Header list of 1e4q.pdb file
Complete list - 25 20 Bytes
HEADER DEFENSIN 12-JUL-00 1E4Q
TITLE SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-DEFENSIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 28-64 OF THE BETA-DEFENSIN 2 PRECURSOR;
COMPND 5 SYNONYM: HBD-2
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 TISSUE: SKIN;
SOURCE 7 CELLULAR_LOCATION: EXTRACELLULAR
KEYWDS DEFENSIN, HUMAN, NMR STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.BAUER,K.SCHWEIMER,E.KLUVER,K.ADERMANN,W.G.FORSSMANN,
AUTHOR 2 P.ROESCH,H.STICHT
REVDAT 3 24-FEB-09 1E4Q 1 VERSN
REVDAT 2 26-NOV-01 1E4Q 1 JRNL
REVDAT 1 12-JUL-01 1E4Q 0
JRNL AUTH F.BAUER,K.SCHWEIMER,E.KLUVER,J.CONEJO-GARCIA,
JRNL AUTH 2 W.G.FORSSMANN,P.ROESCH,K.ADERMANN,H.STICHT
JRNL TITL STRUCTURE DETERMINATION OF HUMAN AND MURINE BETA-
JRNL TITL 2 DEFENSINS REVEALS STRUCTURAL CONSERVATION IN THE
JRNL TITL 3 ABSENCE OF SIGNIFICANT SEQUENCE SIMILARITY
JRNL REF PROTEIN SCI. V. 10 2470 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11714914
JRNL DOI 10.1110/PS.PS.24401
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: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1E4Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-00.
REMARK 100 THE PDBE ID CODE IS EBI-5048.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY, TOCSY, NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600; 400
REMARK 210 SPECTROMETER MODEL : DRX600; AMX400
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY, LEAST
REMARK 210 RESTRAINT VIOLATION
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HIS A 39 - H LYS A 59 1.47
REMARK 500 H HIS A 39 - O LYS A 59 1.48
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 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 41 -93.87 59.27
REMARK 500 1 PRO A 44 -162.40 -72.43
REMARK 500 2 VAL A 41 -82.78 60.73
REMARK 500 2 PRO A 44 -162.29 -70.96
REMARK 500 3 VAL A 41 -97.27 62.30
REMARK 500 3 PRO A 44 -161.33 -68.49
REMARK 500 4 VAL A 41 -108.36 62.96
REMARK 500 4 PRO A 44 -163.03 -71.22
REMARK 500 4 THR A 52 151.17 69.76
REMARK 500 5 VAL A 41 -92.51 61.26
REMARK 500 5 PRO A 44 -162.60 -71.79
REMARK 500 6 CYS A 31 19.66 58.86
REMARK 500 6 VAL A 41 -108.53 61.50
REMARK 500 6 PRO A 44 -161.44 -71.42
REMARK 500 7 VAL A 41 -104.59 62.43
REMARK 500 7 PRO A 44 -161.64 -69.10
REMARK 500 8 VAL A 41 -108.43 54.07
REMARK 500 8 PRO A 44 -162.78 -70.16
REMARK 500 8 THR A 52 134.05 -34.65
REMARK 500 9 VAL A 41 -88.77 -117.91
REMARK 500 9 PRO A 44 -163.04 -69.95
REMARK 500 10 VAL A 41 -100.73 61.02
REMARK 500 10 PRO A 44 -160.05 -69.45
REMARK 500 11 VAL A 41 -87.54 61.57
REMARK 500 11 PRO A 44 -162.18 -71.02
REMARK 500 12 VAL A 41 -105.18 62.11
REMARK 500 12 PRO A 44 -162.94 -67.60
REMARK 500 13 CYS A 31 19.29 57.28
REMARK 500 13 VAL A 41 -84.02 59.71
REMARK 500 13 PRO A 44 -162.52 -70.39
REMARK 500 13 THR A 52 140.09 -29.52
REMARK 500 14 VAL A 41 -112.15 55.82
REMARK 500 14 PRO A 44 -162.54 -70.71
REMARK 500 15 VAL A 41 -109.35 59.15
REMARK 500 15 PRO A 44 -162.76 -68.41
REMARK 500 16 CYS A 31 18.38 56.61
REMARK 500 16 VAL A 41 -105.94 62.99
REMARK 500 16 PRO A 44 -162.16 -68.71
REMARK 500 17 VAL A 29 172.52 56.80
REMARK 500 17 THR A 30 28.21 39.16
REMARK 500 17 VAL A 41 -84.62 64.24
REMARK 500 17 PRO A 44 -160.63 -70.18
REMARK 500 18 VAL A 41 -108.37 61.84
REMARK 500 18 PRO A 44 -162.56 -71.29
REMARK 500 19 VAL A 41 -84.23 57.18
REMARK 500 19 PRO A 44 -162.23 -70.55
REMARK 500 20 VAL A 41 -115.35 54.74
REMARK 500 20 PRO A 44 -161.88 -71.72
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 45 0.30 SIDE CHAIN
REMARK 500 1 ARG A 46 0.31 SIDE CHAIN
REMARK 500 2 ARG A 45 0.30 SIDE CHAIN
REMARK 500 2 ARG A 46 0.28 SIDE CHAIN
REMARK 500 3 ARG A 45 0.31 SIDE CHAIN
REMARK 500 3 ARG A 46 0.32 SIDE CHAIN
REMARK 500 4 ARG A 45 0.20 SIDE CHAIN
REMARK 500 5 ARG A 45 0.16 SIDE CHAIN
REMARK 500 5 ARG A 46 0.26 SIDE CHAIN
REMARK 500 6 ARG A 45 0.26 SIDE CHAIN
REMARK 500 6 ARG A 46 0.20 SIDE CHAIN
REMARK 500 7 ARG A 45 0.23 SIDE CHAIN
REMARK 500 7 ARG A 46 0.28 SIDE CHAIN
REMARK 500 8 ARG A 45 0.24 SIDE CHAIN
REMARK 500 8 ARG A 46 0.31 SIDE CHAIN
REMARK 500 9 ARG A 45 0.29 SIDE CHAIN
REMARK 500 9 ARG A 46 0.31 SIDE CHAIN
REMARK 500 10 ARG A 45 0.30 SIDE CHAIN
REMARK 500 10 ARG A 46 0.24 SIDE CHAIN
REMARK 500 11 ARG A 46 0.29 SIDE CHAIN
REMARK 500 12 ARG A 45 0.30 SIDE CHAIN
REMARK 500 12 ARG A 46 0.32 SIDE CHAIN
REMARK 500 13 ARG A 45 0.13 SIDE CHAIN
REMARK 500 13 ARG A 46 0.10 SIDE CHAIN
REMARK 500 14 ARG A 45 0.30 SIDE CHAIN
REMARK 500 14 ARG A 46 0.17 SIDE CHAIN
REMARK 500 15 ARG A 45 0.26 SIDE CHAIN
REMARK 500 15 ARG A 46 0.31 SIDE CHAIN
REMARK 500 16 ARG A 45 0.32 SIDE CHAIN
REMARK 500 16 ARG A 46 0.31 SIDE CHAIN
REMARK 500 17 ARG A 45 0.26 SIDE CHAIN
REMARK 500 17 ARG A 46 0.32 SIDE CHAIN
REMARK 500 18 ARG A 45 0.14 SIDE CHAIN
REMARK 500 18 ARG A 46 0.24 SIDE CHAIN
REMARK 500 19 ARG A 45 0.32 SIDE CHAIN
REMARK 500 19 ARG A 46 0.27 SIDE CHAIN
REMARK 500 20 ARG A 45 0.16 SIDE CHAIN
REMARK 500 20 ARG A 46 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1E4Q A 28 64 UNP O15263 BD02_HUMAN 28 64
SEQRES 1 A 37 PRO VAL THR CYS LEU LYS SER GLY ALA ILE CYS HIS PRO
SEQRES 2 A 37 VAL PHE CYS PRO ARG ARG TYR LYS GLN ILE GLY THR CYS
SEQRES 3 A 37 GLY LEU PRO GLY THR LYS CYS CYS LYS LYS PRO
SHEET 1 A 3 ILE A 37 PRO A 40 0
SHEET 2 A 3 THR A 58 LYS A 62 -1 O LYS A 59 N HIS A 39
SHEET 3 A 3 LYS A 48 GLN A 49 -1 O LYS A 48 N LYS A 62
SSBOND 1 CYS A 31 CYS A 60 1555 1555 2.02
SSBOND 2 CYS A 38 CYS A 53 1555 1555 2.02
SSBOND 3 CYS A 43 CYS A 61 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 - 25 20 Bytes