Header list of 1kld.pdb file
Complete list - v 29 2 Bytes
HEADER GROWTH FACTOR 16-JAN-96 1KLD
TITLE SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 18-33 OF 33 STRUCTURES
SPLIT 1KLA 1KLD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFORMING GROWTH FACTOR-BETA 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TGF-B1;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: 1 MM (IN DIMER), PH 4.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: OVARY;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS GROWTH FACTOR, MITOGEN, GLYCOPROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR A.P.HINCK,S.J.ARCHER,S.W.QIAN,A.B.ROBERTS,M.B.SPORN,J.A.WEATHERBEE,
AUTHOR 2 M.L.-S.TSANG,R.LUCAS,B.-L.ZHANG,J.WENKER,D.A.TORCHIA
REVDAT 5 29-NOV-17 1KLD 1 HELIX
REVDAT 4 24-NOV-10 1KLD 1 REMARK
REVDAT 3 24-FEB-09 1KLD 1 VERSN
REVDAT 2 01-APR-03 1KLD 1 JRNL
REVDAT 1 17-AUG-96 1KLD 0
JRNL AUTH A.P.HINCK,S.J.ARCHER,S.W.QIAN,A.B.ROBERTS,M.B.SPORN,
JRNL AUTH 2 J.A.WEATHERBEE,M.L.TSANG,R.LUCAS,B.L.ZHANG,J.WENKER,
JRNL AUTH 3 D.A.TORCHIA
JRNL TITL TRANSFORMING GROWTH FACTOR BETA 1: THREE-DIMENSIONAL
JRNL TITL 2 STRUCTURE IN SOLUTION AND COMPARISON WITH THE X-RAY
JRNL TITL 3 STRUCTURE OF TRANSFORMING GROWTH FACTOR BETA 2.
JRNL REF BIOCHEMISTRY V. 35 8517 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8679613
JRNL DOI 10.1021/BI9604946
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KLD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174453.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.1
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 33
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS ENTRY CONTAINS 18 - 33 OF 33 MODELS. 1 MM (IN DIMER).
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 18 LEU A 2 59.88 -108.64
REMARK 500 18 PHE A 8 42.80 -84.83
REMARK 500 18 SER A 9 -153.20 -108.08
REMARK 500 18 THR A 11 -167.16 -117.02
REMARK 500 18 GLU A 12 130.71 64.69
REMARK 500 18 CYS A 15 89.35 -55.61
REMARK 500 18 LEU A 20 45.83 -151.78
REMARK 500 18 PHE A 24 -54.98 -15.59
REMARK 500 18 TYR A 39 168.23 178.54
REMARK 500 18 ASN A 42 177.19 62.02
REMARK 500 18 PHE A 43 177.66 178.43
REMARK 500 18 PRO A 47 -159.36 -78.59
REMARK 500 18 PRO A 49 -168.13 -75.45
REMARK 500 18 TRP A 52 -157.67 -58.01
REMARK 500 18 SER A 53 44.24 -85.02
REMARK 500 18 ALA A 75 -173.74 -53.03
REMARK 500 18 PRO A 76 -162.29 -77.24
REMARK 500 18 PRO A 85 -162.16 -74.24
REMARK 500 18 LEU A 86 109.13 -164.84
REMARK 500 18 ILE A 88 -161.89 -116.47
REMARK 500 18 VAL A 89 111.82 -164.06
REMARK 500 18 ARG A 94 -3.69 -145.21
REMARK 500 18 GLU A 99 -160.12 -129.49
REMARK 500 18 SER A 108 121.66 165.82
REMARK 500 18 LYS A 110 -163.11 -169.82
REMARK 500 18 LEU B 2 60.45 -109.40
REMARK 500 18 PHE B 8 42.11 -84.74
REMARK 500 18 SER B 9 -152.96 -107.27
REMARK 500 18 THR B 11 -167.53 -117.13
REMARK 500 18 GLU B 12 130.70 65.17
REMARK 500 18 CYS B 15 89.34 -55.40
REMARK 500 18 LEU B 20 45.85 -152.39
REMARK 500 18 PHE B 24 -54.98 -15.06
REMARK 500 18 TYR B 39 167.62 177.69
REMARK 500 18 ASN B 42 177.36 62.24
REMARK 500 18 PHE B 43 178.03 178.32
REMARK 500 18 PRO B 47 -159.50 -78.86
REMARK 500 18 PRO B 49 -168.14 -75.30
REMARK 500 18 TRP B 52 -157.52 -57.79
REMARK 500 18 SER B 53 43.44 -85.12
REMARK 500 18 ALA B 75 -174.42 -52.73
REMARK 500 18 PRO B 76 -162.20 -76.86
REMARK 500 18 PRO B 85 -162.58 -74.13
REMARK 500 18 LEU B 86 109.11 -164.42
REMARK 500 18 ILE B 88 -161.65 -116.37
REMARK 500 18 VAL B 89 111.61 -164.08
REMARK 500 18 ARG B 94 -3.64 -144.04
REMARK 500 18 GLU B 99 -160.10 -129.67
REMARK 500 18 SER B 108 121.68 166.35
REMARK 500 18 LYS B 110 -163.33 -169.88
REMARK 500
REMARK 500 THIS ENTRY HAS 819 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 18 ARG A 18 0.31 SIDE CHAIN
REMARK 500 18 ARG A 25 0.22 SIDE CHAIN
REMARK 500 18 ARG A 94 0.20 SIDE CHAIN
REMARK 500 18 ARG A 107 0.28 SIDE CHAIN
REMARK 500 18 ARG B 18 0.31 SIDE CHAIN
REMARK 500 18 ARG B 25 0.14 SIDE CHAIN
REMARK 500 18 ARG B 94 0.19 SIDE CHAIN
REMARK 500 18 ARG B 107 0.27 SIDE CHAIN
REMARK 500 19 ARG A 18 0.32 SIDE CHAIN
REMARK 500 19 ARG A 25 0.30 SIDE CHAIN
REMARK 500 19 ARG A 94 0.17 SIDE CHAIN
REMARK 500 19 ARG A 107 0.22 SIDE CHAIN
REMARK 500 19 ARG B 18 0.32 SIDE CHAIN
REMARK 500 19 ARG B 25 0.31 SIDE CHAIN
REMARK 500 19 ARG B 94 0.17 SIDE CHAIN
REMARK 500 19 ARG B 107 0.23 SIDE CHAIN
REMARK 500 20 ARG A 18 0.23 SIDE CHAIN
REMARK 500 20 ARG A 25 0.12 SIDE CHAIN
REMARK 500 20 ARG A 94 0.31 SIDE CHAIN
REMARK 500 20 ARG A 107 0.28 SIDE CHAIN
REMARK 500 20 ARG B 18 0.23 SIDE CHAIN
REMARK 500 20 ARG B 25 0.18 SIDE CHAIN
REMARK 500 20 ARG B 94 0.31 SIDE CHAIN
REMARK 500 20 ARG B 107 0.27 SIDE CHAIN
REMARK 500 21 ARG A 18 0.26 SIDE CHAIN
REMARK 500 21 ARG A 25 0.31 SIDE CHAIN
REMARK 500 21 ARG A 94 0.21 SIDE CHAIN
REMARK 500 21 ARG A 107 0.30 SIDE CHAIN
REMARK 500 21 ARG B 18 0.26 SIDE CHAIN
REMARK 500 21 ARG B 25 0.31 SIDE CHAIN
REMARK 500 21 ARG B 94 0.21 SIDE CHAIN
REMARK 500 21 ARG B 107 0.30 SIDE CHAIN
REMARK 500 22 ARG A 18 0.26 SIDE CHAIN
REMARK 500 22 ARG A 25 0.30 SIDE CHAIN
REMARK 500 22 ARG A 107 0.18 SIDE CHAIN
REMARK 500 22 ARG B 18 0.26 SIDE CHAIN
REMARK 500 22 ARG B 25 0.30 SIDE CHAIN
REMARK 500 22 ARG B 94 0.10 SIDE CHAIN
REMARK 500 22 ARG B 107 0.17 SIDE CHAIN
REMARK 500 23 ARG A 18 0.25 SIDE CHAIN
REMARK 500 23 ARG A 25 0.31 SIDE CHAIN
REMARK 500 23 ARG A 94 0.26 SIDE CHAIN
REMARK 500 23 ARG A 107 0.30 SIDE CHAIN
REMARK 500 23 ARG B 18 0.25 SIDE CHAIN
REMARK 500 23 ARG B 25 0.32 SIDE CHAIN
REMARK 500 23 ARG B 94 0.26 SIDE CHAIN
REMARK 500 23 ARG B 107 0.31 SIDE CHAIN
REMARK 500 24 ARG A 18 0.32 SIDE CHAIN
REMARK 500 24 ARG A 25 0.26 SIDE CHAIN
REMARK 500 24 ARG A 94 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 125 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KLA RELATED DB: PDB
REMARK 900 RELATED ID: 1KLC RELATED DB: PDB
DBREF 1KLD A 1 112 UNP P01137 TGFB1_HUMAN 279 390
DBREF 1KLD B 1 112 UNP P01137 TGFB1_HUMAN 279 390
SEQRES 1 A 112 ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS
SEQRES 2 A 112 ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS
SEQRES 3 A 112 ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR
SEQRES 4 A 112 HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP
SEQRES 5 A 112 SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR
SEQRES 6 A 112 ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS
SEQRES 7 A 112 VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR
SEQRES 8 A 112 VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET
SEQRES 9 A 112 ILE VAL ARG SER CYS LYS CYS SER
SEQRES 1 B 112 ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS
SEQRES 2 B 112 ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS
SEQRES 3 B 112 ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR
SEQRES 4 B 112 HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP
SEQRES 5 B 112 SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR
SEQRES 6 B 112 ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS
SEQRES 7 B 112 VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR
SEQRES 8 B 112 VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET
SEQRES 9 B 112 ILE VAL ARG SER CYS LYS CYS SER
HELIX 1 1 GLN A 57 HIS A 68 1 12
HELIX 2 2 GLN B 57 HIS B 68 1 12
SHEET 1 A 2 CYS A 16 ARG A 18 0
SHEET 2 A 2 PHE A 43 LEU A 45 -1 N LEU A 45 O CYS A 16
SHEET 1 B 2 TYR A 90 VAL A 92 0
SHEET 2 B 2 LYS A 95 LYS A 97 -1 N LYS A 97 O TYR A 90
SHEET 1 C 2 CYS B 16 ARG B 18 0
SHEET 2 C 2 PHE B 43 LEU B 45 -1 N LEU B 45 O CYS B 16
SHEET 1 D 2 TYR B 90 VAL B 92 0
SHEET 2 D 2 LYS B 95 LYS B 97 -1 N LYS B 97 O TYR B 90
SHEET 1 E 2 CYS A 77 ALA A 82 0
SHEET 2 E 2 SER A 108 SER A 112 -1 N SER A 112 O CYS A 77
SHEET 1 F 2 CYS B 77 ALA B 82 0
SHEET 2 F 2 SER B 108 SER B 112 -1 N SER B 112 O CYS B 77
SSBOND 1 CYS A 7 CYS A 16 1555 1555 2.02
SSBOND 2 CYS A 15 CYS A 78 1555 1555 2.03
SSBOND 3 CYS A 44 CYS A 109 1555 1555 2.02
SSBOND 4 CYS A 48 CYS A 111 1555 1555 2.02
SSBOND 5 CYS A 77 CYS B 77 1555 1555 2.02
SSBOND 6 CYS B 7 CYS B 16 1555 1555 2.02
SSBOND 7 CYS B 15 CYS B 78 1555 1555 2.03
SSBOND 8 CYS B 44 CYS B 109 1555 1555 2.02
SSBOND 9 CYS B 48 CYS B 111 1555 1555 2.02
CISPEP 1 GLU A 35 PRO A 36 18 -0.08
CISPEP 2 GLU B 35 PRO B 36 18 -0.04
CISPEP 3 GLU A 35 PRO A 36 19 0.30
CISPEP 4 GLU B 35 PRO B 36 19 0.17
CISPEP 5 GLU A 35 PRO A 36 20 -0.16
CISPEP 6 GLU B 35 PRO B 36 20 -0.09
CISPEP 7 GLU A 35 PRO A 36 21 -0.26
CISPEP 8 GLU B 35 PRO B 36 21 -0.20
CISPEP 9 GLU A 35 PRO A 36 22 -0.12
CISPEP 10 GLU B 35 PRO B 36 22 -0.15
CISPEP 11 GLU A 35 PRO A 36 23 -0.36
CISPEP 12 GLU B 35 PRO B 36 23 -0.20
CISPEP 13 GLU A 35 PRO A 36 24 -0.09
CISPEP 14 GLU B 35 PRO B 36 24 -0.01
CISPEP 15 GLU A 35 PRO A 36 25 0.12
CISPEP 16 GLU B 35 PRO B 36 25 -0.02
CISPEP 17 GLU A 35 PRO A 36 26 -0.60
CISPEP 18 GLU B 35 PRO B 36 26 -0.48
CISPEP 19 GLU A 35 PRO A 36 27 -0.13
CISPEP 20 GLU B 35 PRO B 36 27 -0.19
CISPEP 21 GLU A 35 PRO A 36 28 -0.07
CISPEP 22 GLU B 35 PRO B 36 28 -0.07
CISPEP 23 GLU A 35 PRO A 36 29 -0.14
CISPEP 24 GLU B 35 PRO B 36 29 0.03
CISPEP 25 GLU A 35 PRO A 36 30 0.26
CISPEP 26 GLU B 35 PRO B 36 30 0.25
CISPEP 27 GLU A 35 PRO A 36 31 0.02
CISPEP 28 GLU B 35 PRO B 36 31 0.01
CISPEP 29 GLU A 35 PRO A 36 32 -0.46
CISPEP 30 GLU B 35 PRO B 36 32 -0.42
CISPEP 31 GLU A 35 PRO A 36 33 0.11
CISPEP 32 GLU B 35 PRO B 36 33 0.09
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 18
Complete list - v 29 2 Bytes