CISPEP 2 MET A 352 GLN A 353 2 20.83
CISPEP 3 GLY A 366 ALA A 367 2 -0.89
CISPEP 4 GLY A 329 GLU A 330 3 -16.28
CISPEP 5 ARG A 355 TYR A 356 3 -22.14
CISPEP 6 MET A 352 GLN A 353 5 27.92
CISPEP 7 THR A 287 GLY A 288 6 1.45
CISPEP 8 GLY A 366 ALA A 367 7 12.34
CISPEP 9 GLY A 288 HIS A 289 8 -25.05
CISPEP 10 THR A 287 GLY A 288 9 6.88
CISPEP 11 GLY A 288 HIS A 289 9 12.86
CISPEP 12 GLY A 366 ALA A 367 9 7.55
CISPEP 13 GLY A 366 ALA A 367 10 1.99
CISPEP 14 GLY A 366 ALA A 367 11 -7.81
CISPEP 15 THR A 287 GLY A 288 12 13.52
CISPEP 16 GLY A 366 ALA A 367 15 -1.55
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes