Header list of 1kmr.pdb file
Complete list - 23 20 Bytes
HEADER LIPID BINDING PROTEIN 17-DEC-01 1KMR
TITLE SOLUTION NMR STRUCTURE OF SURFACTANT PROTEIN B (11-25) (SP-B11-25)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PULMONARY SURFACTANT-ASSOCIATED PROTEIN B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 211-225, NUMBERED 11-25;
COMPND 5 SYNONYM: SP-B, PULMONARY SURFACTANT-ASSOCIATED PROTEOLIPID SPL(PHE),
COMPND 6 18 KDA PULMONARY-SURFACTANT PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PROTEIN IS NATURALLY FOUND IN HOMO SAPIENS (HUMANS).
KEYWDS HELIX, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR J.W.KURUTZ,K.Y.C.LEE
REVDAT 4 23-FEB-22 1KMR 1 REMARK
REVDAT 3 24-FEB-09 1KMR 1 VERSN
REVDAT 2 01-APR-03 1KMR 1 JRNL
REVDAT 1 07-AUG-02 1KMR 0
JRNL AUTH J.W.KURUTZ,K.Y.LEE
JRNL TITL NMR STRUCTURE OF LUNG SURFACTANT PEPTIDE SP-B(11-25).
JRNL REF BIOCHEMISTRY V. 41 9627 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12135384
JRNL DOI 10.1021/BI016077X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, INSIGHT II 98
REMARK 3 AUTHORS : VARIAN ASSOCIATES, INC. (VNMR),
REMARK 3 MSI/BIOSYM/ACCELRYS (INSIGHT II)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KMR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015118.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NO ADDITIONAL SALT OR BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.25 MM PEPTIDE, 0.1 MM DSS-D6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, DISCOVER 2.98,
REMARK 210 INSIGHT II 98
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 78
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: WET WATER SUPPRESSION
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 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 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ALA A 13 N - CA - CB ANGL. DEV. = -12.8 DEGREES
REMARK 500 1 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ILE A 22 CB - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 2 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ALA A 13 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 2 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ILE A 22 CB - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ALA A 13 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 3 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ILE A 22 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 4 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 ALA A 13 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 4 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ILE A 22 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 5 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 ALA A 13 N - CA - CB ANGL. DEV. = -9.6 DEGREES
REMARK 500 5 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ILE A 22 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 6 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ALA A 13 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 6 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ILE A 22 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 7 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ALA A 13 N - CA - CB ANGL. DEV. = -9.9 DEGREES
REMARK 500 7 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ILE A 22 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 8 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 8 ALA A 13 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 8 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 8 ILE A 22 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 9 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 ALA A 13 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 9 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ILE A 22 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 10 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ALA A 13 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 10 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 10 ILE A 22 CB - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 11 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 11 ALA A 13 N - CA - CB ANGL. DEV. = -12.8 DEGREES
REMARK 500 11 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ILE A 22 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 12 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ALA A 13 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 12 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ILE A 22 CB - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 13 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 13 ALA A 13 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 64 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 ARG A 12 -132.28 -139.63
REMARK 500 2 ARG A 12 -128.74 -143.48
REMARK 500 3 ARG A 12 -131.09 -138.25
REMARK 500 4 ARG A 12 -136.40 -135.69
REMARK 500 5 ARG A 12 -131.43 -145.84
REMARK 500 5 LYS A 24 -71.73 76.92
REMARK 500 6 ARG A 12 -132.40 -144.22
REMARK 500 7 ARG A 12 -139.25 -139.04
REMARK 500 8 ARG A 12 -131.67 -138.39
REMARK 500 9 ARG A 12 -128.05 -141.75
REMARK 500 9 LYS A 24 60.93 63.80
REMARK 500 10 ARG A 12 -133.51 -136.99
REMARK 500 10 LYS A 24 60.50 61.06
REMARK 500 11 ARG A 12 -137.35 -135.02
REMARK 500 12 ARG A 12 -132.91 -141.86
REMARK 500 12 LYS A 24 60.09 61.16
REMARK 500 13 ARG A 12 -134.76 -141.09
REMARK 500 13 LYS A 24 60.54 64.28
REMARK 500 14 ARG A 12 -127.70 -142.00
REMARK 500 14 LYS A 24 52.21 80.62
REMARK 500 15 ARG A 12 -128.12 -148.23
REMARK 500 16 ARG A 12 -131.95 -145.83
REMARK 500 17 ARG A 12 -128.14 -148.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DFW RELATED DB: PDB
REMARK 900 CD/FTIR STRUCTURE OF SURFACTANT PROTEIN B (1-25) (SP-B 1-25)
DBREF 1KMR A 11 25 UNP P07988 PSPB_HUMAN 211 225
SEQRES 1 A 15 CYS ARG ALA LEU ILE LYS ARG ILE GLN ALA MET ILE PRO
SEQRES 2 A 15 LYS GLY
HELIX 1 1 ARG A 12 ILE A 22 1 11
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