Header list of 1xu6.pdb file
Complete list - r 25 2 Bytes
HEADER IMMUNE SYSTEM, MEMBRANE PROTEIN 25-OCT-04 1XU6
TITLE STRUCTURE OF THE C-TERMINAL DOMAIN FROM TRYPANOSOMA BRUCEI VARIANT
TITLE 2 SURFACE GLYCOPROTEIN MITAT1.2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VARIANT SURFACE GLYCOPROTEIN MITAT 1.2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VSG 221, MITAT1.2 C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA;
SOURCE 3 ORGANISM_TAXID: 5702;
SOURCE 4 STRAIN: BRUCEI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 TRXB;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CYSTEINE KNOT, IMMUNE SYSTEM, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 60
AUTHOR A.CHATTOPADHYAY,N.G.JONES,D.NIETLISPACH,P.R.NIELSEN,H.P.VOORHEIS,
AUTHOR 2 H.R.MOTT,M.CARRINGTON
REVDAT 6 13-JUL-11 1XU6 1 VERSN
REVDAT 5 24-FEB-09 1XU6 1 VERSN
REVDAT 4 17-MAY-05 1XU6 1
REVDAT 3 22-FEB-05 1XU6 1
REVDAT 2 08-FEB-05 1XU6 1 JRNL
REVDAT 1 30-NOV-04 1XU6 0
JRNL AUTH A.CHATTOPADHYAY,N.G.JONES,D.NIETLISPACH,P.R.NIELSEN,
JRNL AUTH 2 H.P.VOORHEIS,H.R.MOTT,M.CARRINGTON
JRNL TITL STRUCTURE OF THE C-TERMINAL DOMAIN FROM TRYPANOSOMA BRUCEI
JRNL TITL 2 VARIANT SURFACE GLYCOPROTEIN MITAT1.2
JRNL REF J.BIOL.CHEM. V. 280 7228 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15557330
JRNL DOI 10.1074/JBC.M410787200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.1
REMARK 3 AUTHORS : NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 719 UNAMBIGUOUS AND 121 AMBIGUOUS NON-
REMARK 3 DEGENERATE DISTANCE RESTRAINTS, 24 PAIRS OF DIHEDRAL RESTRAINTS
REMARK 3 FROM TALOS, AND 20 HYDROGEN BONDS.
REMARK 4
REMARK 4 1XU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-04.
REMARK 100 THE RCSB ID CODE IS RCSB030774.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATMOSPHERE ATM
REMARK 210 SAMPLE CONTENTS : 1MM 15N-LABELLED C-TERMINAL
REMARK 210 DOMAIN OF MITAT1.2, 50MM SODIUM
REMARK 210 PHOSPHATE, PH 6.5, 100MM SODIUM
REMARK 210 CHLORIDE, 0.05% SODIUM AZIDE, 90%
REMARK 210 H2O, 10% D2O; 1MM 15N,13C-
REMARK 210 LABELLED C- TERMINAL DOMAIN OF
REMARK 210 MITAT1.2, 50MM SODIUM PHOSPHATE,
REMARK 210 PH 6.5, 100MM SODIUM CHLORIDE,
REMARK 210 0.05% SODIUM AZIDE, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_ 13C-
REMARK 210 SEPARATED_NOESY; CLEANEX
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA 2.7, ANSIG 3.3, CNS 1.1,
REMARK 210 ARIA 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 60
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 HE2 HIS A 396 HG1 THR A 405 1.49
REMARK 500 HA CYS A 393 HA LEU A 406 1.49
REMARK 500 HB3 LEU A 358 H GLU A 359 1.52
REMARK 500 H ASP A 385 HB2 GLU A 388 1.60
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 355 44.70 -173.01
REMARK 500 1 LEU A 358 -142.13 -66.20
REMARK 500 1 GLU A 359 -42.61 -173.88
REMARK 500 1 THR A 362 42.46 -175.35
REMARK 500 1 HIS A 365 33.82 -79.68
REMARK 500 1 PRO A 367 38.70 -77.74
REMARK 500 1 ALA A 368 142.46 -177.43
REMARK 500 1 SER A 370 -134.55 -175.74
REMARK 500 1 ALA A 375 98.09 -59.62
REMARK 500 1 GLU A 376 -151.69 -71.28
REMARK 500 1 CYS A 389 97.32 -58.01
REMARK 500 1 CYS A 393 -156.24 -65.12
REMARK 500 1 LYS A 394 113.97 -161.74
REMARK 500 1 ALA A 399 37.01 -82.01
REMARK 500 1 GLU A 400 -32.45 77.14
REMARK 500 1 ASN A 401 25.21 -162.82
REMARK 500 1 LYS A 402 131.94 65.39
REMARK 500 1 ASP A 416 35.17 -83.95
REMARK 500 1 ALA A 419 -43.99 -167.36
REMARK 500 1 THR A 427 132.97 65.29
REMARK 500 1 ASN A 428 -41.11 -177.29
REMARK 500 1 THR A 430 -39.18 74.24
REMARK 500 2 MET A 357 -137.15 -69.08
REMARK 500 2 GLN A 363 -34.95 -174.60
REMARK 500 2 LYS A 364 80.53 -67.20
REMARK 500 2 PRO A 367 -151.60 -68.24
REMARK 500 2 GLN A 371 -149.23 -179.66
REMARK 500 2 ALA A 399 41.65 -83.88
REMARK 500 2 GLU A 400 -23.36 73.02
REMARK 500 2 ASN A 401 28.89 -175.10
REMARK 500 2 LYS A 402 134.02 65.73
REMARK 500 2 ALA A 419 -44.70 -146.55
REMARK 500 2 ASP A 421 134.86 -172.00
REMARK 500 2 THR A 427 -141.68 49.40
REMARK 500 2 ASN A 428 -137.39 -156.89
REMARK 500 3 THR A 362 -140.41 -74.75
REMARK 500 3 GLN A 363 -1.51 66.32
REMARK 500 3 HIS A 365 -34.85 72.81
REMARK 500 3 LYS A 366 61.24 61.13
REMARK 500 3 ALA A 368 134.24 68.50
REMARK 500 3 SER A 370 138.95 -172.32
REMARK 500 3 GLN A 371 -45.11 -168.98
REMARK 500 3 GLN A 373 -178.07 -68.37
REMARK 500 3 ASN A 401 42.48 -165.46
REMARK 500 3 LYS A 402 131.67 65.60
REMARK 500 3 ASP A 416 36.73 -78.89
REMARK 500 3 GLU A 417 40.76 -170.91
REMARK 500 3 THR A 418 42.05 -174.02
REMARK 500 3 ALA A 419 -44.07 -173.04
REMARK 500 3 THR A 424 -138.46 -72.48
REMARK 500
REMARK 500 THIS ENTRY HAS 1223 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XU6 A 359 433 UNP P26332 VSM2_TRYBB 385 459
SEQADV 1XU6 GLY A 354 UNP P26332 CLONING ARTIFACT
SEQADV 1XU6 SER A 355 UNP P26332 CLONING ARTIFACT
SEQADV 1XU6 HIS A 356 UNP P26332 CLONING ARTIFACT
SEQADV 1XU6 MET A 357 UNP P26332 CLONING ARTIFACT
SEQADV 1XU6 LEU A 358 UNP P26332 CLONING ARTIFACT
SEQRES 1 A 80 GLY SER HIS MET LEU GLU VAL LEU THR GLN LYS HIS LYS
SEQRES 2 A 80 PRO ALA GLU SER GLN GLN GLN ALA ALA GLU THR GLU GLY
SEQRES 3 A 80 SER CYS ASN LYS LYS ASP GLN ASN GLU CYS LYS SER PRO
SEQRES 4 A 80 CYS LYS TRP HIS ASN ASP ALA GLU ASN LYS LYS CYS THR
SEQRES 5 A 80 LEU ASP LYS GLU GLU ALA LYS LYS VAL ALA ASP GLU THR
SEQRES 6 A 80 ALA LYS ASP GLY LYS THR GLY ASN THR ASN THR THR GLY
SEQRES 7 A 80 SER SER
HELIX 1 1 THR A 377 LYS A 384 1 8
HELIX 2 2 ASP A 407 ASP A 416 1 10
SHEET 1 A 2 TRP A 395 HIS A 396 0
SSBOND 1 CYS A 381 CYS A 393 1555 1555 2.03
SSBOND 2 CYS A 389 CYS A 404 1555 1555 2.04
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 25 2 Bytes