Header list of 1lv9.pdb file
Complete list - 23 20 Bytes
HEADER CYTOKINE 27-MAY-02 1LV9
TITLE CXCR3 BINDING CHEMOKINE IP-10/CXCL10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL INDUCIBLE CYTOKINE B10;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CXCL10, INTERFERON-GAMMA INDUCED PROTEIN, GAMMA-IP10, IP-10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE OF THE PROTEIN IS NATURALLY FOUND IN
SOURCE 4 HOMO SAPIENS. IT WAS SYNTHESIZED BY STEPWISE SOLID PHASE METHODS
SOURCE 5 USING T-BUTOXYCARBONYL PROTECTION CHEMISTRY.
KEYWDS CHEMOKINE, CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR V.BOOTH,D.W.KEIZER,M.B.KAMPHUIS,I.CLARK-LEWIS,B.D.SYKES
REVDAT 3 23-FEB-22 1LV9 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1LV9 1 VERSN
REVDAT 1 18-SEP-02 1LV9 0
JRNL AUTH V.BOOTH,D.W.KEIZER,M.B.KAMPHUIS,I.CLARK-LEWIS,B.D.SYKES
JRNL TITL THE CXCR3 BINDING CHEMOKINE IP-10/CXCL10: STRUCTURE AND
JRNL TITL 2 RECEPTOR INTERACTIONS.
JRNL REF BIOCHEMISTRY V. 41 10418 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12173928
JRNL DOI 10.1021/BI026020Q
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, X-PLOR 3.851, ARIA 1999
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LV9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016308.
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 : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM NMELEU 27 IP-10 (NO ISOTOPE
REMARK 210 LABELLING), 1 MM SODIUM AZIDE, 1
REMARK 210 MM DSS, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 4.1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND 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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 VAL A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 ARG A 5
REMARK 465 THR A 6
REMARK 465 GLU A 71
REMARK 465 MET A 72
REMARK 465 SER A 73
REMARK 465 LYS A 74
REMARK 465 ARG A 75
REMARK 465 SER A 76
REMARK 465 PRO A 77
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 HH21 ARG A 38 OE1 GLU A 57 1.56
REMARK 500 O ASN A 63 H ALA A 67 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 PRO A 18 -27.86 -38.15
REMARK 500 1 PRO A 21 -16.88 -40.76
REMARK 500 1 GLU A 25 -74.03 -146.39
REMARK 500 1 LYS A 26 79.51 -104.87
REMARK 500 1 SER A 33 -58.22 -160.27
REMARK 500 1 ARG A 38 -162.71 -160.71
REMARK 500 1 LYS A 47 -35.36 176.14
REMARK 500 1 LYS A 48 27.53 -162.51
REMARK 500 1 PRO A 56 93.66 -23.73
REMARK 500 1 SER A 58 -164.40 -160.75
REMARK 500 1 LYS A 59 -80.78 -87.67
REMARK 500 2 PRO A 18 -28.64 -38.42
REMARK 500 2 PRO A 21 -15.52 -41.01
REMARK 500 2 GLU A 25 -76.34 -146.18
REMARK 500 2 SER A 33 -67.06 -157.18
REMARK 500 2 ARG A 38 -160.47 -160.53
REMARK 500 2 LYS A 47 -33.72 172.49
REMARK 500 2 LYS A 48 24.83 -159.73
REMARK 500 2 ASN A 55 77.09 -150.98
REMARK 500 2 PRO A 56 96.73 -25.86
REMARK 500 2 GLU A 57 53.90 -140.49
REMARK 500 2 LYS A 59 -81.07 -87.02
REMARK 500 3 CYS A 9 -165.88 -79.64
REMARK 500 3 PRO A 18 -27.95 -38.02
REMARK 500 3 ASN A 20 -175.72 -68.07
REMARK 500 3 GLU A 25 -74.41 -145.43
REMARK 500 3 SER A 33 -48.52 -161.72
REMARK 500 3 PHE A 35 -52.09 -132.06
REMARK 500 3 PRO A 37 68.58 -63.74
REMARK 500 3 ARG A 38 -159.01 -147.07
REMARK 500 3 LYS A 47 -36.12 175.67
REMARK 500 3 LYS A 48 21.97 -162.54
REMARK 500 3 PRO A 56 96.72 -25.89
REMARK 500 3 GLU A 57 55.44 -141.80
REMARK 500 3 SER A 58 -165.73 -160.69
REMARK 500 3 LYS A 59 -80.88 -85.82
REMARK 500 4 PRO A 18 -27.73 -39.61
REMARK 500 4 ASN A 20 -174.01 -68.85
REMARK 500 4 PRO A 21 -9.78 -57.70
REMARK 500 4 GLU A 25 -71.81 -144.08
REMARK 500 4 LYS A 26 78.41 -106.92
REMARK 500 4 SER A 33 -57.37 -161.05
REMARK 500 4 PHE A 35 -54.59 -125.10
REMARK 500 4 LYS A 47 -33.86 172.63
REMARK 500 4 LYS A 48 23.26 -155.36
REMARK 500 4 ASN A 55 75.56 -151.79
REMARK 500 4 PRO A 56 96.71 -21.39
REMARK 500 4 SER A 58 -166.75 -160.39
REMARK 500 4 LYS A 59 -80.53 -86.37
REMARK 500 5 ARG A 8 115.20 -160.92
REMARK 500
REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LV9 A 1 77 UNP P02778 SCYBA_HUMAN 22 98
SEQADV 1LV9 MLE A 27 UNP P02778 LEU 48 MODIFIED RESIDUE
SEQRES 1 A 77 VAL PRO LEU SER ARG THR VAL ARG CYS THR CYS ILE SER
SEQRES 2 A 77 ILE SER ASN GLN PRO VAL ASN PRO ARG SER LEU GLU LYS
SEQRES 3 A 77 MLE GLU ILE ILE PRO ALA SER GLN PHE CYS PRO ARG VAL
SEQRES 4 A 77 GLU ILE ILE ALA THR MET LYS LYS LYS GLY GLU LYS ARG
SEQRES 5 A 77 CYS LEU ASN PRO GLU SER LYS ALA ILE LYS ASN LEU LEU
SEQRES 6 A 77 LYS ALA VAL SER LYS GLU MET SER LYS ARG SER PRO
MODRES 1LV9 MLE A 27 LEU N-METHYLLEUCINE
HET MLE A 27 22
HETNAM MLE N-METHYLLEUCINE
FORMUL 1 MLE C7 H15 N O2
HELIX 1 1 ALA A 60 LYS A 70 1 11
SHEET 1 A 3 LYS A 26 PRO A 31 0
SHEET 2 A 3 VAL A 39 MET A 45 -1 O GLU A 40 N ILE A 30
SHEET 3 A 3 GLU A 50 LEU A 54 -1 O ARG A 52 N ALA A 43
SSBOND 1 CYS A 9 CYS A 36 1555 1555 2.14
SSBOND 2 CYS A 11 CYS A 53 1555 1555 2.14
LINK C LYS A 26 N MLE A 27 1555 1555 1.34
LINK C MLE A 27 N GLU A 28 1555 1555 1.33
CISPEP 1 ILE A 14 SER A 15 10 1.38
CISPEP 2 VAL A 19 ASN A 20 10 9.84
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 - 23 20 Bytes