HEADER STRUCTURAL PROTEIN 01-JAN-17 5MS9
TITLE SOLUTION STRUCTURE OF HUMAN FIBRILLIN-1 EGF2-EGF3-HYBRID1-CBEGF1 FOUR
TITLE 2 DOMAIN FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRILLIN-1;
COMPND 3 CHAIN: A;
COMPND 4 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, FBN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FIBRILLIN EGF HYBRID EXTRACELLULAR, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.B.ROBERTSON,C.REDFIELD,P.A.HANDFORD
REVDAT 3 23-OCT-24 5MS9 1 REMARK
REVDAT 2 08-MAY-19 5MS9 1 REMARK
REVDAT 1 09-AUG-17 5MS9 0
JRNL AUTH I.B.ROBERTSON,H.F.DIAS,I.H.OSUCH,E.D.LOWE,S.A.JENSEN,
JRNL AUTH 2 C.REDFIELD,P.A.HANDFORD
JRNL TITL THE N-TERMINAL REGION OF FIBRILLIN-1 MEDIATES A BIPARTITE
JRNL TITL 2 INTERACTION WITH LTBP1.
JRNL REF STRUCTURE V. 25 1208 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28669633
JRNL DOI 10.1016/J.STR.2017.06.003
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.B.ROBERTSON,I.OSUCH,D.A.YADIN,P.A.HANDFORD,S.A.JENSEN,
REMARK 1 AUTH 2 C.REDFIELD
REMARK 1 TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS FOR THE FIBRILLIN-1
REMARK 1 TITL 2 EGF2-EGF3-HYBRID1-CBEGF1 FOUR-DOMAIN FRAGMENT.
REMARK 1 REF BIOMOL NMR ASSIGN V. 8 189 2014
REMARK 1 REFN ESSN 1874-270X
REMARK 1 PMID 23649688
REMARK 1 DOI 10.1007/S12104-013-9481-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH, ARIA
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (XPLOR
REMARK 3 -NIH), LINGE, O'DONOGHUE AND NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5MS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1200002729.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 268
REMARK 210 PH : 5.4
REMARK 210 IONIC STRENGTH : 15
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM FIBRILLIN-1 E2CB1, 5 MM
REMARK 210 CALCIUM ION, 100% D2O; 1 MM [U-
REMARK 210 15N] FIBRILLIN-1 E2CB1, 5 MM
REMARK 210 CALCIUM ION, 95% H2O/5% D2O; 1
REMARK 210 MM [U-13C; U-15N] FIBRILLIN-1
REMARK 210 E2CB1, 5 MM CALCIUM ION, 95% H2O/
REMARK 210 5% D2O; 1 MM [U-15N] FIBRILLIN-1
REMARK 210 E2CB1, 5 MM CALCIUM ION, 4 %
REMARK 210 BICELLES, 90% H2O/10% D2O; 1 MM
REMARK 210 [U-15N] FIBRILLIN-1 E2CB1, 5 MM
REMARK 210 CALCIUM ION, 2.2 % PEG-HEXANOL
REMARK 210 SOLUTION, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D 1H-15N NOESY; 3D 1H
REMARK 210 -13C NOESY; 3D 1H-13C NOESY
REMARK 210 AROMATIC; IPAP
REMARK 210 SPECTROMETER FIELD STRENGTH : 950 MHZ; 750 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CCPNMR ANALYSIS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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: 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 GLN A 117 47.51 -88.14
REMARK 500 1 HIS A 118 -153.78 -166.47
REMARK 500 1 ILE A 121 -169.89 -69.97
REMARK 500 1 ASP A 131 -44.23 77.66
REMARK 500 1 ASP A 132 -39.63 156.53
REMARK 500 1 ASN A 156 31.25 35.43
REMARK 500 1 PRO A 163 107.14 -51.16
REMARK 500 1 ASN A 164 -11.35 75.28
REMARK 500 1 TYR A 170 125.89 177.75
REMARK 500 1 CYS A 177 59.54 24.31
REMARK 500 1 ASP A 180 49.60 -80.50
REMARK 500 1 SER A 191 -166.50 -117.08
REMARK 500 1 GLN A 193 -73.79 -83.76
REMARK 500 1 GLN A 196 -58.70 -161.27
REMARK 500 1 LEU A 199 175.48 62.75
REMARK 500 1 SER A 200 130.30 176.14
REMARK 500 1 VAL A 213 -40.50 66.12
REMARK 500 1 ARG A 215 -90.12 -128.64
REMARK 500 1 CYS A 221 94.57 33.23
REMARK 500 1 ALA A 226 -122.98 -63.75
REMARK 500 1 GLN A 227 108.97 -52.68
REMARK 500 1 CYS A 231 -103.85 -119.48
REMARK 500 1 PRO A 254 114.23 -39.41
REMARK 500 1 GLN A 284 44.87 29.46
REMARK 500 2 SER A 115 86.26 56.64
REMARK 500 2 ASP A 131 -9.57 63.10
REMARK 500 2 ASP A 132 38.65 108.52
REMARK 500 2 ASN A 164 -14.35 77.11
REMARK 500 2 TYR A 170 -86.51 -158.19
REMARK 500 2 CYS A 177 56.37 28.68
REMARK 500 2 ASP A 180 48.63 -85.63
REMARK 500 2 SER A 191 -166.84 -115.56
REMARK 500 2 GLN A 193 -74.01 -73.30
REMARK 500 2 GLN A 196 -85.90 166.06
REMARK 500 2 ILE A 202 99.39 -60.09
REMARK 500 2 VAL A 213 -45.05 67.55
REMARK 500 2 ARG A 215 -75.98 -125.64
REMARK 500 2 CYS A 221 88.85 45.17
REMARK 500 2 ALA A 226 -142.24 -65.35
REMARK 500 2 GLN A 227 106.37 -52.37
REMARK 500 2 PRO A 230 83.27 -64.31
REMARK 500 2 ARG A 240 -62.46 -100.90
REMARK 500 2 PRO A 274 152.71 -48.94
REMARK 500 2 SER A 283 25.75 -142.47
REMARK 500 2 GLN A 284 41.93 28.57
REMARK 500 3 SER A 113 46.90 -103.14
REMARK 500 3 ASP A 131 -113.32 49.75
REMARK 500 3 ASN A 156 27.02 48.87
REMARK 500 3 ASN A 164 -1.82 69.91
REMARK 500 3 TYR A 170 117.89 -175.70
REMARK 500
REMARK 500 THIS ENTRY HAS 419 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 ILE A 190 SER A 191 4 145.87
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 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 246 OD1
REMARK 620 2 ASP A 246 OD2 63.2
REMARK 620 3 VAL A 247 O 113.0 78.3
REMARK 620 4 GLU A 249 OE1 87.1 133.2 81.9
REMARK 620 5 GLU A 249 OE2 143.0 153.3 83.4 61.6
REMARK 620 6 ASN A 264 OD1 136.2 79.1 77.7 136.5 78.2
REMARK 620 7 THR A 265 O 76.1 74.8 143.3 134.8 111.2 73.0
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 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19078 RELATED DB: BMRB
DBREF 5MS9 A 113 287 UNP P35555 FBN1_HUMAN 113 287
SEQADV 5MS9 SER A 111 UNP P35555 EXPRESSION TAG
SEQADV 5MS9 ALA A 112 UNP P35555 EXPRESSION TAG
SEQADV 5MS9 SER A 204 UNP P35555 CYS 204 CONFLICT
SEQRES 1 A 177 SER ALA SER ARG SER ILE GLN HIS CYS ASN ILE ARG CYS
SEQRES 2 A 177 MET ASN GLY GLY SER CYS SER ASP ASP HIS CYS LEU CYS
SEQRES 3 A 177 GLN LYS GLY TYR ILE GLY THR HIS CYS GLY GLN PRO VAL
SEQRES 4 A 177 CYS GLU SER GLY CYS LEU ASN GLY GLY ARG CYS VAL ALA
SEQRES 5 A 177 PRO ASN ARG CYS ALA CYS THR TYR GLY PHE THR GLY PRO
SEQRES 6 A 177 GLN CYS GLU ARG ASP TYR ARG THR GLY PRO CYS PHE THR
SEQRES 7 A 177 VAL ILE SER ASN GLN MET CYS GLN GLY GLN LEU SER GLY
SEQRES 8 A 177 ILE VAL SER THR LYS THR LEU CYS CYS ALA THR VAL GLY
SEQRES 9 A 177 ARG ALA TRP GLY HIS PRO CYS GLU MET CYS PRO ALA GLN
SEQRES 10 A 177 PRO HIS PRO CYS ARG ARG GLY PHE ILE PRO ASN ILE ARG
SEQRES 11 A 177 THR GLY ALA CYS GLN ASP VAL ASP GLU CYS GLN ALA ILE
SEQRES 12 A 177 PRO GLY LEU CYS GLN GLY GLY ASN CYS ILE ASN THR VAL
SEQRES 13 A 177 GLY SER PHE GLU CYS LYS CYS PRO ALA GLY HIS LYS LEU
SEQRES 14 A 177 ASN GLU VAL SER GLN LYS CYS GLU
HET CA A 301 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 AA1 THR A 205 THR A 212 1 8
HELIX 2 AA2 ASP A 248 ILE A 253 1 6
SHEET 1 AA1 2 SER A 128 SER A 130 0
SHEET 2 AA1 2 HIS A 133 LEU A 135 -1 O LEU A 135 N SER A 128
SHEET 1 AA2 2 TYR A 140 ILE A 141 0
SHEET 2 AA2 2 GLN A 147 PRO A 148 -1 O GLN A 147 N ILE A 141
SHEET 1 AA3 2 ARG A 159 ALA A 162 0
SHEET 2 AA3 2 ARG A 165 ALA A 167 -1 O ARG A 165 N VAL A 161
SHEET 1 AA4 4 VAL A 203 SER A 204 0
SHEET 2 AA4 4 GLY A 184 PHE A 187 -1 N GLY A 184 O SER A 204
SHEET 3 AA4 4 ALA A 216 TRP A 217 -1 O ALA A 216 N PHE A 187
SHEET 4 AA4 4 GLU A 222 MET A 223 -1 O GLU A 222 N TRP A 217
SHEET 1 AA5 2 PHE A 235 PRO A 237 0
SHEET 2 AA5 2 CYS A 244 ASP A 246 -1 O GLN A 245 N ILE A 236
SHEET 1 AA6 2 ASN A 261 THR A 265 0
SHEET 2 AA6 2 SER A 268 LYS A 272 -1 O GLU A 270 N ILE A 263
SHEET 1 AA7 2 LEU A 279 ASN A 280 0
SHEET 2 AA7 2 LYS A 285 CYS A 286 -1 O LYS A 285 N ASN A 280
SSBOND 1 CYS A 119 CYS A 129 1555 1555 2.02
SSBOND 2 CYS A 123 CYS A 134 1555 1555 2.03
SSBOND 3 CYS A 136 CYS A 145 1555 1555 2.03
SSBOND 4 CYS A 150 CYS A 160 1555 1555 2.02
SSBOND 5 CYS A 154 CYS A 166 1555 1555 2.03
SSBOND 6 CYS A 168 CYS A 177 1555 1555 2.03
SSBOND 7 CYS A 186 CYS A 209 1555 1555 2.03
SSBOND 8 CYS A 195 CYS A 221 1555 1555 2.03
SSBOND 9 CYS A 210 CYS A 224 1555 1555 2.03
SSBOND 10 CYS A 231 CYS A 244 1555 1555 2.03
SSBOND 11 CYS A 250 CYS A 262 1555 1555 2.03
SSBOND 12 CYS A 257 CYS A 271 1555 1555 2.03
SSBOND 13 CYS A 273 CYS A 286 1555 1555 2.03
LINK OD1 ASP A 246 CA CA A 301 1555 1555 1.95
LINK OD2 ASP A 246 CA CA A 301 1555 1555 2.14
LINK O VAL A 247 CA CA A 301 1555 1555 2.15
LINK OE1 GLU A 249 CA CA A 301 1555 1555 2.08
LINK OE2 GLU A 249 CA CA A 301 1555 1555 2.11
LINK OD1 ASN A 264 CA CA A 301 1555 1555 2.03
LINK O THR A 265 CA CA A 301 1555 1555 2.84
CISPEP 1 HIS A 219 PRO A 220 1 -5.07
CISPEP 2 HIS A 219 PRO A 220 2 -4.49
CISPEP 3 HIS A 219 PRO A 220 3 -5.28
CISPEP 4 HIS A 219 PRO A 220 4 -2.03
CISPEP 5 HIS A 219 PRO A 220 5 -4.98
CISPEP 6 HIS A 219 PRO A 220 6 -0.65
CISPEP 7 HIS A 219 PRO A 220 7 -4.78
CISPEP 8 HIS A 219 PRO A 220 8 -5.07
CISPEP 9 HIS A 219 PRO A 220 9 -3.48
CISPEP 10 HIS A 219 PRO A 220 10 -3.90
CISPEP 11 HIS A 219 PRO A 220 11 -3.14
CISPEP 12 HIS A 219 PRO A 220 12 -1.13
CISPEP 13 HIS A 219 PRO A 220 13 -3.85
CISPEP 14 HIS A 219 PRO A 220 14 -9.01
CISPEP 15 HIS A 219 PRO A 220 15 -3.67
CISPEP 16 HIS A 219 PRO A 220 16 -0.35
CISPEP 17 HIS A 219 PRO A 220 17 -4.73
CISPEP 18 HIS A 219 PRO A 220 18 -2.50
CISPEP 19 HIS A 219 PRO A 220 19 -4.77
CISPEP 20 HIS A 219 PRO A 220 20 -2.61
SITE 1 AC1 5 ASP A 246 VAL A 247 GLU A 249 ASN A 264
SITE 2 AC1 5 THR A 265
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
(ATOM LINES ARE NOT SHOWN.)
END
