Header list of 1mi2.pdb file
Complete list - b 23 2 Bytes
HEADER CYTOKINE 24-OCT-97 1MI2
TITLE SOLUTION STRUCTURE OF MURINE MACROPHAGE INFLAMMATORY PROTEIN-2, NMR,
TITLE 2 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE INFLAMMATORY PROTEIN-2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS MIP-2, CHEMOKINE, CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.SHAO,L.F.JERVA,J.WEST,E.LOLIS,B.I.SCHWEITZER
REVDAT 4 23-FEB-22 1MI2 1 REMARK
REVDAT 3 24-FEB-09 1MI2 1 VERSN
REVDAT 2 20-JAN-00 1MI2 1 JRNL
REVDAT 1 29-APR-98 1MI2 0
JRNL AUTH W.SHAO,L.F.JERVA,J.WEST,E.LOLIS,B.I.SCHWEITZER
JRNL TITL SOLUTION STRUCTURE OF MURINE MACROPHAGE INFLAMMATORY
JRNL TITL 2 PROTEIN-2.
JRNL REF BIOCHEMISTRY V. 37 8303 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9622482
JRNL DOI 10.1021/BI980112R
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: THE STRUCTURES OF THE MURINE MACROPHAGE
REMARK 3 INFLAMMATORY PROTEIN-2 (MIP-2) WERE GENERATED USING TORSION-
REMARK 3 ANGLE MOLECULAR DYNAMICS APPROACH (STEIN, E.G., RICE, L.M., &
REMARK 3 BRUNGER, A.T. (1997) J. MAGN. RESON. 124, 154-164) AND X-PLOR
REMARK 3 3.851 (ONLINE)(BRUNGER, A.T. (1992) X-PLOR (VERSION 3.1) MANUAL,
REMARK 3 YALE UNIVERSITY PRESS) BASED ON A TOTAL OF 2740 EXPERIMENTAL
REMARK 3 RESTRAINTS, COMPRISING 2596 NOE-DERIVED DISTANCE RESTRAINTS, 44
REMARK 3 DISTANCE RESTRAINTS FOR 22 HYDROGEN BONDS, AND 100 TORSION ANGLE
REMARK 3 RESTRAINTS DERIVED FROM NOE AND COUPLING CONSTANT MEASUREMENTS.
REMARK 4
REMARK 4 1MI2 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_1000175011.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; HSQC; COSY; ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : TORSION-ANGLE MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ASN A 73 O
REMARK 470 ASN B 73 O
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 LEU A 15 H ASP A 53 1.45
REMARK 500 O LEU B 15 H ASP B 53 1.45
REMARK 500 O GLN A 60 H GLN A 64 1.49
REMARK 500 O GLN B 60 H GLN B 64 1.49
REMARK 500 O VAL B 18 N PHE B 20 1.94
REMARK 500 O VAL A 18 N PHE A 20 1.94
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 GLU A 6 -121.45 -127.30
REMARK 500 1 ARG A 8 -103.88 -98.69
REMARK 500 1 CYS A 9 -144.15 -144.84
REMARK 500 1 ARG A 17 60.25 -163.44
REMARK 500 1 VAL A 18 165.11 -40.85
REMARK 500 1 ASP A 19 72.67 -34.96
REMARK 500 1 PHE A 20 -78.73 -40.94
REMARK 500 1 ILE A 23 98.60 -39.04
REMARK 500 1 PRO A 33 49.59 -76.42
REMARK 500 1 HIS A 34 -51.92 177.85
REMARK 500 1 ALA A 36 21.69 42.06
REMARK 500 1 GLN A 37 138.18 -175.10
REMARK 500 1 GLN A 48 95.86 -164.71
REMARK 500 1 VAL A 50 -159.91 -170.67
REMARK 500 1 ASP A 53 173.22 -23.03
REMARK 500 1 ALA A 56 68.53 35.29
REMARK 500 1 GLU B 6 -121.51 -127.35
REMARK 500 1 ARG B 8 -103.94 -98.71
REMARK 500 1 CYS B 9 -144.20 -144.76
REMARK 500 1 ARG B 17 60.25 -163.44
REMARK 500 1 VAL B 18 165.00 -40.75
REMARK 500 1 ASP B 19 72.57 -34.92
REMARK 500 1 PHE B 20 -78.81 -40.74
REMARK 500 1 ILE B 23 98.60 -38.95
REMARK 500 1 PRO B 33 49.47 -76.44
REMARK 500 1 HIS B 34 -51.84 177.88
REMARK 500 1 ALA B 36 21.60 42.22
REMARK 500 1 GLN B 37 138.21 -175.16
REMARK 500 1 GLN B 48 95.92 -164.77
REMARK 500 1 VAL B 50 -159.90 -170.64
REMARK 500 1 ASP B 53 173.14 -23.05
REMARK 500 1 ALA B 56 68.50 35.26
REMARK 500 2 VAL A 2 -165.85 -67.95
REMARK 500 2 VAL A 3 86.10 -58.37
REMARK 500 2 GLU A 6 42.43 -91.46
REMARK 500 2 LEU A 7 48.17 -85.88
REMARK 500 2 ARG A 8 -122.30 -98.14
REMARK 500 2 CYS A 9 -158.36 -133.92
REMARK 500 2 ARG A 17 55.27 -176.56
REMARK 500 2 VAL A 18 169.82 -41.37
REMARK 500 2 ASP A 19 74.73 -38.41
REMARK 500 2 PHE A 20 -78.36 -44.20
REMARK 500 2 ILE A 23 111.55 -37.59
REMARK 500 2 SER A 25 126.58 -170.09
REMARK 500 2 PRO A 33 47.36 -77.55
REMARK 500 2 HIS A 34 -49.69 -179.98
REMARK 500 2 ALA A 36 16.91 48.55
REMARK 500 2 GLN A 48 101.67 -172.91
REMARK 500 2 VAL A 50 -168.76 -170.76
REMARK 500 2 ASP A 53 -163.29 -46.76
REMARK 500
REMARK 500 THIS ENTRY HAS 720 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 8 0.24 SIDE CHAIN
REMARK 500 1 ARG A 17 0.18 SIDE CHAIN
REMARK 500 1 ARG B 8 0.24 SIDE CHAIN
REMARK 500 1 ARG B 17 0.18 SIDE CHAIN
REMARK 500 2 ARG A 8 0.14 SIDE CHAIN
REMARK 500 2 ARG A 17 0.31 SIDE CHAIN
REMARK 500 2 ARG B 8 0.14 SIDE CHAIN
REMARK 500 2 ARG B 17 0.31 SIDE CHAIN
REMARK 500 3 ARG A 8 0.16 SIDE CHAIN
REMARK 500 3 ARG A 17 0.30 SIDE CHAIN
REMARK 500 3 ARG B 8 0.16 SIDE CHAIN
REMARK 500 3 ARG B 17 0.30 SIDE CHAIN
REMARK 500 4 ARG A 8 0.28 SIDE CHAIN
REMARK 500 4 ARG A 17 0.28 SIDE CHAIN
REMARK 500 4 ARG B 8 0.28 SIDE CHAIN
REMARK 500 4 ARG B 17 0.28 SIDE CHAIN
REMARK 500 5 ARG A 8 0.31 SIDE CHAIN
REMARK 500 5 ARG A 17 0.28 SIDE CHAIN
REMARK 500 5 ARG B 8 0.31 SIDE CHAIN
REMARK 500 5 ARG B 17 0.28 SIDE CHAIN
REMARK 500 6 ARG A 17 0.11 SIDE CHAIN
REMARK 500 6 ARG B 17 0.11 SIDE CHAIN
REMARK 500 7 ARG A 8 0.10 SIDE CHAIN
REMARK 500 7 ARG A 17 0.22 SIDE CHAIN
REMARK 500 7 ARG B 8 0.10 SIDE CHAIN
REMARK 500 7 ARG B 17 0.22 SIDE CHAIN
REMARK 500 8 ARG A 8 0.30 SIDE CHAIN
REMARK 500 8 ARG A 17 0.20 SIDE CHAIN
REMARK 500 8 ARG B 8 0.30 SIDE CHAIN
REMARK 500 8 ARG B 17 0.20 SIDE CHAIN
REMARK 500 9 ARG A 8 0.14 SIDE CHAIN
REMARK 500 9 ARG A 17 0.29 SIDE CHAIN
REMARK 500 9 ARG B 8 0.14 SIDE CHAIN
REMARK 500 9 ARG B 17 0.29 SIDE CHAIN
REMARK 500 10 ARG A 8 0.16 SIDE CHAIN
REMARK 500 10 ARG A 17 0.18 SIDE CHAIN
REMARK 500 10 ARG B 8 0.16 SIDE CHAIN
REMARK 500 10 ARG B 17 0.18 SIDE CHAIN
REMARK 500 11 ARG A 8 0.16 SIDE CHAIN
REMARK 500 11 ARG A 17 0.19 SIDE CHAIN
REMARK 500 11 ARG B 8 0.16 SIDE CHAIN
REMARK 500 11 ARG B 17 0.19 SIDE CHAIN
REMARK 500 12 ARG A 8 0.29 SIDE CHAIN
REMARK 500 12 ARG A 17 0.27 SIDE CHAIN
REMARK 500 12 ARG B 8 0.29 SIDE CHAIN
REMARK 500 12 ARG B 17 0.27 SIDE CHAIN
REMARK 500 13 ARG A 8 0.23 SIDE CHAIN
REMARK 500 13 ARG B 8 0.23 SIDE CHAIN
REMARK 500 14 ARG A 17 0.16 SIDE CHAIN
REMARK 500 14 ARG B 17 0.16 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 74 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MI2 A 1 73 UNP P10889 MIP2_MOUSE 28 100
DBREF 1MI2 B 1 73 UNP P10889 MIP2_MOUSE 28 100
SEQRES 1 A 73 ALA VAL VAL ALA SER GLU LEU ARG CYS GLN CYS LEU LYS
SEQRES 2 A 73 THR LEU PRO ARG VAL ASP PHE LYS ASN ILE GLN SER LEU
SEQRES 3 A 73 SER VAL THR PRO PRO GLY PRO HIS CYS ALA GLN THR GLU
SEQRES 4 A 73 VAL ILE ALA THR LEU LYS GLY GLY GLN LYS VAL CYS LEU
SEQRES 5 A 73 ASP PRO GLU ALA PRO LEU VAL GLN LYS ILE ILE GLN LYS
SEQRES 6 A 73 ILE LEU ASN LYS GLY LYS ALA ASN
SEQRES 1 B 73 ALA VAL VAL ALA SER GLU LEU ARG CYS GLN CYS LEU LYS
SEQRES 2 B 73 THR LEU PRO ARG VAL ASP PHE LYS ASN ILE GLN SER LEU
SEQRES 3 B 73 SER VAL THR PRO PRO GLY PRO HIS CYS ALA GLN THR GLU
SEQRES 4 B 73 VAL ILE ALA THR LEU LYS GLY GLY GLN LYS VAL CYS LEU
SEQRES 5 B 73 ASP PRO GLU ALA PRO LEU VAL GLN LYS ILE ILE GLN LYS
SEQRES 6 B 73 ILE LEU ASN LYS GLY LYS ALA ASN
HELIX 1 1 GLN A 60 GLY A 70 1 11
HELIX 2 2 GLN B 60 GLY B 70 1 11
SHEET 1 A 3 SER A 25 THR A 29 0
SHEET 2 A 3 GLU A 39 THR A 43 -1 N THR A 43 O SER A 25
SHEET 3 A 3 LYS A 49 LEU A 52 -1 N LEU A 52 O VAL A 40
SHEET 1 B 3 SER B 25 THR B 29 0
SHEET 2 B 3 GLU B 39 THR B 43 -1 N THR B 43 O SER B 25
SHEET 3 B 3 LYS B 49 LEU B 52 -1 N LEU B 52 O VAL B 40
SSBOND 1 CYS A 9 CYS A 35 1555 1555 2.02
SSBOND 2 CYS A 11 CYS A 51 1555 1555 2.02
SSBOND 3 CYS B 9 CYS B 35 1555 1555 2.02
SSBOND 4 CYS B 11 CYS B 51 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 - b 23 2 Bytes