HEADER ANTIMICROBIAL PROTEIN 02-AUG-12 2LWL
TITLE STRUCTURAL BASIS FOR THE INTERACTION OF HUMAN β-DEFENSIN 6 AND
TITLE 2 ITS PUTATIVE CHEMOKINE RECEPTOR CCR2 AND BREAST CANCER MICROVESICLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-DEFENSIN 106;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-DEFENSIN 6, BD-6, DEFB-6, DEFENSIN, BETA 106;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DEFB106A, BD6, DEFB106, DEFB6, DEFB106B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS BREAST CANCER, DYNAMIC, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.S.DE PAULA,N.S.F.GOMES,L.G.LIMA,C.A.MIYAMOTO,R.Q.MONTEIRO,
AUTHOR 2 F.C.L.ALMEIDA,A.VALENTE
REVDAT 3 13-NOV-13 2LWL 1 JRNL
REVDAT 2 11-SEP-13 2LWL 1 JRNL
REVDAT 1 21-AUG-13 2LWL 0
JRNL AUTH V.S.DE PAULA,N.S.GOMES,L.G.LIMA,C.A.MIYAMOTO,R.Q.MONTEIRO,
JRNL AUTH 2 F.C.ALMEIDA,A.P.VALENTE
JRNL TITL STRUCTURAL BASIS FOR THE INTERACTION OF HUMAN BETA-DEFENSIN
JRNL TITL 2 6 AND ITS PUTATIVE CHEMOKINE RECEPTOR CCR2 AND BREAST CANCER
JRNL TITL 3 MICROVESICLES.
JRNL REF J.MOL.BIOL. V. 425 4479 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23938203
JRNL DOI 10.1016/J.JMB.2013.08.001
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA/CNS VERSION 1.2
REMARK 3 AUTHORS : NILGES, M.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB102922.
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 : 5
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.6 MM [U-99% 13C; U-99% 15N]
REMARK 210 SODIUM PHOSPHATE, 0.2-0.6 MM [U-
REMARK 210 99% 15N] SODIUM PHOSPHATE, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-13C NOESY; 3D 1H-15N NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
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 LYS A 10 30.47 70.97
REMARK 500 1 ASN A 20 17.25 58.28
REMARK 500 1 SER A 40 -47.18 80.77
REMARK 500 1 ILE A 43 -114.57 38.48
REMARK 500 2 ILE A 43 -15.09 78.22
REMARK 500 2 ILE A 44 -51.27 -144.17
REMARK 500 3 SER A 42 -177.29 69.04
REMARK 500 3 ILE A 43 -61.96 73.77
REMARK 500 3 ILE A 44 148.51 -170.18
REMARK 500 4 SER A 42 123.39 69.19
REMARK 500 4 ILE A 43 132.08 76.99
REMARK 500 4 ILE A 44 97.28 44.15
REMARK 500 5 SER A 40 -2.78 74.77
REMARK 500 5 ILE A 43 -42.38 76.44
REMARK 500 6 ILE A 37 99.93 -62.19
REMARK 500 6 PRO A 39 146.51 -38.21
REMARK 500 6 SER A 42 165.15 72.37
REMARK 500 6 ILE A 43 -74.48 68.89
REMARK 500 7 SER A 40 -145.27 -135.06
REMARK 500 7 SER A 42 -144.80 60.51
REMARK 500 7 ILE A 43 -82.57 -79.86
REMARK 500 8 ILE A 43 -66.23 71.70
REMARK 500 9 SER A 42 -171.77 65.46
REMARK 500 9 ILE A 43 -72.10 68.99
REMARK 500 10 SER A 42 -145.03 62.71
REMARK 500 11 SER A 30 -4.20 80.97
REMARK 500 11 SER A 42 159.45 65.60
REMARK 500 11 ILE A 43 -66.68 74.32
REMARK 500 12 SER A 40 -61.64 73.64
REMARK 500 12 SER A 42 -114.60 42.01
REMARK 500 12 ILE A 43 -88.23 -140.37
REMARK 500 13 ILE A 24 -30.26 -130.93
REMARK 500 13 PRO A 39 -171.19 -58.94
REMARK 500 13 SER A 42 -168.08 55.38
REMARK 500 14 SER A 40 161.10 179.29
REMARK 500 14 SER A 42 -150.86 64.61
REMARK 500 14 ILE A 43 -78.19 75.34
REMARK 500 15 SER A 40 -167.57 -165.50
REMARK 500 15 SER A 42 80.80 39.14
REMARK 500 15 ILE A 43 -97.06 33.37
REMARK 500 16 LYS A 29 14.53 59.54
REMARK 500 16 SER A 40 165.21 70.53
REMARK 500 16 SER A 42 143.93 167.63
REMARK 500 16 ILE A 43 -57.14 70.69
REMARK 500 17 LYS A 10 43.96 71.41
REMARK 500 17 LYS A 19 109.56 -41.48
REMARK 500 17 SER A 30 -1.57 77.92
REMARK 500 17 SER A 40 123.33 72.25
REMARK 500 17 ILE A 43 -50.48 73.42
REMARK 500 18 ILE A 37 99.87 -67.73
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18634 RELATED DB: BMRB
DBREF 2LWL A 1 45 UNP Q8N104 D106A_HUMAN 21 65
SEQADV 2LWL GLY A -3 UNP Q8N104 EXPRESSION TAG
SEQADV 2LWL SER A -2 UNP Q8N104 EXPRESSION TAG
SEQADV 2LWL HIS A -1 UNP Q8N104 EXPRESSION TAG
SEQADV 2LWL MET A 0 UNP Q8N104 EXPRESSION TAG
SEQADV 2LWL SER A 40 UNP Q8N104 CYS 60 ENGINEERED MUTATION
SEQRES 1 A 49 GLY SER HIS MET PHE PHE ASP GLU LYS CYS ASN LYS LEU
SEQRES 2 A 49 LYS GLY THR CYS LYS ASN ASN CYS GLY LYS ASN GLU GLU
SEQRES 3 A 49 LEU ILE ALA LEU CYS GLN LYS SER LEU LYS CYS CYS ARG
SEQRES 4 A 49 THR ILE GLN PRO SER GLY SER ILE ILE ASP
HELIX 1 1 PHE A 1 LEU A 9 1 9
SHEET 1 A 3 THR A 12 LYS A 14 0
SHEET 2 A 3 LYS A 32 THR A 36 -1 O CYS A 34 N THR A 12
SHEET 3 A 3 GLU A 21 LEU A 26 -1 N ILE A 24 O CYS A 33
SSBOND 1 CYS A 6 CYS A 33 1555 1555 2.99
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
