Header list of 7hsc.pdb file
Complete list - 16 20 Bytes
HEADER MOLECULAR CHAPERONE 03-MAY-99 7HSC TITLE HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD TITLE 2 SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (HEAT SHOCK COGNATE 70 KD PROTEIN 1); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SUBSTRATE BINDING DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 STRAIN: JM109(DE3); SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109(DE3) KEYWDS MOLECULAR CHAPERONE, HSP70, PEPTIDE BINDING, PROTEIN FOLDING EXPDTA SOLUTION NMR AUTHOR R.C.MORSHAUSER,W.HU,H.WANG,Y.PANG,G.C.FLYNN,E.R.P.ZUIDERWEG REVDAT 5 16-MAR-22 7HSC 1 REMARK REVDAT 4 24-FEB-09 7HSC 1 VERSN REVDAT 3 01-APR-03 7HSC 1 JRNL REVDAT 2 25-JUN-99 7HSC 1 JRNL REVDAT 1 10-MAY-99 7HSC 0 JRNL AUTH R.C.MORSHAUSER,W.HU,H.WANG,Y.PANG,G.C.FLYNN,E.R.ZUIDERWEG JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE 18 KDA JRNL TITL 2 SUBSTRATE-BINDING DOMAIN OF THE MAMMALIAN CHAPERONE PROTEIN JRNL TITL 3 HSC70. JRNL REF J.MOL.BIOL. V. 289 1387 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10373374 JRNL DOI 10.1006/JMBI.1999.2776 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE WAS EXTENSIVELY MINIMIZED. REMARK 3 THE PROTOCOL CAN BE FOUND IN THE JMB PAPER (IN PRESS, 1999) REMARK 4 REMARK 4 7HSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-99. REMARK 100 THE DEPOSITION ID IS D_1000000993. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.5 MM 15N OR 15N,13C LABELED REMARK 210 PROTEIN 5%D20/95%H2O AND 100%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CA)HA; HN(CO)CA; REMARK 210 HA(CACO)NH; CP H(C)CCH-TOCSY; CP REMARK 210 (H)CCH-TOCSY; CP(H)C(CCACO)NH- REMARK 210 TOCSY; 15N-RESOLVED NOESY-HSQC; REMARK 210 13CRESOLVED NOESY-HMQC; 4D 13C; REMARK 210 13C RESOLVED HMQC-NOESY3D 13C; REMARK 210 13N RESOLVED HMQC-NOESY-HSQC3D REMARK 210 13C; 13C RESOLVED HMQC-NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AMX 500; AMX 600; DMX 750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX, MSI INSIGHT INSIGHT, MSI REMARK 210 DISCOVER DISCOVER REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATE REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE OF LOWEST TOTAL ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: ENERGY MINIMIZED AVERAGE. ASSIGNMENTS OBTAINED WITH TRIPLE REMARK 210 RESONANCE NMR SPECTROSCOPY; STEREO-SPECIFIC ASSIGNMENTS WITH 10% REMARK 210 13C LABELED GLUCOSE; STRUCTURE WITH 2 HIGH RESOLUTION 4-D AND 6 REMARK 210 3D HETERONUCLEAR-RESOLVED NOESY EXPERIMENTS. SCALAR COUPLINGS REMARK 210 WITH HNHA; DYNAMICS WITH T1 AND T2 (NITROGEN) 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 HG1 THR A 502 OD2 ASP A 504 1.35 REMARK 500 HG SER A 538 OXT GLU A 540 1.36 REMARK 500 HG SER A 487 OE1 GLU A 496 1.39 REMARK 500 HG SER A 534 O GLU A 540 1.42 REMARK 500 HG1 THR A 425 OE1 GLU A 473 1.48 REMARK 500 HG1 THR A 420 OE1 GLN A 422 1.49 REMARK 500 HG1 THR A 427 O GLY A 468 1.51 REMARK 500 OD2 ASP A 531 HZ2 LYS A 532 1.52 REMARK 500 HG1 THR A 428 O PRO A 470 1.54 REMARK 500 OE2 GLU A 473 HZ3 LYS A 491 1.55 REMARK 500 OD1 ASN A 485 HG1 THR A 500 1.55 REMARK 500 HZ3 LYS A 449 OE2 GLU A 518 1.58 REMARK 500 O MET A 447 HG1 THR A 448 1.59 REMARK 500 HZ1 LYS A 521 OE1 GLU A 525 1.60 REMARK 500 REMARK 500 REMARK: NULL 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 MET A 408 CA - CB - CG ANGL. DEV. = 17.3 DEGREES REMARK 500 ARG A 414 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG A 445 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ALA A 446 CA - C - N ANGL. DEV. = -17.9 DEGREES REMARK 500 MET A 447 C - N - CA ANGL. DEV. = 17.4 DEGREES REMARK 500 MET A 447 CB - CA - C ANGL. DEV. = 12.9 DEGREES REMARK 500 MET A 447 N - CA - CB ANGL. DEV. = -20.0 DEGREES REMARK 500 MET A 447 CG - SD - CE ANGL. DEV. = 10.7 DEGREES REMARK 500 MET A 447 N - CA - C ANGL. DEV. = 20.0 DEGREES REMARK 500 MET A 447 CA - C - N ANGL. DEV. = -15.4 DEGREES REMARK 500 THR A 448 C - N - CA ANGL. DEV. = 15.6 DEGREES REMARK 500 ASN A 451 CB - CA - C ANGL. DEV. = 13.6 DEGREES REMARK 500 ARG A 467 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES REMARK 500 THR A 493 CA - CB - CG2 ANGL. DEV. = 9.7 DEGREES REMARK 500 ARG A 506A NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG A 514 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 LYS A 528 CB - CA - C ANGL. DEV. = 12.8 DEGREES REMARK 500 GLN A 529 CB - CA - C ANGL. DEV. = 12.6 DEGREES REMARK 500 GLN A 529 N - CA - CB ANGL. DEV. = -13.9 DEGREES REMARK 500 ARG A 530 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 VAL A 533 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES 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 GLN A 387 36.42 -157.16 REMARK 500 THR A 403 -137.74 -120.20 REMARK 500 THR A 427 -157.24 -109.42 REMARK 500 ASN A 432 102.88 70.11 REMARK 500 GLN A 433 76.34 63.01 REMARK 500 PRO A 434 -121.55 -71.64 REMARK 500 GLU A 444 116.62 122.89 REMARK 500 ALA A 446 91.19 -36.85 REMARK 500 MET A 447 148.20 -21.27 REMARK 500 THR A 448 57.79 89.04 REMARK 500 LYS A 449 -85.60 -83.61 REMARK 500 ASP A 450 84.47 148.37 REMARK 500 ASN A 451 -153.10 -99.45 REMARK 500 LYS A 456 138.88 59.94 REMARK 500 ARG A 467 123.29 68.32 REMARK 500 ASN A 481 39.50 -94.44 REMARK 500 ARG A 506A 53.22 39.75 REMARK 500 SER A 508 -142.23 41.26 REMARK 500 ALA A 519 -103.62 -84.63 REMARK 500 LYS A 523 -59.82 -123.63 REMARK 500 GLU A 527 67.21 99.82 REMARK 500 GLN A 529 -80.45 -9.20 REMARK 500 VAL A 533 -106.82 -116.69 REMARK 500 SER A 534 -74.95 -84.18 REMARK 500 LYS A 536 -100.44 68.16 REMARK 500 LEU A 539 33.48 -89.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 PHE A 476 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 7HSC A 383 540 UNP P63018 HSP7C_RAT 385 543 SEQRES 1 A 159 SER GLU ASN VAL GLN ASP LEU LEU LEU LEU ASP VAL THR SEQRES 2 A 159 PRO LEU SER LEU GLY ILE GLU THR ALA GLY GLY VAL MET SEQRES 3 A 159 THR VAL LEU ILE LYS ARG ASN THR THR ILE PRO THR LYS SEQRES 4 A 159 GLN THR GLN THR PHE THR THR TYR SER ASP ASN GLN PRO SEQRES 5 A 159 GLY VAL LEU ILE GLN VAL TYR GLU GLY GLU ARG ALA MET SEQRES 6 A 159 THR LYS ASP ASN ASN LEU LEU GLY LYS PHE GLU LEU THR SEQRES 7 A 159 GLY ILE PRO PRO ALA PRO ARG GLY VAL PRO GLN ILE GLU SEQRES 8 A 159 VAL THR PHE ASP ILE ASP ALA ASN GLY ILE LEU ASN VAL SEQRES 9 A 159 SER ALA VAL ASP LYS SER THR GLY LYS GLU ASN LYS ILE SEQRES 10 A 159 THR ILE THR ASN ASP LYS GLY ARG LEU SER LYS GLU ASP SEQRES 11 A 159 ILE GLU ARG MET VAL GLN GLU ALA GLU LYS TYR LYS ALA SEQRES 12 A 159 GLU ASP GLU LYS GLN ARG ASP LYS VAL SER SER LYS ASN SEQRES 13 A 159 SER LEU GLU HELIX 1 1 SER A 508 MET A 515 1 8 HELIX 2 2 GLU A 520 ALA A 524 1 5 SHEET 1 A 2 LEU A 399 GLU A 402 0 SHEET 2 A 2 GLN A 439 GLU A 442 -1 N TYR A 441 O GLY A 400 SHEET 1 B 4 THR A 420 THR A 427 0 SHEET 2 B 4 GLN A 471 ASP A 479 -1 N ILE A 478 O THR A 420 SHEET 3 B 4 ILE A 483 ASP A 490 -1 N VAL A 489 O GLU A 473 SHEET 4 B 4 LYS A 495 ILE A 501 -1 N ILE A 501 O LEU A 484 SHEET 1 C 2 VAL A 436 ILE A 438 0 SHEET 2 C 2 PHE A 457 LEU A 459 -1 N LEU A 459 O VAL A 436 CISPEP 1 ILE A 418 PRO A 419 0 -2.85 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
Complete list - 16 20 Bytes