Header list of 1q68.pdb file
Complete list - 27 20 Bytes
HEADER MEMBRANE PROTEIN/TRANSFERASE 12-AUG-03 1Q68
TITLE SOLUTION STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4 AND PROTO-
TITLE 2 ONCOGENE TYROSINE-PROTEIN KINASE LCK FRAGMENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 421-458;
COMPND 5 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 6-34;
COMPND 12 SYNONYM: P56-LCK, LSK, T CELL-SPECIFIC PROTEIN-TYROSINE KINASE;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMM;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: LCK;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PMM
KEYWDS PEPTIDE-PEPTIDE COMPLEX, HELIX-HELIX INTERACTION, ZINC COORDINATION,
KEYWDS 2 BETA HAIRPIN, MEMBRANE PROTEIN-TRANSFERASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.W.KIM,Z.Y.SUN,S.C.BLACKLOW,G.WAGNER,M.J.ECK
REVDAT 3 27-OCT-21 1Q68 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1Q68 1 VERSN
REVDAT 1 25-NOV-03 1Q68 0
JRNL AUTH P.W.KIM,Z.Y.SUN,S.C.BLACKLOW,G.WAGNER,M.J.ECK
JRNL TITL A ZINC CLASP STRUCTURE TETHERS LCK TO T CELL CORECEPTORS CD4
JRNL TITL 2 AND CD8.
JRNL REF SCIENCE V. 301 1725 2003
JRNL REFN ISSN 0036-8075
JRNL PMID 14500983
JRNL DOI 10.1126/SCIENCE.1085643
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX, X-PLOR
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC. (FELIX), BRUNGER (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 419 DISTANCE RESTRAINTS (406 NOES, FOUR ZN-S RESTRAINTS FROM CD-
REMARK 3 H HMQC EXPERIMENTS, NINE HYDROGEN BONDS) AND 63 ANGLE RESTRAINTS
REMARK 3 (57 DIHEDRAL ANGLE RESTRAINTS, SIX S-ZN-S ANGLE RESTRAINTS FROM
REMARK 3 CD-H HMQC EXPERIMENTS).
REMARK 4
REMARK 4 1Q68 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019967.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM CD4-LCK-ZN2+, U-15N,13C;
REMARK 210 20 MM ACETATE, 20 MM NACL, 0.15%
REMARK 210 BETA-MERCAPTOETHANOL; 0.5 MM CD4-
REMARK 210 LCK-ZN2+, U-15N; 20 MM ACETATE,
REMARK 210 20 MM NACL, 0.15% BETA-
REMARK 210 MERCAPTOETHANOL; 0.5 MM CD4-LCK-
REMARK 210 ZN2+; 20 MM ACETATE, 20 MM NACL,
REMARK 210 0.15% BETA-MERCAPTOETHANOL; 1.0
REMARK 210 MM CD4-LCK-CD2+; 20 MM ACETATE,
REMARK 210 20 MM NACL, 0.15% BETA-
REMARK 210 MERCAPTOETHANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HN(CO)CA, HNCACB,
REMARK 210 HN(CO)CACB, CCONH, HCCONH, HCCH
REMARK 210 TOCSY; 15N-NOESY, 15N-TOCSY; D2O
REMARK 210 NOESY, D2O TOCSY; CD-H HMQC, CD-
REMARK 210 H NOESY-HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 10 STRUCTURES WITH THE
REMARK 210 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: 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 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 ARG A 406 H ILE A 410 1.51
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 CYS A 420 93.58 -32.38
REMARK 500 1 CYS A 422 157.31 -44.73
REMARK 500 1 PRO A 423 -166.04 -55.85
REMARK 500 1 PHE A 426 98.17 52.75
REMARK 500 1 THR A 429 178.91 54.48
REMARK 500 1 CYS A 430 177.04 59.52
REMARK 500 1 SER A 431 85.79 59.06
REMARK 500 1 ASN B 22 -57.12 -134.37
REMARK 500 2 ARG A 398 57.33 -147.67
REMARK 500 2 HIS A 399 -65.61 -122.89
REMARK 500 2 CYS A 420 94.35 -26.59
REMARK 500 2 CYS A 422 151.96 -44.27
REMARK 500 2 PRO A 423 171.66 -56.70
REMARK 500 2 LYS A 428 112.76 60.63
REMARK 500 2 SER A 431 135.64 63.44
REMARK 500 2 HIS B 8 73.06 57.40
REMARK 500 2 ASN B 22 -54.60 -134.09
REMARK 500 2 LEU B 30 152.60 -49.64
REMARK 500 2 ASP B 31 48.50 -150.17
REMARK 500 3 ARG A 398 -60.98 -99.93
REMARK 500 3 ARG A 400 -175.33 -66.97
REMARK 500 3 ARG A 401 76.49 -176.23
REMARK 500 3 ARG A 402 -54.90 -154.18
REMARK 500 3 GLN A 403 57.07 -91.23
REMARK 500 3 LYS A 418 65.25 -101.53
REMARK 500 3 CYS A 420 92.87 -31.89
REMARK 500 3 CYS A 422 150.03 -39.84
REMARK 500 3 GLN A 427 -78.80 -65.90
REMARK 500 3 SER A 431 150.69 62.38
REMARK 500 3 ASN B 22 -55.70 -133.75
REMARK 500 3 LEU B 30 130.25 176.37
REMARK 500 3 ASP B 31 -175.36 -170.35
REMARK 500 4 CYS A 397 78.10 -174.05
REMARK 500 4 ARG A 398 71.47 -152.53
REMARK 500 4 ARG A 401 -59.25 -160.09
REMARK 500 4 ALA A 404 28.69 -144.35
REMARK 500 4 LYS A 418 64.90 -104.44
REMARK 500 4 CYS A 420 93.94 -27.99
REMARK 500 4 CYS A 422 161.05 -43.77
REMARK 500 4 PRO A 423 57.17 -68.91
REMARK 500 4 LYS A 428 -170.31 -56.17
REMARK 500 4 THR A 429 119.18 171.97
REMARK 500 4 LEU B 30 174.69 -51.09
REMARK 500 4 ASP B 31 88.10 -167.92
REMARK 500 5 ARG A 398 -58.74 -135.29
REMARK 500 5 ARG A 402 74.65 55.44
REMARK 500 5 LYS A 418 62.61 -103.89
REMARK 500 5 CYS A 420 93.10 -33.04
REMARK 500 5 CYS A 422 149.59 -39.95
REMARK 500 5 ARG A 425 -179.76 -172.26
REMARK 500
REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 420 SG
REMARK 620 2 CYS A 422 SG 111.2
REMARK 620 3 CYS B 20 SG 110.0 108.1
REMARK 620 4 CYS B 23 SG 107.7 109.4 110.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
DBREF 1Q68 A 396 433 UNP P01730 CD4_HUMAN 421 458
DBREF 1Q68 B 7 35 UNP P06239 LCK_HUMAN 6 34
SEQADV 1Q68 LEU A 407 UNP P01730 MET 432 ENGINEERED MUTATION
SEQADV 1Q68 LEU B 14 UNP P06239 MET 13 ENGINEERED MUTATION
SEQRES 1 A 38 ARG CYS ARG HIS ARG ARG ARG GLN ALA GLU ARG LEU SER
SEQRES 2 A 38 GLN ILE LYS ARG LEU LEU SER GLU LYS LYS THR CYS GLN
SEQRES 3 A 38 CYS PRO HIS ARG PHE GLN LYS THR CYS SER PRO ILE
SEQRES 1 B 29 SER HIS PRO GLU ASP ASP TRP LEU GLU ASN ILE ASP VAL
SEQRES 2 B 29 CYS GLU ASN CYS HIS TYR PRO ILE VAL PRO LEU ASP GLY
SEQRES 3 B 29 LYS GLY THR
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 3 ZN ZN 2+
HELIX 1 1 GLU A 405 GLU A 416 1 12
HELIX 2 2 ASP B 11 ASN B 16 1 6
LINK ZN ZN A 201 SG CYS A 420 1555 1555 2.35
LINK ZN ZN A 201 SG CYS A 422 1555 1555 2.35
LINK ZN ZN A 201 SG CYS B 20 1555 1555 2.35
LINK ZN ZN A 201 SG CYS B 23 1555 1555 2.35
SITE 1 AC1 4 CYS A 420 CYS A 422 CYS B 20 CYS B 23
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 - 27 20 Bytes