Header list of 1lmj.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 02-MAY-02 1LMJ
TITLE NMR STUDY OF THE FIBRILLIN-1 CBEGF12-13 PAIR OF CA2+ BINDING EPIDERMAL
TITLE 2 GROWTH FACTOR-LIKE DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRILLIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CBEGF12-13;
COMPND 5 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: FBN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: NM554 AND BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS EGF, CALCIUM, MICROFIBRIL, NEONATAL, MARFAN SYNDROME, CONNECTIVE
KEYWDS 2 TISSUE, EXTRACELLULAR MATRIX, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR R.S.SMALLRIDGE,P.WHITEMAN,J.M.WERNER,I.D.CAMPBELL,P.A.HANDFORD,
AUTHOR 2 A.K.DOWNING
REVDAT 3 23-FEB-22 1LMJ 1 REMARK LINK
REVDAT 2 24-FEB-09 1LMJ 1 VERSN
REVDAT 1 29-APR-03 1LMJ 0
JRNL AUTH R.S.SMALLRIDGE,P.WHITEMAN,J.M.WERNER,I.D.CAMPBELL,
JRNL AUTH 2 P.A.HANDFORD,A.K.DOWNING
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF A CALCIUM BINDING
JRNL TITL 2 EPIDERMAL GROWTH FACTOR-LIKE DOMAIN PAIR FROM THE NEONATAL
JRNL TITL 3 REGION OF HUMAN FIBRILLIN-1.
JRNL REF J.BIOL.CHEM. V. 278 12199 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12511552
JRNL DOI 10.1074/JBC.M208266200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.81, X-PLOR 3.81
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 1892 DISTANCE CONSTRAINTS INCLUDING 411 AMBIGUOUS CONSTRAINTS, 26
REMARK 3 TORSION ANGLE PHI RESTRAINTS, 24 RESTRAINTS FOR 12 HYDROGEN BONDS
REMARK 3
REMARK 3 RMSD FROM EXPERIMENTAL RESTRAINTS
REMARK 3 ALL 0.013+/-0.001
REMARK 3 (1932)
REMARK 3 INTRARESIDUE 0.009+/-0.002
REMARK 3 (504)
REMARK 3 SEQUENTIAL 0.011+/-0.002
REMARK 3 (388)
REMARK 3 SHORT-RANGE
REMARK 3 (I-J<=4) (211) 0.015+/-0.003
REMARK 3 LONG-RANGE 0.013+/-0.002
REMARK 3 (378)
REMARK 3 AMBIGUOUS 0.015+/-0.002
REMARK 3 (411)
REMARK 3 H-BONDS 0.014+/-0.004
REMARK 3 (24)
REMARK 3 CALCIUM 0.012+/-0.005
REMARK 3 (16)
REMARK 3 RMSD PHI REST. 0.177+/-0.093
REMARK 3 (26)
REMARK 4
REMARK 4 1LMJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000016086.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 306
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20 MM CACL2, 4.55 MM TRIS
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20 MM CACL2, 4.55 MM TRIS, 3 MM
REMARK 210 PROTEIN; 20 MM CACL2, 4.55 MM
REMARK 210 TRIS, 3.6 MM PROTEIN; 20 MM
REMARK 210 CACL2, 4.55 MM TRIS, 3.8 MM 15N-
REMARK 210 PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HMQC-J; HSQC
REMARK 210 (SLOW HN)
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA
REMARK 210 SPECTROMETER MANUFACTURER : GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6
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 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 ASP A 49 H GLN A 52 1.52
REMARK 500 O GLY A 34 H ILE A 48 1.54
REMARK 500 O GLY A 38 H MET A 42 1.56
REMARK 500 O ASP A 13 H GLY A 16 1.57
REMARK 500 O ILE A 5 HD22 ASN A 22 1.58
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 ASP A 4 68.52 39.20
REMARK 500 1 ARG A 17 -50.39 173.21
REMARK 500 1 ASP A 26 -178.38 167.30
REMARK 500 1 LYS A 30 74.33 -117.88
REMARK 500 1 CYS A 31 -179.71 -46.06
REMARK 500 1 ASP A 32 -141.53 -106.62
REMARK 500 1 GLU A 33 -92.32 -23.10
REMARK 500 1 SER A 37 114.76 -33.96
REMARK 500 1 MET A 42 -81.23 178.73
REMARK 500 1 LYS A 43 33.49 178.01
REMARK 500 1 ASN A 44 -157.97 -85.21
REMARK 500 1 ASP A 47 131.01 -10.91
REMARK 500 1 CYS A 58 26.98 44.01
REMARK 500 1 THR A 66 -165.55 -120.01
REMARK 500 1 SER A 69 -178.67 169.95
REMARK 500 1 PRO A 75 -169.30 -71.85
REMARK 500 1 PRO A 76 178.81 -43.22
REMARK 500 1 HIS A 78 -127.95 -104.23
REMARK 500 1 GLN A 79 59.90 -150.53
REMARK 500 1 ASN A 83 21.21 -146.95
REMARK 500 1 SER A 85 91.93 75.57
REMARK 500 1 ALA A 86 103.81 150.61
REMARK 500 2 GLU A 7 -52.91 68.53
REMARK 500 2 ILE A 10 -37.69 -39.92
REMARK 500 2 ARG A 17 -50.79 178.42
REMARK 500 2 ASP A 26 -167.39 169.13
REMARK 500 2 GLU A 28 -145.59 -144.74
REMARK 500 2 LYS A 30 67.82 -105.82
REMARK 500 2 CYS A 31 175.90 -45.40
REMARK 500 2 ASP A 32 -93.15 -72.86
REMARK 500 2 GLU A 33 -39.87 -141.95
REMARK 500 2 MET A 40 -31.79 176.69
REMARK 500 2 MET A 42 -21.15 104.62
REMARK 500 2 LYS A 43 100.32 -171.38
REMARK 500 2 ASN A 44 33.72 -158.98
REMARK 500 2 CYS A 45 106.74 9.52
REMARK 500 2 ASP A 47 105.30 -2.10
REMARK 500 2 ILE A 48 174.46 -50.55
REMARK 500 2 CYS A 58 24.66 48.97
REMARK 500 2 ARG A 59 61.52 -65.22
REMARK 500 2 ASN A 65 109.77 -47.83
REMARK 500 2 SER A 69 178.61 158.06
REMARK 500 2 PRO A 76 -28.18 -35.37
REMARK 500 2 HIS A 78 -129.20 -91.85
REMARK 500 2 ASN A 83 -1.24 72.62
REMARK 500 2 SER A 85 84.79 65.77
REMARK 500 2 ALA A 86 98.45 156.59
REMARK 500 3 ASP A 4 66.54 -177.90
REMARK 500 3 ARG A 17 -29.70 174.11
REMARK 500 3 ASP A 26 -174.22 167.42
REMARK 500
REMARK 500 THIS ENTRY HAS 566 RAMACHANDRAN OUTLIERS.
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 CA A 101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 4 OD1
REMARK 620 2 ILE A 5 O 115.3
REMARK 620 3 GLU A 7 OE2 139.8 54.9
REMARK 620 4 GLU A 7 OE1 168.4 66.9 51.4
REMARK 620 5 ASN A 22 OD1 68.8 89.5 139.5 100.2
REMARK 620 6 ASN A 22 ND2 115.8 57.4 91.9 54.8 49.1
REMARK 620 7 THR A 23 O 78.0 155.3 101.2 104.5 115.1 137.9
REMARK 620 8 THR A 23 N 93.6 137.6 119.7 79.0 72.0 82.8 55.9
REMARK 620 9 ASP A 26 O 122.2 120.3 70.8 60.3 124.6 106.7 44.4 54.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 47 OD2
REMARK 620 2 ILE A 48 O 108.2
REMARK 620 3 GLU A 50 OE1 138.4 103.0
REMARK 620 4 GLU A 50 OE2 154.8 86.2 51.5
REMARK 620 5 ASN A 65 OD1 66.0 98.3 83.0 133.8
REMARK 620 6 ASN A 65 ND2 105.2 57.9 69.5 100.0 49.2
REMARK 620 7 THR A 66 O 54.9 161.6 89.2 112.2 69.2 115.8
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EMO RELATED DB: PDB
REMARK 900 FIBRILLIN-1 CBEGF32-33
REMARK 900 RELATED ID: 1HJ7 RELATED DB: PDB
REMARK 900 LDL RECEPTOR CBEGF AB
DBREF 1LMJ A 3 88 UNP P35555 FBN1_HUMAN 1200 1285
SEQRES 1 A 86 THR ASP ILE ASP GLU CYS ARG ILE SER PRO ASP LEU CYS
SEQRES 2 A 86 GLY ARG GLY GLN CYS VAL ASN THR PRO GLY ASP PHE GLU
SEQRES 3 A 86 CYS LYS CYS ASP GLU GLY TYR GLU SER GLY PHE MET MET
SEQRES 4 A 86 MET LYS ASN CYS MET ASP ILE ASP GLU CYS GLN ARG ASP
SEQRES 5 A 86 PRO LEU LEU CYS ARG GLY GLY VAL CYS HIS ASN THR GLU
SEQRES 6 A 86 GLY SER TYR ARG CYS GLU CYS PRO PRO GLY HIS GLN LEU
SEQRES 7 A 86 SER PRO ASN ILE SER ALA CYS ILE
HET CA A 101 1
HET CA A 102 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 ASP A 49 ASP A 54 1 6
SHEET 1 A 2 CYS A 20 THR A 23 0
SHEET 2 A 2 ASP A 26 CYS A 29 -1 O GLU A 28 N VAL A 21
SHEET 1 B 2 TYR A 35 SER A 37 0
SHEET 2 B 2 CYS A 45 ASP A 47 -1 O MET A 46 N GLU A 36
SHEET 1 C 2 VAL A 62 THR A 66 0
SHEET 2 C 2 SER A 69 GLU A 73 -1 O ARG A 71 N HIS A 64
SSBOND 1 CYS A 8 CYS A 20 1555 1555 2.03
SSBOND 2 CYS A 15 CYS A 29 1555 1555 2.03
SSBOND 3 CYS A 31 CYS A 45 1555 1555 2.04
SSBOND 4 CYS A 51 CYS A 63 1555 1555 2.03
SSBOND 5 CYS A 58 CYS A 72 1555 1555 2.03
SSBOND 6 CYS A 74 CYS A 87 1555 1555 2.03
LINK OD1 ASP A 4 CA CA A 101 1555 1555 2.58
LINK O ILE A 5 CA CA A 101 1555 1555 2.45
LINK OE2 GLU A 7 CA CA A 101 1555 1555 2.61
LINK OE1 GLU A 7 CA CA A 101 1555 1555 2.45
LINK OD1 ASN A 22 CA CA A 101 1555 1555 2.60
LINK ND2 ASN A 22 CA CA A 101 1555 1555 2.79
LINK O THR A 23 CA CA A 101 1555 1555 2.45
LINK N THR A 23 CA CA A 101 1555 1555 3.23
LINK O ASP A 26 CA CA A 101 1555 1555 3.34
LINK OD2 ASP A 47 CA CA A 102 1555 1555 2.45
LINK O ILE A 48 CA CA A 102 1555 1555 2.44
LINK OE1 GLU A 50 CA CA A 102 1555 1555 2.44
LINK OE2 GLU A 50 CA CA A 102 1555 1555 2.61
LINK OD1 ASN A 65 CA CA A 102 1555 1555 2.45
LINK ND2 ASN A 65 CA CA A 102 1555 1555 2.87
LINK O THR A 66 CA CA A 102 1555 1555 2.61
CISPEP 1 CYS A 74 PRO A 75 1 1.00
CISPEP 2 CYS A 74 PRO A 75 2 1.26
CISPEP 3 CYS A 74 PRO A 75 3 1.15
CISPEP 4 CYS A 74 PRO A 75 4 1.05
CISPEP 5 CYS A 74 PRO A 75 5 1.17
CISPEP 6 CYS A 74 PRO A 75 6 1.28
CISPEP 7 CYS A 74 PRO A 75 7 1.07
CISPEP 8 CYS A 74 PRO A 75 8 0.99
CISPEP 9 CYS A 74 PRO A 75 9 1.43
CISPEP 10 CYS A 74 PRO A 75 10 1.01
CISPEP 11 CYS A 74 PRO A 75 11 1.46
CISPEP 12 CYS A 74 PRO A 75 12 0.83
CISPEP 13 CYS A 74 PRO A 75 13 0.96
CISPEP 14 CYS A 74 PRO A 75 14 1.18
CISPEP 15 CYS A 74 PRO A 75 15 0.86
CISPEP 16 CYS A 74 PRO A 75 16 1.38
CISPEP 17 CYS A 74 PRO A 75 17 1.04
CISPEP 18 CYS A 74 PRO A 75 18 1.10
CISPEP 19 CYS A 74 PRO A 75 19 1.02
CISPEP 20 CYS A 74 PRO A 75 20 1.07
CISPEP 21 CYS A 74 PRO A 75 21 0.98
CISPEP 22 CYS A 74 PRO A 75 22 0.92
CISPEP 23 CYS A 74 PRO A 75 23 1.18
CISPEP 24 CYS A 74 PRO A 75 24 1.13
CISPEP 25 CYS A 74 PRO A 75 25 1.09
SITE 1 AC1 6 ASP A 4 ILE A 5 GLU A 7 ASN A 22
SITE 2 AC1 6 THR A 23 ASP A 26
SITE 1 AC2 6 ASP A 47 ILE A 48 GLU A 50 ASN A 65
SITE 2 AC2 6 THR A 66 SER A 69
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 - b 23 2 Bytes