Header list of 1bwm.pdb file
Complete list - v 3 2 Bytes
HEADER IMMUNE SYSTEM 23-SEP-98 1BWM
TITLE A SINGLE-CHAIN T CELL RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ALPHA-BETA T CELL RECEPTOR (TCR) (D10));
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: VARIABLE DOMAINS FROM ALPHA AND BETA CHAINS;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: 27-RESIDUE HYDROPHILIC LINKER CONNECTS C TERMINUS OF
COMPND 8 BETA DOMAIN WITH N TERMINUS OF ALPHA DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASMIC INCLUSION BODIES;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 10 OTHER_DETAILS: SYNTHETIC GENE CONNECTS ALPHA AND BETA DOMAINS
KEYWDS IMMUNOGLOBULIN, IMMUNORECEPTOR, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.J.HARE,D.F.WYSS,E.L.REINHERZ,G.WAGNER
REVDAT 5 03-NOV-21 1BWM 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1BWM 1 VERSN
REVDAT 3 01-APR-03 1BWM 1 JRNL
REVDAT 2 17-AUG-99 1BWM 1 REMARK DBREF SEQADV
REVDAT 1 22-JUL-99 1BWM 0
JRNL AUTH B.J.HARE,D.F.WYSS,M.S.OSBURNE,P.S.KERN,E.L.REINHERZ,G.WAGNER
JRNL TITL STRUCTURE, SPECIFICITY AND CDR MOBILITY OF A CLASS II
JRNL TITL 2 RESTRICTED SINGLE-CHAIN T-CELL RECEPTOR.
JRNL REF NAT.STRUCT.BIOL. V. 6 574 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10360364
JRNL DOI 10.1038/9359
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.J.HARE,G.WAGNER
REMARK 1 TITL APPLICATION OF AUTOMATED NOE ASSIGNMENT TO THREE-DIMENSIONAL
REMARK 1 TITL 2 STRUCTURE REFINEMENT OF A 28 KD SINGLE-CHAIN T CELL RECEPTOR
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BWM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000001227.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 20 MM SODIUM ACETATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY (1H; 15N; 13C); HNCA;
REMARK 210 HN(CO)CA; HA(CA)(CO)NH; TOCSY-
REMARK 210 HSQC (15N)
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE DISTANCE VIOLATION
REMARK 210 GREATER THAN 0.5 A, NO DIHEDRAL
REMARK 210 VIOLATION GREATER THAN 5 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR
REMARK 210 SPECTROSCOPY ON UNIFORM 13C, 15N, AND FRACTIONALLY 2H-LABELED
REMARK 210 SINGLE-CHAIN TCR
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 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 GLN A 37 HG SER A 88 1.55
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 VAL A 4 107.85 -55.78
REMARK 500 1 SER A 7 105.98 -45.75
REMARK 500 1 LYS A 18 147.86 179.94
REMARK 500 1 THR A 26 52.85 -177.90
REMARK 500 1 ASN A 28 41.99 70.30
REMARK 500 1 THR A 39 -165.51 -55.64
REMARK 500 1 ILE A 46 -38.92 -140.23
REMARK 500 1 TYR A 50 -37.69 -139.28
REMARK 500 1 ALA A 52 162.44 57.42
REMARK 500 1 THR A 55 53.14 -175.08
REMARK 500 1 GLU A 56 64.82 -167.18
REMARK 500 1 LYS A 57 34.76 -155.32
REMARK 500 1 ASP A 59 -60.39 -96.30
REMARK 500 1 GLU A 80 21.82 -140.58
REMARK 500 1 LEU A 81 70.90 -168.01
REMARK 500 1 PRO A 84 35.97 -67.59
REMARK 500 1 SER A 85 27.09 -174.04
REMARK 500 1 THR A 87 178.08 -53.57
REMARK 500 1 SER A 88 -161.65 166.94
REMARK 500 1 PHE A 107 73.51 -68.84
REMARK 500 1 PRO A 110 86.70 -60.95
REMARK 500 1 LEU A 116A 143.95 61.84
REMARK 500 1 SER A 202 -53.91 -161.52
REMARK 500 1 ARG A 211 49.41 -91.91
REMARK 500 1 ALA A 227 105.53 57.92
REMARK 500 1 GLN A 301 -175.90 -63.99
REMARK 500 1 SER A 306 104.87 -44.01
REMARK 500 1 PRO A 307 -165.11 -63.16
REMARK 500 1 GLN A 308 86.97 52.65
REMARK 500 1 GLU A 314 -174.73 53.32
REMARK 500 1 GLU A 316 -168.90 -69.08
REMARK 500 1 THR A 328 28.81 -162.39
REMARK 500 1 PRO A 333 90.19 -60.03
REMARK 500 1 TYR A 335 -177.73 -175.05
REMARK 500 1 ARG A 336 -85.99 167.55
REMARK 500 1 GLN A 337 133.83 -174.23
REMARK 500 1 PRO A 339 -75.62 -64.57
REMARK 500 1 SER A 342 79.05 -151.24
REMARK 500 1 ILE A 349 -149.82 -89.46
REMARK 500 1 SER A 350 -10.88 -175.48
REMARK 500 1 ASN A 354 -10.78 71.75
REMARK 500 1 ASP A 379 88.89 60.11
REMARK 500 1 PRO A 382 -157.70 -61.02
REMARK 500 1 SER A 385 -93.27 51.92
REMARK 500 1 ALA A 386 157.89 175.70
REMARK 500 1 THR A 393 42.47 -149.92
REMARK 500 1 ALA A 408 88.96 50.42
REMARK 500 2 SER A 7 105.31 -46.89
REMARK 500 2 ARG A 9 107.39 -170.47
REMARK 500 2 LYS A 18 161.96 60.95
REMARK 500
REMARK 500 THIS ENTRY HAS 655 RAMACHANDRAN 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 ARG A 9 0.20 SIDE CHAIN
REMARK 500 1 ARG A 36 0.21 SIDE CHAIN
REMARK 500 1 ARG A 44 0.22 SIDE CHAIN
REMARK 500 1 ARG A 69 0.18 SIDE CHAIN
REMARK 500 1 ARG A 99 0.31 SIDE CHAIN
REMARK 500 1 ARG A 113 0.32 SIDE CHAIN
REMARK 500 1 ARG A 211 0.31 SIDE CHAIN
REMARK 500 1 ARG A 304 0.23 SIDE CHAIN
REMARK 500 1 ARG A 336 0.31 SIDE CHAIN
REMARK 500 1 ARG A 361 0.29 SIDE CHAIN
REMARK 500 1 ARG A 369 0.24 SIDE CHAIN
REMARK 500 1 ARG A 411 0.24 SIDE CHAIN
REMARK 500 2 ARG A 9 0.23 SIDE CHAIN
REMARK 500 2 ARG A 36 0.27 SIDE CHAIN
REMARK 500 2 ARG A 44 0.29 SIDE CHAIN
REMARK 500 2 ARG A 69 0.21 SIDE CHAIN
REMARK 500 2 ARG A 99 0.32 SIDE CHAIN
REMARK 500 2 ARG A 113 0.27 SIDE CHAIN
REMARK 500 2 ARG A 211 0.28 SIDE CHAIN
REMARK 500 2 ARG A 304 0.30 SIDE CHAIN
REMARK 500 2 ARG A 336 0.18 SIDE CHAIN
REMARK 500 2 ARG A 361 0.32 SIDE CHAIN
REMARK 500 2 ARG A 369 0.29 SIDE CHAIN
REMARK 500 2 ARG A 411 0.30 SIDE CHAIN
REMARK 500 3 ARG A 9 0.23 SIDE CHAIN
REMARK 500 3 ARG A 36 0.31 SIDE CHAIN
REMARK 500 3 ARG A 44 0.23 SIDE CHAIN
REMARK 500 3 ARG A 69 0.32 SIDE CHAIN
REMARK 500 3 ARG A 99 0.31 SIDE CHAIN
REMARK 500 3 ARG A 113 0.31 SIDE CHAIN
REMARK 500 3 ARG A 211 0.30 SIDE CHAIN
REMARK 500 3 ARG A 304 0.27 SIDE CHAIN
REMARK 500 3 ARG A 336 0.22 SIDE CHAIN
REMARK 500 3 ARG A 361 0.31 SIDE CHAIN
REMARK 500 3 ARG A 369 0.26 SIDE CHAIN
REMARK 500 3 ARG A 411 0.31 SIDE CHAIN
REMARK 500 4 ARG A 9 0.28 SIDE CHAIN
REMARK 500 4 ARG A 36 0.28 SIDE CHAIN
REMARK 500 4 ARG A 44 0.29 SIDE CHAIN
REMARK 500 4 ARG A 69 0.25 SIDE CHAIN
REMARK 500 4 ARG A 99 0.26 SIDE CHAIN
REMARK 500 4 ARG A 113 0.20 SIDE CHAIN
REMARK 500 4 ARG A 211 0.25 SIDE CHAIN
REMARK 500 4 ARG A 304 0.31 SIDE CHAIN
REMARK 500 4 ARG A 336 0.28 SIDE CHAIN
REMARK 500 4 ARG A 361 0.26 SIDE CHAIN
REMARK 500 4 ARG A 369 0.22 SIDE CHAIN
REMARK 500 4 ARG A 411 0.30 SIDE CHAIN
REMARK 500 5 ARG A 9 0.30 SIDE CHAIN
REMARK 500 5 ARG A 36 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 180 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BWM A 3 116A GB 1791255 U83243 32 141
DBREF 1BWM A 301 417 GB 5724764 U83242 29 140
SEQADV 1BWM SER A 415 GB 5724764 CYS 137 ENGINEERED MUTATION
SEQRES 1 A 249 ALA VAL THR GLN SER PRO ARG ASN LYS VAL ALA VAL THR
SEQRES 2 A 249 GLY GLY LYS VAL THR LEU SER CYS ASN GLN THR ASN ASN
SEQRES 3 A 249 HIS ASN ASN MET TYR TRP TYR ARG GLN ASP THR GLY HIS
SEQRES 4 A 249 GLY LEU ARG LEU ILE HIS TYR SER TYR GLY ALA GLY SER
SEQRES 5 A 249 THR GLU LYS GLY ASP ILE PRO ASP GLY TYR LYS ALA SER
SEQRES 6 A 249 ARG PRO SER GLN GLU ASN PHE SER LEU ILE LEU GLU LEU
SEQRES 7 A 249 ALA THR PRO SER GLN THR SER VAL TYR PHE CYS ALA SER
SEQRES 8 A 249 GLY GLY GLN GLY ARG ALA GLU GLN PHE PHE GLY PRO GLY
SEQRES 9 A 249 THR ARG LEU THR VAL LEU GLY SER ASP TYR LYS ASP ASP
SEQRES 10 A 249 ASP ASP LYS ARG SER GLY GLY GLY GLY SER GLY GLY GLY
SEQRES 11 A 249 GLY SER GLY GLY SER GLY ALA GLN GLN GLN VAL ARG GLN
SEQRES 12 A 249 SER PRO GLN SER LEU THR VAL TRP GLU GLY GLU THR THR
SEQRES 13 A 249 ILE LEU ASN CYS SER TYR GLU ASP SER THR PHE ASP TYR
SEQRES 14 A 249 PHE PRO TRP TYR ARG GLN PHE PRO GLY LYS SER PRO ALA
SEQRES 15 A 249 LEU LEU ILE ALA ILE SER LEU VAL SER ASN LYS LYS GLU
SEQRES 16 A 249 ASP GLY ARG PHE THR ILE PHE PHE ASN LYS ARG GLU LYS
SEQRES 17 A 249 LYS LEU SER LEU HIS ILE THR ASP SER GLN PRO GLY ASP
SEQRES 18 A 249 SER ALA THR TYR PHE CYS ALA ALA THR GLY SER PHE ASN
SEQRES 19 A 249 LYS LEU THR PHE GLY ALA GLY THR ARG LEU ALA VAL SER
SEQRES 20 A 249 PRO TYR
SHEET 1 B1 4 VAL A 4 GLN A 6 0
SHEET 2 B1 4 LEU A 21 ASN A 24 -1
SHEET 3 B1 4 PHE A 75 LEU A 79 -1
SHEET 4 B1 4 ALA A 67 ARG A 69 -1
SHEET 1 B2 5 LYS A 11 ALA A 13 0
SHEET 2 B2 5 THR A 112 THR A 115 1
SHEET 3 B2 5 TYR A 90 GLY A 95 -1
SHEET 4 B2 5 MET A 32 ARG A 36 -1
SHEET 5 B2 5 ARG A 44 TYR A 48 -1
SHEET 1 A1 5 ARG A 304 SER A 306 0
SHEET 2 A1 5 THR A 318 SER A 323 -1
SHEET 3 A1 5 LEU A 373 ILE A 377 -1
SHEET 4 A1 5 PHE A 362 PHE A 365 -1
SHEET 5 A1 5 LYS A 356 ASP A 358 -1
SHEET 1 A2 5 LEU A 310 VAL A 312 0
SHEET 2 A2 5 THR A 410 ALA A 413 1
SHEET 3 A2 5 ALA A 386 ALA A 391 -1
SHEET 4 A2 5 PHE A 332 ARG A 336 -1
SHEET 5 A2 5 ALA A 344 ALA A 348 -1
SSBOND 1 CYS A 23 CYS A 92 1555 1555 2.02
SSBOND 2 CYS A 322 CYS A 390 1555 1555 2.02
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 - v 3 2 Bytes