Header list of 1ilp.pdb file
Complete list - r 4 2 Bytes
HEADER CYTOKINE 16-DEC-98 1ILP
TITLE CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-8 (PRECURSOR);
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IL-8,C-X-C MOTIF CHEMOKINE 8,CHEMOKINE (C-X-C MOTIF) LIGAND
COMPND 5 8,EMOCTAKIN,GRANULOCYTE CHEMOTACTIC PROTEIN 1,GCP-1,MONOCYTE-DERIVED
COMPND 6 NEUTROPHIL CHEMOTACTIC FACTOR,MDNCF,MONOCYTE-DERIVED NEUTROPHIL-
COMPND 7 ACTIVATING PEPTIDE,MONAP,NEUTROPHIL-ACTIVATING PROTEIN 1,NAP-1,
COMPND 8 PROTEIN 3-10C,T-CELL CHEMOTACTIC FACTOR;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 1;
COMPND 12 CHAIN: C;
COMPND 13 FRAGMENT: 9-29;
COMPND 14 SYNONYM: CXCR-1,CDW128A,HIGH AFFINITY INTERLEUKIN-8 RECEPTOR A,IL-8R
COMPND 15 A,IL-8 RECEPTOR TYPE 1;
COMPND 16 ENGINEERED: YES;
COMPND 17 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: CXCL8, IL8;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: ALKALINE PHOSPHATASE PROMOTER (PPHOA);
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PPS0170;
SOURCE 13 MOL_ID: 2;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606
KEYWDS CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.J.SKELTON,C.QUAN,H.LOWMAN
REVDAT 5 04-MAR-20 1ILP 1 COMPND SOURCE REMARK DBREF
REVDAT 5 2 1 SEQADV SEQRES LINK ATOM
REVDAT 4 24-FEB-09 1ILP 1 VERSN
REVDAT 3 01-APR-03 1ILP 1 JRNL
REVDAT 2 22-DEC-99 1ILP 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 23-DEC-98 1ILP 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 : DISCOVER
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. SEE JRNL ENTRY FOR MORE DETAILS.
REMARK 4
REMARK 4 1ILP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008098.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.5
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
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 MODELS 1-20
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: 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 O PRO A 16 O1 ACA C 7 1.77
REMARK 500
REMARK 500 REMARK: NULL
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 1 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 1 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 1 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 2 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 2 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 2 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 3 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 3 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 3 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 4 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 4 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 4 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 5 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 5 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 5 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 6 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 6 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 6 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 7 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 7 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 7 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 8 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 8 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 8 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 9 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 9 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 9 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 10 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 10 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 10 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 11 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 11 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 11 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 12 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 12 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 12 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 13 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 13 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 13 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 14 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 14 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 14 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 15 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 15 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 15 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 16 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 16 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 16 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 17 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 17 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500
REMARK 500 THIS ENTRY HAS 60 BOND DEVIATIONS.
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 1 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 TRP B 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP B 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 2 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 2 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 2 TRP B 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP B 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 2 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 3 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 3 TRP B 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 TRP B 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 4 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 4 TRP B 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TRP B 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 5 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 5 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 5 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 5 TRP B 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP B 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 5 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 5 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 6 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 6 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 6 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 6 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 6 TRP B 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 6 TRP B 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 6 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 6 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 7 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 7 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 161 ANGLE DEVIATIONS.
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 LYS A 3 -66.50 -130.78
REMARK 500 1 PRO A 16 96.33 -56.67
REMARK 500 1 ASN A 36 -149.51 -140.30
REMARK 500 1 PRO A 53 -2.49 -59.30
REMARK 500 1 LYS B 3 -66.56 -130.83
REMARK 500 1 SER B 14 37.75 -99.02
REMARK 500 1 ASN B 36 -149.49 -140.25
REMARK 500 1 ASP B 45 -6.23 -59.18
REMARK 500 1 PRO B 53 -2.49 -59.36
REMARK 500 1 ASP C 5 93.39 -67.44
REMARK 500 1 PRO C 9 164.05 -46.26
REMARK 500 1 GLU C 13 98.78 -160.04
REMARK 500 1 ASP C 14 51.89 -156.62
REMARK 500 2 LYS A 3 -66.50 -130.78
REMARK 500 2 ASN A 36 -149.51 -140.30
REMARK 500 2 ARG A 47 -163.94 -79.36
REMARK 500 2 PRO A 53 -2.49 -59.30
REMARK 500 2 LYS B 3 -66.56 -130.83
REMARK 500 2 SER B 14 37.75 -99.02
REMARK 500 2 ASN B 36 -149.49 -140.25
REMARK 500 2 ASP B 45 -6.23 -59.18
REMARK 500 2 PRO B 53 -2.49 -59.36
REMARK 500 2 PHE C 4 -7.77 -147.25
REMARK 500 2 PRO C 10 86.99 -29.06
REMARK 500 2 ASP C 12 33.59 -151.48
REMARK 500 2 ASP C 14 43.88 -156.39
REMARK 500 3 LYS A 3 -66.50 -130.78
REMARK 500 3 ASN A 36 -149.51 -140.30
REMARK 500 3 ARG A 47 -141.65 -99.45
REMARK 500 3 PRO A 53 -2.49 -59.30
REMARK 500 3 LYS B 3 -66.56 -130.83
REMARK 500 3 SER B 14 37.75 -99.02
REMARK 500 3 ASN B 36 -149.49 -140.25
REMARK 500 3 ASP B 45 -6.23 -59.18
REMARK 500 3 PRO B 53 -2.49 -59.36
REMARK 500 3 PHE C 4 92.59 -69.54
REMARK 500 3 PRO C 9 174.01 -52.11
REMARK 500 3 PRO C 10 85.98 -23.63
REMARK 500 3 SER C 16 77.99 -163.65
REMARK 500 4 LYS A 3 -66.50 -130.78
REMARK 500 4 ASN A 36 -149.51 -140.30
REMARK 500 4 ARG A 47 -150.92 -116.16
REMARK 500 4 PRO A 53 -2.49 -59.30
REMARK 500 4 LYS B 3 -66.56 -130.83
REMARK 500 4 SER B 14 37.75 -99.02
REMARK 500 4 ASN B 36 -149.49 -140.25
REMARK 500 4 ASP B 45 -6.23 -59.18
REMARK 500 4 PRO B 53 -2.49 -59.36
REMARK 500 4 PRO C 10 -169.45 -73.18
REMARK 500 4 ALA C 11 22.86 -72.08
REMARK 500
REMARK 500 THIS ENTRY HAS 256 RAMACHANDRAN OUTLIERS.
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 6 0.32 SIDE CHAIN
REMARK 500 1 ARG A 26 0.22 SIDE CHAIN
REMARK 500 1 ARG A 60 0.21 SIDE CHAIN
REMARK 500 1 ARG B 6 0.32 SIDE CHAIN
REMARK 500 1 ARG B 26 0.22 SIDE CHAIN
REMARK 500 1 ARG B 47 0.31 SIDE CHAIN
REMARK 500 1 ARG B 60 0.21 SIDE CHAIN
REMARK 500 2 ARG A 6 0.32 SIDE CHAIN
REMARK 500 2 ARG A 26 0.22 SIDE CHAIN
REMARK 500 2 ARG A 60 0.21 SIDE CHAIN
REMARK 500 2 ARG B 6 0.32 SIDE CHAIN
REMARK 500 2 ARG B 26 0.22 SIDE CHAIN
REMARK 500 2 ARG B 47 0.31 SIDE CHAIN
REMARK 500 2 ARG B 60 0.21 SIDE CHAIN
REMARK 500 3 ARG A 6 0.32 SIDE CHAIN
REMARK 500 3 ARG A 26 0.22 SIDE CHAIN
REMARK 500 3 ARG A 60 0.21 SIDE CHAIN
REMARK 500 3 ARG B 6 0.32 SIDE CHAIN
REMARK 500 3 ARG B 26 0.22 SIDE CHAIN
REMARK 500 3 ARG B 47 0.31 SIDE CHAIN
REMARK 500 3 ARG B 60 0.21 SIDE CHAIN
REMARK 500 4 ARG A 6 0.32 SIDE CHAIN
REMARK 500 4 ARG A 26 0.22 SIDE CHAIN
REMARK 500 4 ARG A 60 0.21 SIDE CHAIN
REMARK 500 4 ARG B 6 0.32 SIDE CHAIN
REMARK 500 4 ARG B 26 0.22 SIDE CHAIN
REMARK 500 4 ARG B 47 0.31 SIDE CHAIN
REMARK 500 4 ARG B 60 0.21 SIDE CHAIN
REMARK 500 5 ARG A 6 0.32 SIDE CHAIN
REMARK 500 5 ARG A 26 0.22 SIDE CHAIN
REMARK 500 5 ARG A 60 0.21 SIDE CHAIN
REMARK 500 5 ARG B 6 0.32 SIDE CHAIN
REMARK 500 5 ARG B 26 0.22 SIDE CHAIN
REMARK 500 5 ARG B 47 0.31 SIDE CHAIN
REMARK 500 5 ARG B 60 0.21 SIDE CHAIN
REMARK 500 6 ARG A 6 0.32 SIDE CHAIN
REMARK 500 6 ARG A 26 0.22 SIDE CHAIN
REMARK 500 6 ARG A 60 0.21 SIDE CHAIN
REMARK 500 6 ARG B 6 0.32 SIDE CHAIN
REMARK 500 6 ARG B 26 0.22 SIDE CHAIN
REMARK 500 6 ARG B 47 0.31 SIDE CHAIN
REMARK 500 6 ARG B 60 0.21 SIDE CHAIN
REMARK 500 7 ARG A 6 0.32 SIDE CHAIN
REMARK 500 7 ARG A 26 0.22 SIDE CHAIN
REMARK 500 7 ARG A 60 0.21 SIDE CHAIN
REMARK 500 7 ARG B 6 0.32 SIDE CHAIN
REMARK 500 7 ARG B 26 0.22 SIDE CHAIN
REMARK 500 7 ARG B 47 0.31 SIDE CHAIN
REMARK 500 7 ARG B 60 0.21 SIDE CHAIN
REMARK 500 8 ARG A 6 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 141 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
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: 1ILQ RELATED DB: PDB
DBREF 1ILP A 1 72 UNP P10145 IL8_HUMAN 28 99
DBREF 1ILP B 1 72 UNP P10145 IL8_HUMAN 28 99
DBREF 1ILP C 1 17 UNP P25024 CXCR1_HUMAN 9 29
SEQADV 1ILP ACE C 0 UNP P25024 ACETYLATION
SEQADV 1ILP C UNP P25024 LEU 15 DELETION
SEQADV 1ILP C UNP P25024 ASN 16 DELETION
SEQADV 1ILP C UNP P25024 PHE 17 DELETION
SEQADV 1ILP C UNP P25024 THR 18 DELETION
SEQADV 1ILP ACA C 7 UNP P25024 GLY 19 ENGINEERED MUTATION
SEQADV 1ILP NH2 C 18 UNP P25024 AMIDATION
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 ARG A 47 LEU A 51 0
SHEET 2 A 3 GLU A 38 LEU A 43 -1 N LEU A 43 O ARG A 47
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 AC1 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
MODEL 1
Complete list - r 4 2 Bytes