Header list of 2il8.pdb file
Complete list - r 9 2 Bytes
HEADER CYTOKINE 08-MAR-90 2IL8
TITLE THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-8;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POTENTIAL
KEYWDS CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.M.CLORE
REVDAT 3 09-MAR-22 2IL8 1 REMARK
REVDAT 2 24-FEB-09 2IL8 1 VERSN
REVDAT 1 15-JAN-91 2IL8 0
JRNL AUTH G.M.CLORE,E.APPELLA,M.YAMADA,K.MATSUSHIMA,A.M.GRONENBORN
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION.
JRNL REF BIOCHEMISTRY V. 29 1689 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2184886
JRNL DOI 10.1021/BI00459A004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.M.CLORE,E.APPELLA,M.YAMADA,K.MATSUSHIMA,A.M.GRONENBORN
REMARK 1 TITL DETERMINATION OF THE SECONDARY STRUCTURE OF INTERLEUKIN-8 BY
REMARK 1 TITL 2 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF J.BIOL.CHEM. V. 264 18907 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISGEO, X-PLOR
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURE DETERMINATION. THE METHOD USED TO DETERMINE AND
REMARK 3 REFINE THE STRUCTURE IS THE HYBRID DISTANCE
REMARK 3 GEOMETRY-SIMULATED ANNEALING METHOD (M.NILGES, G.M.CLORE,
REMARK 3 A.M. GRONENBORN, FEBS LETT. 229, 317 (1988)) USING THE
REMARK 3 PROGRAMS *DISGEO* (T.F. HAVEL, QCPE NO. 507, INDIANA
REMARK 3 UNIVERSITY) AND *XPLOR* (A.T. BRUNGER, YALE UNIVERSITY,
REMARK 3 NEW HAVEN, CT 06511).
REMARK 3
REMARK 3 STRUCTURAL STATISTICS - THESE ARE CALCULATED FROM ALL THE
REMARK 3 30 MODELS GIVEN IN THIS ENTRY.
REMARK 3 NUMBERS ENCLOSED IN PARENTHESIS
REMARK 3 REPRESENT THE MINIMIZED MEAN
REMARK 3 STRUCTURE OBTAINED BY RESTRAINED
REMARK 3 MINIMIZATION OF THE AVERAGE RMS.
REMARK 3
REMARK 3 RMS DEVIATION FROM EXPERIMENTAL RESTRAINTS *(1)*
REMARK 3
REMARK 3 RESTRAINT TYPE NUMBER OF RESTRAINTS RMS (ANGSTROMS)
REMARK 3
REMARK 3 ALL 1880 0.031(0.029)
REMARK 3 INTRASUBUNIT
REMARK 3 SHORT RANGE 784 0.019(0.020)
REMARK 3 INTERRESIDUE
REMARK 3 LONG RANGE 370 0.027(0.026)
REMARK 3 INTRARESIDUE 540 0.044(0.042)
REMARK 3 HBOND *(2)* 104 0.031(0.028)
REMARK 3 INTERSUBUNIT
REMARK 3 INTERPROTON 70 0.022(0.014)
REMARK 3 HBOND 12 0.004(0.000)
REMARK 3
REMARK 3 TORSION ANGLES (DEGREES) 362 0.203 (0.211)
REMARK 3 POTENTIAL ENERGY TERMS
REMARK 3
REMARK 3 TYPE ENERGY (KCAL/MOL)
REMARK 3
REMARK 3 F(NOE) *(3)* 53(48)
REMARK 3 F(TOR) *(4)* 0.94(0.98)
REMARK 3 F(REPEL) *(5)* 38(37)
REMARK 3 F(SYM) *(6)* 0.15(424)
REMARK 3
REMARK 3 LENNARD-JONES VAN DER WAALS ENERGY (E(L-J)) CALCULATED
REMARK 3 USING THE *CHARMM* EMPIRICAL ENERGY FUNCTION IS
REMARK 3 -542(-474) KCAL/MOL.
REMARK 3
REMARK 3 DEVIATIONS FROM IDEALIZED GEOMETRY *(6)*
REMARK 3
REMARK 3 TYPE TOTAL NUMBER RMS DEVIATION
REMARK 3
REMARK 3 BONDS 2392 0.006(0.011) (ANGSTROMS)
REMARK 3 ANGLES 4362 2.016(2.458) (DEGREES)
REMARK 3 IMPROPERS 882 0.504(0.485) (DEGREES)
REMARK 3
REMARK 3 NOTES.
REMARK 3 *(1)* THE RMS DEVIATION FROM THE EXPERIMENTAL RESTRAINTS
REMARK 3 IS CALCULATED WITH RESPECT TO THE UPPER AND
REMARK 3 LOWER LIMITS OF THE DISTANCE RESTRAINTS. NONE OF
REMARK 3 THE STRUCTURES EXHIBITED VIOLATIONS GREATER THAN
REMARK 3 0.3 ANGSTROMS.
REMARK 3 *(2)* FOR EACH BACKBONE HYDROGEN BOND THERE ARE TWO
REMARK 3 RESTRAINTS - R(NH-O) 1.7 TO 2.3 ANGSTROMS AND
REMARK 3 R(N-O) 2.4 TO 3.3 ANGSTROMS.
REMARK 3 *(3)* THE VALUES OF THE SQUARE-WELL NOE POTENTIAL
REMARK 3 50 KCAL/MOL/ANGSTROM**2.
REMARK 3 *(4)* THE VALUES OF F(PHI) ARE CALCULATED WITH A FORCE
REMARK 3 CONSTANT OF 200 KCAL/MOL/RAD**2. F(PHI) IS A
REMARK 3 SQUARE-WELL DIHEDRAL POTENTIAL WHICH IS USED TO
REMARK 3 RESTRICT THE RANGES OF TORSION ANGLES.
REMARK 3 *(5)* THE VALUE OF THE VAN DER WAALS REPULSION TERM
REMARK 3 F(REPEL) IS CALCULATED WITH A FORCE CONSTANT OF
REMARK 3 4 KCAL/MOL/ANGSTROM**4 WITH THE HARD SPHERE
REMARK 3 VAN DER WAALS RADII SET TO 0.8 TIMES THE STANDARD
REMARK 3 VALUES USED IN THE *CHARMM* EMPIRICAL ENERGY
REMARK 3 FUNCTION.
REMARK 3 *(6)* F(SYM) IS AN EFFECTIVE HARMONIC POTENTIAL USED TO
REMARK 3 MAINTAIN SYMMETRY BETWEEN THE TWO SUBUNITS WITH
REMARK 3 A FORCE CONSTANT SET TO 300.0 KCAL/MOL/ANGSTROMS**2
REMARK 3 *(7)* THE IMPROPER TERMS SERVE TO MAINTAIN PLANARITY
REMARK 3 AND APPROPRIATE CHIRALITY. THEY ALSO MAINTAIN THE
REMARK 3 PEPTIDE BONDS OF ALL RESIDUES (WITH THE EXCEPTION
REMARK 3 OF PROLINES) IN THE TRANS CONFORMATION. IN THE
REMARK 3 DYNAMICAL SIMULATED ANNEALING CALCULATIONS.
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE INTERLEUKIN-8 DIMER IN SOLUTION
REMARK 3 DERIVED FROM NMR EXPERIMENTS IS BASED ON 1880 EXPERIMENTAL
REMARK 3 DISTANCE RESTRAINTS (OF WHICH 82 ARE INTERSUBUNIT) AND 362
REMARK 3 TORSION ANGLE RESTRAINTS DERIVED FROM NOE AND COUPLING
REMARK 3 CONSTANT MEASUREMENTS. A COMPLETE LIST OF EXPERIMENTAL
REMARK 3 RESTRAINTS HAS BEEN DEPOSITED WITH THE BROOKHAVEN PROTEIN
REMARK 3 DATA BANK AND IS LOCATED IN ENTRY R1IL8MR.
REMARK 3
REMARK 3 A TOTAL OF 30 STRUCTURES CONSISTENT WITH THE NMR DATA
REMARK 3 WERE CALCULATED AND ARE GIVEN IN THIS ENTRY. THE PROTEIN
REMARK 3 DATA BANK ENTRY *1IL8* CONTAIN THE COORDINATES OBTAINED BY
REMARK 3 AVERAGING THE COORDINATES OF THESE INDIVIDUAL STRUCTURES
REMARK 3 AND SUBJECTING THE RESULTING COORDINATES TO FURTHER
REMARK 3 RESTRAINED MINIMIZATION.
REMARK 3
REMARK 3 THE FIVE N-TERMINAL RESIDUES ARE ILL-DEFINED.
REMARK 3
REMARK 3 THE CYS 9 - CYS 50 DISULFIDE BRIDGE IS LEFT-HANDED.
REMARK 4
REMARK 4 2IL8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178254.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 1-30
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
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 HIS A 18 NE2 HIS A 18 CD2 -0.076
REMARK 500 1 TRP A 57 CG TRP A 57 CD2 -0.108
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 HIS A 18 NE2 HIS A 18 CD2 -0.076
REMARK 500 2 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500 2 HIS B 18 NE2 HIS B 18 CD2 -0.078
REMARK 500 2 TRP B 57 CG TRP B 57 CD2 -0.107
REMARK 500 3 HIS A 18 NE2 HIS A 18 CD2 -0.075
REMARK 500 3 TRP A 57 CG TRP A 57 CD2 -0.109
REMARK 500 3 HIS B 18 NE2 HIS B 18 CD2 -0.077
REMARK 500 3 TRP B 57 CG TRP B 57 CD2 -0.107
REMARK 500 4 HIS A 18 NE2 HIS A 18 CD2 -0.076
REMARK 500 4 TRP A 57 CG TRP A 57 CD2 -0.106
REMARK 500 4 HIS B 18 NE2 HIS B 18 CD2 -0.077
REMARK 500 4 TRP B 57 CG TRP B 57 CD2 -0.107
REMARK 500 5 HIS A 18 NE2 HIS A 18 CD2 -0.076
REMARK 500 5 TRP A 57 CG TRP A 57 CD2 -0.108
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 HIS A 18 NE2 HIS A 18 CD2 -0.077
REMARK 500 6 TRP A 57 CG TRP A 57 CD2 -0.109
REMARK 500 6 HIS B 18 NE2 HIS B 18 CD2 -0.078
REMARK 500 6 TRP B 57 CG TRP B 57 CD2 -0.110
REMARK 500 7 HIS A 18 NE2 HIS A 18 CD2 -0.077
REMARK 500 7 TRP A 57 CG TRP A 57 CD2 -0.109
REMARK 500 7 HIS B 18 NE2 HIS B 18 CD2 -0.077
REMARK 500 7 TRP B 57 CG TRP B 57 CD2 -0.109
REMARK 500 8 HIS A 18 NE2 HIS A 18 CD2 -0.077
REMARK 500 8 TRP A 57 CG TRP A 57 CD2 -0.109
REMARK 500 8 HIS B 18 NE2 HIS B 18 CD2 -0.077
REMARK 500 8 TRP B 57 CG TRP B 57 CD2 -0.108
REMARK 500 9 HIS A 18 NE2 HIS A 18 CD2 -0.076
REMARK 500 9 TRP A 57 CG TRP A 57 CD2 -0.108
REMARK 500 9 HIS B 18 NE2 HIS B 18 CD2 -0.075
REMARK 500 9 TRP B 57 CG TRP B 57 CD2 -0.108
REMARK 500 10 HIS A 18 NE2 HIS A 18 CD2 -0.075
REMARK 500 10 TRP A 57 CG TRP A 57 CD2 -0.108
REMARK 500 10 HIS B 18 NE2 HIS B 18 CD2 -0.076
REMARK 500 10 TRP B 57 CG TRP B 57 CD2 -0.108
REMARK 500 11 HIS A 18 NE2 HIS A 18 CD2 -0.075
REMARK 500 11 TRP A 57 CG TRP A 57 CD2 -0.108
REMARK 500 11 HIS B 18 NE2 HIS B 18 CD2 -0.077
REMARK 500 11 TRP B 57 CG TRP B 57 CD2 -0.108
REMARK 500 12 HIS A 18 NE2 HIS A 18 CD2 -0.076
REMARK 500 12 TRP A 57 CG TRP A 57 CD2 -0.109
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 HIS A 18 NE2 HIS A 18 CD2 -0.076
REMARK 500 13 TRP A 57 CG TRP A 57 CD2 -0.107
REMARK 500
REMARK 500 THIS ENTRY HAS 120 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. = -6.3 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. = -6.9 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. = 5.4 DEGREES
REMARK 500 2 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -6.9 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. = 8.8 DEGREES
REMARK 500 2 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 3 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 3 TRP A 57 NE1 - CE2 - CZ2 ANGL. DEV. = 9.0 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. = -6.3 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. = 8.7 DEGREES
REMARK 500 4 TRP A 57 NE1 - CE2 - CD2 ANGL. DEV. = -6.9 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. = 5.6 DEGREES
REMARK 500 4 TRP B 57 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 4 TRP B 57 NE1 - CE2 - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 5 TRP A 57 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 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. = -6.9 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. = -6.3 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. = 8.8 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. = -6.4 DEGREES
REMARK 500 7 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 240 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 -18.48 -158.33
REMARK 500 1 ILE A 10 -61.11 -96.35
REMARK 500 1 ASN A 36 -144.96 -146.84
REMARK 500 1 ASP A 45 -5.34 -59.59
REMARK 500 1 LYS B 3 -18.42 -158.30
REMARK 500 1 ILE B 10 -61.13 -96.37
REMARK 500 1 ASN B 36 -144.97 -146.83
REMARK 500 1 ASP B 45 -5.27 -59.63
REMARK 500 2 ILE A 10 -65.86 -99.10
REMARK 500 2 PRO A 19 -6.74 -57.32
REMARK 500 2 SER A 30 119.66 -37.92
REMARK 500 2 ASP A 45 -7.64 -59.23
REMARK 500 2 ILE B 10 -65.91 -99.14
REMARK 500 2 PRO B 19 -6.78 -57.24
REMARK 500 2 SER B 30 119.66 -37.96
REMARK 500 2 ASP B 45 -7.64 -59.24
REMARK 500 3 ARG A 6 -173.80 -68.90
REMARK 500 3 ILE A 10 -64.81 -94.85
REMARK 500 3 SER A 30 121.11 -39.78
REMARK 500 3 ASN A 36 -156.43 -141.03
REMARK 500 3 ASP A 45 -7.48 -58.99
REMARK 500 3 ARG B 6 -173.74 -68.98
REMARK 500 3 ILE B 10 -64.89 -94.75
REMARK 500 3 SER B 30 121.07 -39.85
REMARK 500 3 ASN B 36 -156.40 -141.10
REMARK 500 3 ASP B 45 -7.46 -58.87
REMARK 500 4 PHE A 17 -165.79 -114.61
REMARK 500 4 ASN A 36 -151.32 -144.82
REMARK 500 4 ASP A 45 -5.52 -59.05
REMARK 500 4 PHE B 17 -165.80 -114.66
REMARK 500 4 ASN B 36 -151.30 -144.89
REMARK 500 4 ASP B 45 -5.39 -59.08
REMARK 500 4 PRO B 53 -5.03 -59.97
REMARK 500 5 SER A 14 44.14 -101.80
REMARK 500 5 SER A 30 124.12 -38.14
REMARK 500 5 ASN A 36 -150.59 -142.92
REMARK 500 5 ASP A 45 -8.68 -59.46
REMARK 500 5 SER B 14 44.23 -101.79
REMARK 500 5 SER B 30 124.19 -38.05
REMARK 500 5 ASN B 36 -150.55 -142.88
REMARK 500 5 ASP B 45 -8.66 -59.39
REMARK 500 6 ARG A 6 -174.98 -69.80
REMARK 500 6 ILE A 10 -63.46 -90.11
REMARK 500 6 PRO A 32 0.88 -66.09
REMARK 500 6 ASN A 36 -148.68 -141.50
REMARK 500 6 ASP A 45 -5.90 -59.32
REMARK 500 6 PRO A 53 -5.45 -59.66
REMARK 500 6 ARG B 6 -174.91 -69.93
REMARK 500 6 ILE B 10 -63.46 -90.07
REMARK 500 6 PRO B 32 0.82 -65.99
REMARK 500
REMARK 500 THIS ENTRY HAS 284 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 0.10 SIDE CHAIN
REMARK 500 1 ARG A 47 0.29 SIDE CHAIN
REMARK 500 1 ARG A 60 0.30 SIDE CHAIN
REMARK 500 1 ARG A 68 0.24 SIDE CHAIN
REMARK 500 1 ARG B 6 0.32 SIDE CHAIN
REMARK 500 1 ARG B 26 0.10 SIDE CHAIN
REMARK 500 1 ARG B 47 0.29 SIDE CHAIN
REMARK 500 1 ARG B 60 0.30 SIDE CHAIN
REMARK 500 1 ARG B 68 0.24 SIDE CHAIN
REMARK 500 2 ARG A 6 0.12 SIDE CHAIN
REMARK 500 2 ARG A 60 0.27 SIDE CHAIN
REMARK 500 2 ARG A 68 0.25 SIDE CHAIN
REMARK 500 2 ARG B 6 0.12 SIDE CHAIN
REMARK 500 2 ARG B 60 0.27 SIDE CHAIN
REMARK 500 2 ARG B 68 0.25 SIDE CHAIN
REMARK 500 3 ARG A 6 0.24 SIDE CHAIN
REMARK 500 3 ARG A 26 0.12 SIDE CHAIN
REMARK 500 3 ARG A 47 0.27 SIDE CHAIN
REMARK 500 3 ARG A 60 0.32 SIDE CHAIN
REMARK 500 3 ARG A 68 0.24 SIDE CHAIN
REMARK 500 3 ARG B 6 0.24 SIDE CHAIN
REMARK 500 3 ARG B 26 0.12 SIDE CHAIN
REMARK 500 3 ARG B 47 0.27 SIDE CHAIN
REMARK 500 3 ARG B 60 0.32 SIDE CHAIN
REMARK 500 3 ARG B 68 0.24 SIDE CHAIN
REMARK 500 4 ARG A 6 0.28 SIDE CHAIN
REMARK 500 4 ARG A 26 0.32 SIDE CHAIN
REMARK 500 4 ARG A 47 0.32 SIDE CHAIN
REMARK 500 4 ARG A 60 0.29 SIDE CHAIN
REMARK 500 4 ARG A 68 0.29 SIDE CHAIN
REMARK 500 4 ARG B 6 0.28 SIDE CHAIN
REMARK 500 4 ARG B 26 0.32 SIDE CHAIN
REMARK 500 4 ARG B 47 0.32 SIDE CHAIN
REMARK 500 4 ARG B 60 0.29 SIDE CHAIN
REMARK 500 4 ARG B 68 0.29 SIDE CHAIN
REMARK 500 5 ARG A 6 0.32 SIDE CHAIN
REMARK 500 5 ARG A 26 0.23 SIDE CHAIN
REMARK 500 5 ARG A 47 0.32 SIDE CHAIN
REMARK 500 5 ARG A 60 0.20 SIDE CHAIN
REMARK 500 5 ARG A 68 0.29 SIDE CHAIN
REMARK 500 5 ARG B 6 0.32 SIDE CHAIN
REMARK 500 5 ARG B 26 0.23 SIDE CHAIN
REMARK 500 5 ARG B 47 0.32 SIDE CHAIN
REMARK 500 5 ARG B 60 0.20 SIDE CHAIN
REMARK 500 5 ARG B 68 0.29 SIDE CHAIN
REMARK 500 6 ARG A 6 0.08 SIDE CHAIN
REMARK 500 6 ARG A 47 0.31 SIDE CHAIN
REMARK 500 6 ARG A 60 0.22 SIDE CHAIN
REMARK 500 6 ARG A 68 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 280 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IL8 RELATED DB: PDB
DBREF 2IL8 A 1 72 UNP P10145 IL8_HUMAN 28 99
DBREF 2IL8 B 1 72 UNP P10145 IL8_HUMAN 28 99
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
HELIX 1 1 HIS A 18 LYS A 20 5 3
HELIX 2 2 GLU A 55 SER A 72 1 18
HELIX 3 3 HIS B 18 LYS B 20 5 3
HELIX 4 4 GLU B 55 SER B 72 1 18
SHEET 1 A 6 ARG A 47 LEU A 51 0
SHEET 2 A 6 GLU A 38 LEU A 43 -1 O ILE A 39 N LEU A 51
SHEET 3 A 6 ILE A 22 ILE A 28 -1 N LYS A 23 O LYS A 42
SHEET 4 A 6 ILE B 22 ILE B 28 -1 N LEU B 25 O VAL A 27
SHEET 5 A 6 ILE B 39 LEU B 43 -1 O ILE B 40 N ARG B 26
SHEET 6 A 6 ARG B 47 LEU B 51 -1 O ARG B 47 N LEU B 43
SSBOND 1 CYS A 7 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 50 1555 1555 2.02
SSBOND 3 CYS B 7 CYS B 34 1555 1555 2.02
SSBOND 4 CYS B 9 CYS B 50 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 - r 9 2 Bytes