Header list of 1ilq.pdb file
Complete list - 23 20 Bytes
HEADER CYTOKINE 17-DEC-98 1ILQ
TITLE CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-8 PRECURSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IL-8;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INTERLEUKIN-8 RECEPTOR A;
COMPND 8 CHAIN: C;
COMPND 9 FRAGMENT: 9-29;
COMPND 10 SYNONYM: IL8-RA;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: ALKALINE PHOSPHATASE PROMOTER (PPHOA);
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPS0170;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS CYTOKINE
EXPDTA SOLUTION NMR
AUTHOR N.J.SKELTON,C.QUAN,H.LOWMAN
REVDAT 4 23-FEB-22 1ILQ 1 REMARK LINK
REVDAT 3 24-FEB-09 1ILQ 1 VERSN
REVDAT 2 22-DEC-99 1ILQ 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 23-DEC-98 1ILQ 0
JRNL AUTH N.J.SKELTON,C.QUAN,D.REILLY,H.LOWMAN
JRNL TITL STRUCTURE OF A CXC CHEMOKINE-RECEPTOR FRAGMENT IN COMPLEX
JRNL TITL 2 WITH INTERLEUKIN-8.
JRNL REF STRUCTURE FOLD.DES. V. 7 157 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10368283
JRNL DOI 10.1016/S0969-2126(99)80022-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.R.ATTWOOD,ET AL.
REMARK 1 TITL PEPTIDE BASED INHIBITORS OF IL-8: STRUCTURAL SIMPLIFICATION
REMARK 1 TITL 2 AND IMPROVED POTENCY
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 7 429 1997
REMARK 1 REFN ISSN 0960-894X
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.M.CLORE,E.APPELLA,M.YAMADA,A.M.GRONENBORN
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF IL-8 IN SOLUTION
REMARK 1 REF BIOCHEMISTRY V. 29 1689 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INITIAL COORDINATES FOR IL-8 WERE TAKEN
REMARK 3 FROM PDB ENTRY 1IL8; A LINEAR CHAIN FOR THE CXCR-1 FRAGMENT WAS
REMARK 3 BUILT IN INSIGHT (MSI). THE CXCR-1 FRAGMENT WAS POSITIONED
REMARK 3 RANDOMLY WITH RESPECT TO IL8 - OBTAIN 40 STARTING CONFORMATIONS.
REMARK 3 THE INITIAL STRUCTURES WERE THEN REFINED USING RMD WITH THE
REMARK 3 AMBER ALL ATOM FORCE FIELD AS IMPLIMENTED WITHIN DISCOVER. ALL
REMARK 3 OF IL8 MONOMER B AND PARTS OF IL8 MONOMER A (2-7, 22-38 AND 51-
REMARK 3 72) WERE KEPT FIXED DURING THE REFINEMENT SINCE CHEMICAL SHIFT
REMARK 3 CHANGES INDICATED THAT THESE PORTION OF THE MOLECULE WERE NOT
REMARK 3 PERTURBED BY PEPTIDE BINDING. THIS MODEL IS THE RESULT OF
REMARK 3 RESTRAINED ENERGY MINIMIZATION OF THE GEOMETRIC MEAN OF 20
REMARK 3 STRUCTURES FROM THE ENSEMBLE (ENTRY 1ILP) SEE JRNL ENTRY FOR
REMARK 3 MORE DETAILS.
REMARK 4
REMARK 4 1ILQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174185.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.00
REMARK 210 PH : 5.50
REMARK 210 IONIC STRENGTH : 0.15 M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : ASSIGNMENT: SEE REFERENCE 1;
REMARK 210 RESTRAINTS: 3D 15N-EDITED-NOESY
REMARK 210 HSQC; 3D 13C-FILTERED; 13C-
REMARK 210 EDITED-NOESY HMQC; 2D 15N-
REMARK 210 FILTERED NOESY; 2D 13C-FILTERED
REMARK 210 NOESY (100MS); 15N-FILTERED
REMARK 210 NOESY (ALL MIXING TIMES = 100 MS)
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MSI DISCOVER DISCOVER DISCOVER
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE ASSIGNMENTS WERE MADE USING TRIPLE RESONANCE NMR
REMARK 210 EXPERIMENTS CONDUCTED ON 13C/15N LABELED IL-8 BOUND TO UNLABELED
REMARK 210 CXCR-1 PEPTIDE (SEE JRNL ENTRY FOR MORE DETAILS) NOE RESTRAINTS
REMARK 210 WERE OBTAINED FROM 15N EDITED EXPERIMENTS (INTRA IL8), 13C OR
REMARK 210 15N FILTERED EXPERIMENTS (INTRA CXCR-1) OR 13C-FILTERED/ EDITED
REMARK 210 EXPERIMENTS (INTERMOLECULAR RESTRAINTS)
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 SER B 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 57 CG TRP A 57 CD2 -0.108
REMARK 500 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 TRP B 57 CG TRP B 57 CD2 -0.110
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP B 57 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 TRP B 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
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 LYS A 3 -66.54 -130.81
REMARK 500 ASN A 36 -149.51 -140.28
REMARK 500 PRO A 53 -2.56 -59.24
REMARK 500 LYS B 3 -66.57 -130.86
REMARK 500 SER B 14 37.75 -99.02
REMARK 500 ASN B 36 -149.44 -140.28
REMARK 500 ASP B 45 -6.26 -59.16
REMARK 500 PRO B 53 -2.55 -59.37
REMARK 500 PHE C 4 -174.95 -65.89
REMARK 500 PRO C 9 -179.30 -56.77
REMARK 500 GLU C 13 102.64 -162.36
REMARK 500 ASP C 14 47.40 -146.37
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 ARG A 6 0.32 SIDE CHAIN
REMARK 500 ARG A 26 0.22 SIDE CHAIN
REMARK 500 ARG A 60 0.21 SIDE CHAIN
REMARK 500 ARG B 6 0.32 SIDE CHAIN
REMARK 500 ARG B 26 0.22 SIDE CHAIN
REMARK 500 ARG B 47 0.31 SIDE CHAIN
REMARK 500 ARG B 60 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 C 18
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ILP RELATED DB: PDB
DBREF 1ILQ A 1 72 UNP P10145 IL8_HUMAN 28 99
DBREF 1ILQ B 1 72 UNP P10145 IL8_HUMAN 28 99
DBREF 1ILQ C 1 17 UNP P25024 CXCR1_HUMAN 20 29
SEQADV 1ILQ ACA C 7 UNP P25024 LEU 15 SEE REMARK 999
SEQADV 1ILQ C UNP P25024 ASN 16 SEE REMARK 999
SEQADV 1ILQ C UNP P25024 PHE 17 SEE REMARK 999
SEQADV 1ILQ C UNP P25024 THR 18 SEE REMARK 999
SEQADV 1ILQ C UNP P25024 GLY 19 SEE REMARK 999
SEQRES 1 A 72 SER ALA LYS GLU LEU ARG CYS GLN CYS ILE LYS THR TYR
SEQRES 2 A 72 SER LYS PRO PHE HIS PRO LYS PHE ILE LYS GLU LEU ARG
SEQRES 3 A 72 VAL ILE GLU SER GLY PRO HIS CYS ALA ASN THR GLU ILE
SEQRES 4 A 72 ILE VAL LYS LEU SER ASP GLY ARG GLU LEU CYS LEU ASP
SEQRES 5 A 72 PRO LYS GLU ASN TRP VAL GLN ARG VAL VAL GLU LYS PHE
SEQRES 6 A 72 LEU LYS ARG ALA GLU ASN SER
SEQRES 1 B 72 SER ALA LYS GLU LEU ARG CYS GLN CYS ILE LYS THR TYR
SEQRES 2 B 72 SER LYS PRO PHE HIS PRO LYS PHE ILE LYS GLU LEU ARG
SEQRES 3 B 72 VAL ILE GLU SER GLY PRO HIS CYS ALA ASN THR GLU ILE
SEQRES 4 B 72 ILE VAL LYS LEU SER ASP GLY ARG GLU LEU CYS LEU ASP
SEQRES 5 B 72 PRO LYS GLU ASN TRP VAL GLN ARG VAL VAL GLU LYS PHE
SEQRES 6 B 72 LEU LYS ARG ALA GLU ASN SER
SEQRES 1 C 19 ACE MET TRP ASP PHE ASP ASP ACA MET PRO PRO ALA ASP
SEQRES 2 C 19 GLU ASP TYR SER PRO NH2
HET ACE C 0 6
HET ACA C 7 19
HET NH2 C 18 3
HETNAM ACE ACETYL GROUP
HETNAM ACA 6-AMINOHEXANOIC ACID
HETNAM NH2 AMINO GROUP
HETSYN ACA AMINOCAPROIC ACID
FORMUL 3 ACE C2 H4 O
FORMUL 3 ACA C6 H13 N O2
FORMUL 3 NH2 H2 N
HELIX 1 1 PRO A 19 PHE A 21 5 3
HELIX 2 2 ASN A 56 GLU A 70 1 15
HELIX 3 3 PRO B 19 PHE B 21 5 3
HELIX 4 4 ASN B 56 GLU B 70 1 15
SHEET 1 A 3 GLU A 48 LEU A 51 0
SHEET 2 A 3 GLU A 38 LEU A 43 -1 N VAL A 41 O LEU A 49
SHEET 3 A 3 ILE A 22 ILE A 28 -1 N ILE A 28 O GLU A 38
SHEET 1 B 3 ARG B 47 LEU B 51 0
SHEET 2 B 3 GLU B 38 LEU B 43 -1 N LEU B 43 O ARG B 47
SHEET 3 B 3 ILE B 22 ILE B 28 -1 N ILE B 28 O GLU B 38
SSBOND 1 CYS A 7 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 50 1555 1555 2.04
SSBOND 3 CYS B 7 CYS B 34 1555 1555 2.02
SSBOND 4 CYS B 9 CYS B 50 1555 1555 2.02
LINK C ACE C 0 N MET C 1 1555 1555 1.34
LINK C ASP C 6 N6 ACA C 7 1555 1555 1.34
LINK C1 ACA C 7 N MET C 8 1555 1555 1.34
LINK C PRO C 17 N NH2 C 18 1555 1555 1.33
SITE 1 AC2 2 GLN A 8 PRO C 17
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
Complete list - 23 20 Bytes