Header list of 1ieh.pdb file
Complete list - b 23 2 Bytes
HEADER IMMUNE SYSTEM 09-APR-01 1IEH
TITLE SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH
TITLE 2 HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRUC.D4.4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SINGLE DOMAIN ANTIBODY FROM A NAIVE LLAMA LIBRARY;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA;
SOURCE 3 ORGANISM_COMMON: LLAMA;
SOURCE 4 ORGANISM_TAXID: 9844;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TWO PLEATED BETA-SHEET, IMMUNOGLOBULIN BETA-BARREL, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR W.VRANKEN,D.TOLKATCHEV,P.XU,J.TANHA,Z.CHEN,S.NARANG,F.NI
REVDAT 3 23-FEB-22 1IEH 1 REMARK
REVDAT 2 24-FEB-09 1IEH 1 VERSN
REVDAT 1 07-AUG-02 1IEH 0
JRNL AUTH W.VRANKEN,D.TOLKATCHEV,P.XU,J.TANHA,Z.CHEN,S.NARANG,F.NI
JRNL TITL SOLUTION STRUCTURE OF A LLAMA SINGLE-DOMAIN ANTIBODY WITH
JRNL TITL 2 HYDROPHOBIC RESIDUES TYPICAL OF THE VH/VL INTERFACE.
JRNL REF BIOCHEMISTRY V. 41 8570 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12093273
JRNL DOI 10.1021/BI012169A
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, ARIA 1.0
REMARK 3 AUTHORS : FRANK DELAGLIO, STEPHAN GRZESIEK, AD BAX, GEERTEN
REMARK 3 W. VUISTER, GUANG ZHU, JOHN PFEIFER (NMRPIPE),
REMARK 3 LINGE, NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NO MANUAL ASSIGNMENTS OF NOE PEAKS WERE
REMARK 3 INITIALLY PERFORMED - THE GLOBAL FOLD OF THE PROTEIN WAS
REMARK 3 DETERMINED USING
REMARK 3 RESTRAINTS WITH LOW AMBIGUITY. THE SET OF GLOBAL FOLD STRUCTURES
REMARK 3 SERVED AS
REMARK 3 AN ASSIGNMENT FILTER TO REDUCE THE AMBIGUITY OF THE OTHER
REMARK 3 RESTRAINTS. THE
REMARK 3 RESTRAINT LIST AND STRUCTURES WERE FURTHER REFINED BY MANUALLY
REMARK 3 CHOOSING
REMARK 3 POSSIBILITIES FROM THE RESTRAINTS WITH LOW AMBIGUITY (BASED ON THE
REMARK 3 SPECTRA).
REMARK 4
REMARK 4 1IEH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013207.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.16
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10MM SODIUM PHOSPHATE 150MM NACL
REMARK 210 0.2MM EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D COMBINED 13C/15N-SEPARATED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.1.2, ARIA 1.0, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING USING
REMARK 210 TORSION ANGLE AND CARTESIAN
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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: 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
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 SER A 7 -178.21 -171.82
REMARK 500 1 PRO A 14 90.55 -51.69
REMARK 500 1 SER A 30 30.24 -78.23
REMARK 500 1 SER A 31 -34.85 -150.71
REMARK 500 1 PRO A 41 93.35 -31.80
REMARK 500 1 LYS A 43 -155.74 41.38
REMARK 500 1 LEU A 45 142.58 66.55
REMARK 500 1 ASP A 62 -56.33 75.55
REMARK 500 1 ALA A 75 69.71 -162.57
REMARK 500 1 LYS A 76 -16.21 -167.64
REMARK 500 1 LYS A 87 45.85 -162.24
REMARK 500 1 THR A 91 95.57 -60.31
REMARK 500 1 ALA A 92 -163.93 -175.06
REMARK 500 1 SER A 100 57.79 -143.49
REMARK 500 1 ALA A 106 111.97 63.43
REMARK 500 1 LYS A 122 -13.21 -157.80
REMARK 500 1 LEU A 123 111.60 63.33
REMARK 500 1 ILE A 124 -58.74 -131.38
REMARK 500 1 GLU A 126 16.76 -164.75
REMARK 500 1 GLU A 127 109.04 61.31
REMARK 500 1 LEU A 129 -147.24 56.48
REMARK 500 1 ASN A 130 -59.67 -152.70
REMARK 500 1 HIS A 131 29.39 -163.42
REMARK 500 2 PRO A 14 91.26 -48.83
REMARK 500 2 SER A 25 111.35 -172.60
REMARK 500 2 PHE A 27 -11.79 -168.06
REMARK 500 2 THR A 28 144.01 65.10
REMARK 500 2 SER A 30 14.59 58.38
REMARK 500 2 LEU A 45 153.38 64.66
REMARK 500 2 VAL A 48 -75.94 59.04
REMARK 500 2 ASP A 55 73.90 52.10
REMARK 500 2 SER A 57 -165.99 -65.05
REMARK 500 2 ASP A 62 -12.80 71.41
REMARK 500 2 ARG A 67 -65.01 -122.29
REMARK 500 2 ALA A 75 -62.24 -168.93
REMARK 500 2 LYS A 87 -57.68 -135.30
REMARK 500 2 SER A 88 -20.91 -173.42
REMARK 500 2 THR A 91 90.70 -60.71
REMARK 500 2 ALA A 92 -171.06 -172.58
REMARK 500 2 ALA A 106 96.74 67.61
REMARK 500 2 SER A 116 -117.92 -159.70
REMARK 500 2 SER A 117 -13.75 69.62
REMARK 500 2 LYS A 122 48.53 -90.00
REMARK 500 2 SER A 125 -177.61 57.83
REMARK 500 2 GLU A 126 -93.69 55.66
REMARK 500 2 HIS A 133 -178.65 59.61
REMARK 500 2 HIS A 134 85.66 55.40
REMARK 500 3 PRO A 14 91.33 -49.03
REMARK 500 3 THR A 28 -116.09 -72.53
REMARK 500 3 PHE A 29 -54.90 -177.52
REMARK 500
REMARK 500 THIS ENTRY HAS 255 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4969 RELATED DB: BMRB
REMARK 900 NMR DATA
DBREF 1IEH A 1 135 PDB 1IEH 1IEH 1 135
SEQRES 1 A 135 ASP VAL GLN LEU GLN ALA SER GLY GLY GLY LEU VAL GLN
SEQRES 2 A 135 PRO GLY GLY SER LEU ARG VAL SER CYS ALA ALA SER GLY
SEQRES 3 A 135 PHE THR PHE SER SER TYR HIS MET ALA TRP VAL ARG GLN
SEQRES 4 A 135 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER THR ILE ASN
SEQRES 5 A 135 PRO GLY ASP GLY SER THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 A 135 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR
SEQRES 7 A 135 LEU TYR LEU GLN MET ASN SER LEU LYS SER GLU ASP THR
SEQRES 8 A 135 ALA VAL TYR TYR CYS ALA LYS TYR SER GLY GLY ALA LEU
SEQRES 9 A 135 ASP ALA TRP GLY GLN GLY THR GLN VAL THR VAL SER SER
SEQRES 10 A 135 GLN SER GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN
SEQRES 11 A 135 HIS HIS HIS HIS HIS
SHEET 1 A 4 GLN A 3 SER A 7 0
SHEET 2 A 4 SER A 17 SER A 25 -1 O SER A 21 N SER A 7
SHEET 3 A 4 LEU A 79 ASN A 84 -1 O MET A 83 N LEU A 18
SHEET 4 A 4 PHE A 68 ARG A 72 -1 N SER A 71 O TYR A 80
SHEET 1 B 6 LEU A 11 VAL A 12 0
SHEET 2 B 6 THR A 111 VAL A 115 1 O THR A 114 N VAL A 12
SHEET 3 B 6 ALA A 92 LYS A 98 -1 N ALA A 92 O VAL A 113
SHEET 4 B 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95
SHEET 5 B 6 GLU A 46 ILE A 51 -1 O SER A 49 N TRP A 36
SHEET 6 B 6 THR A 58 TYR A 60 -1 O TYR A 59 N THR A 50
SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03
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