Header list of 1smz.pdb file
Complete list - 2 20 Bytes
HEADER TRANSPORT PROTEIN 10-MAR-04 1SMZ
TITLE STRUCTURE OF TRANSPORTAN IN PHOSPHOLIPID BICELLAR SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSPORTAN IN BICELLAR SOLUTION WITH [DMPC]/[DHPC]=0.33;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 DOES NOT OCCUR NATURALLY.
KEYWDS TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR E.BARANY-WALLJE,A.ANDERSSON,L.MALER,A.GRASLUND
REVDAT 4 02-MAR-22 1SMZ 1 REMARK
REVDAT 3 24-FEB-09 1SMZ 1 VERSN
REVDAT 2 22-JUN-04 1SMZ 1 JRNL
REVDAT 1 16-MAR-04 1SMZ 0
JRNL AUTH A.ANDERSSON
JRNL TITL NMR SOLUTION STRUCTURE AND POSITION OF TRANSPORTAN IN
JRNL TITL 2 NEUTRAL PHOSPHOLIPID BICELLES
JRNL REF FEBS LETT. V. 567 265 2004
JRNL REFN ISSN 0014-5793
JRNL PMID 15178334
JRNL DOI 10.1016/J.FEBSLET.2004.04.079
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, SUPPOSE
REMARK 3 AUTHORS : WUTHRICH, K. ET AL (DYANA), SMITH, J. (SUPPOSE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 220 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS
REMARK 4
REMARK 4 1SMZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021840.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM TRANSPORTAN IN NEUTRAL
REMARK 210 BICELLES, [LIPID]=300MM [DMPC]/
REMARK 210 [PHPC]=0.33, 50MM PHOSPHATE
REMARK 210 BUFFER, 90% H2O, 10% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000.1, VNMR 6.1 A,
REMARK 210 PROCHECK
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 25 STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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 19 H ALA A 23 1.59
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 TRP A 2 73.20 55.04
REMARK 500 1 TYR A 9 30.37 -167.92
REMARK 500 2 TRP A 2 -62.67 -131.35
REMARK 500 2 TYR A 9 27.89 -143.58
REMARK 500 3 ILE A 14 -50.63 -136.53
REMARK 500 4 TRP A 2 52.16 -165.84
REMARK 500 4 THR A 3 -152.14 -162.08
REMARK 500 4 TYR A 9 32.00 -157.79
REMARK 500 4 ILE A 14 -55.66 -121.07
REMARK 500 5 TRP A 2 54.22 72.43
REMARK 500 5 THR A 3 -144.60 -90.69
REMARK 500 5 TYR A 9 32.25 -156.65
REMARK 500 5 ILE A 14 -55.67 -121.29
REMARK 500 6 TYR A 9 33.16 -159.56
REMARK 500 7 TRP A 2 53.28 78.50
REMARK 500 7 THR A 3 -148.87 -92.58
REMARK 500 7 LEU A 10 33.08 -95.29
REMARK 500 7 LYS A 13 -80.81 -41.25
REMARK 500 8 TRP A 2 -64.98 -126.29
REMARK 500 8 LEU A 10 45.45 -92.03
REMARK 500 8 ILE A 14 -55.63 -120.99
REMARK 500 9 TRP A 2 105.00 -174.93
REMARK 500 9 THR A 3 -154.04 -119.32
REMARK 500 9 TYR A 9 30.48 -154.90
REMARK 500 9 ILE A 14 -55.79 -122.55
REMARK 500 10 TRP A 2 140.94 72.00
REMARK 500 10 LEU A 10 47.27 -95.15
REMARK 500 11 TRP A 2 -77.00 -61.85
REMARK 500 11 THR A 3 -148.61 -160.65
REMARK 500 11 TYR A 9 30.95 -162.47
REMARK 500 11 LYS A 13 -77.58 -45.40
REMARK 500 12 TRP A 2 154.81 -45.38
REMARK 500 12 THR A 3 155.45 -37.21
REMARK 500 12 LEU A 11 41.05 -96.68
REMARK 500 13 THR A 3 -147.78 -157.60
REMARK 500 14 TRP A 2 95.10 65.59
REMARK 500 14 LEU A 11 -70.44 -40.34
REMARK 500 14 LYS A 13 -53.52 71.06
REMARK 500 15 LEU A 4 -31.00 -38.49
REMARK 500 15 LYS A 13 -52.82 79.36
REMARK 500 16 TRP A 2 75.08 71.28
REMARK 500 16 LEU A 4 -46.68 -137.14
REMARK 500 17 THR A 3 -82.82 -144.64
REMARK 500 17 LEU A 4 -55.78 72.71
REMARK 500 17 ASN A 15 -30.24 -39.66
REMARK 500 18 THR A 3 170.66 -45.34
REMARK 500 18 LEU A 4 -46.16 -132.56
REMARK 500 19 TYR A 9 28.47 -164.51
REMARK 500 19 LYS A 13 -53.96 71.04
REMARK 500 20 TRP A 2 44.30 -173.58
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SMZ A 1 27 PDB 1SMZ 1SMZ 1 27
SEQRES 1 A 27 GLY TRP THR LEU ASN SER ALA GLY TYR LEU LEU GLY LYS
SEQRES 2 A 27 ILE ASN LEU LYS ALA LEU ALA ALA LEU ALA LYS LYS ILE
SEQRES 3 A 27 LEU
HELIX 1 1 THR A 3 GLY A 8 1 6
HELIX 2 2 ILE A 14 LEU A 27 1 14
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 - 2 20 Bytes