Header list of 1ckr.pdb file
Complete list - b 16 2 Bytes
HEADER CHAPERONE 22-APR-99 1CKR
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: HEAT SHOCK SUBSTRATE BINDING DOMAIN OF HSC-70;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109(DE3)
KEYWDS MOLECULAR CHAPERONE, HSP70, PEPTIDE BINDING, PROTEIN FOLDING,
KEYWDS 2 CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.C.MORSHAUSER,W.HU,H.WANG,Y.PANG,G.C.FLYNN,E.R.P.ZUIDERWEG
REVDAT 6 16-FEB-22 1CKR 1 REMARK
REVDAT 5 24-FEB-09 1CKR 1 VERSN
REVDAT 4 01-APR-03 1CKR 1 JRNL
REVDAT 3 25-NOV-99 1CKR 3 ATOM HEADER
REVDAT 2 25-JUN-99 1CKR 1 JRNL
REVDAT 1 30-APR-99 1CKR 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 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1CKR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000924.
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; DMX
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 : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: ASSIGNMENTS OBTAINED WITH TRIPLE RESONANCE NMR
REMARK 210 SPECTROSCOPY; STEREO-SPECIFIC ASSIGNMENTS WITH 10% 13C LABELED
REMARK 210 GLUCOSE; STRUCTURE WITH 2 HIGH RESOLUTION 4-D AND 6 3D
REMARK 210 HETERONUCLEAR-RESOLVED NOESY EXPERIMENTS. SCALAR COUPLINGS WITH
REMARK 210 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 HG SER A 487 OE1 GLU A 496 1.40
REMARK 500 HG SER A 534 O GLU A 540 1.43
REMARK 500 HG1 THR A 409 OD1 ASP A 531 1.49
REMARK 500 HZ3 LYS A 509 OE2 GLU A 510 1.49
REMARK 500 HG1 THR A 427 O GLY A 468 1.53
REMARK 500 HG1 THR A 428 O PRO A 470 1.55
REMARK 500 O THR A 428 HG SER A 535 1.56
REMARK 500 HZ2 LYS A 449 OE2 GLU A 518 1.57
REMARK 500 H1 SER A 383 OE1 GLU A 384 1.58
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 1 ARG A 414 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 GLU A 444 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 1 ARG A 445 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 445 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 1 MET A 447 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 1 MET A 447 N - CA - C ANGL. DEV. = 21.5 DEGREES
REMARK 500 1 ARG A 467 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 THR A 493 CA - CB - CG2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 ARG A 506A NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 ARG A 514 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ALA A 524 CB - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500 1 ALA A 524 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 1 LYS A 528 CB - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 1 ARG A 530 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 SER A 398 N - CA - CB ANGL. DEV. = -9.5 DEGREES
REMARK 500 2 VAL A 410 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 ARG A 414 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 TYR A 441 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 2 GLU A 444 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 2 ARG A 445 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 2 MET A 447 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 2 MET A 447 N - CA - C ANGL. DEV. = 25.5 DEGREES
REMARK 500 2 ARG A 467 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 2 THR A 493 CA - CB - CG2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 2 ARG A 506A NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 514 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 514 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 MET A 515 CA - CB - CG ANGL. DEV. = 10.5 DEGREES
REMARK 500 2 ALA A 524 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 2 ALA A 524 N - CA - CB ANGL. DEV. = -10.0 DEGREES
REMARK 500 2 LYS A 528 CB - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500 2 GLN A 529 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 2 ARG A 530 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ARG A 414 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 445 C - N - CA ANGL. DEV. = 15.3 DEGREES
REMARK 500 3 ARG A 445 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 3 MET A 447 N - CA - CB ANGL. DEV. = -17.0 DEGREES
REMARK 500 3 MET A 447 N - CA - C ANGL. DEV. = 32.1 DEGREES
REMARK 500 3 ARG A 467 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 506A NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 514 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 ALA A 519 N - CA - CB ANGL. DEV. = -10.8 DEGREES
REMARK 500 3 LYS A 523 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 3 LYS A 528 CB - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 3 GLN A 529 CB - CA - C ANGL. DEV. = 13.8 DEGREES
REMARK 500 3 GLN A 529 N - CA - CB ANGL. DEV. = -14.4 DEGREES
REMARK 500 3 ARG A 530 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 MET A 408 CA - CB - CG ANGL. DEV. = 19.4 DEGREES
REMARK 500 4 ARG A 414 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 4 TYR A 429 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 337 ANGLE DEVIATIONS.
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 LEU A 389 45.84 -81.29
REMARK 500 1 ALA A 404 -105.62 58.63
REMARK 500 1 THR A 427 -159.04 -116.62
REMARK 500 1 ASN A 432 94.92 46.84
REMARK 500 1 GLN A 433 96.24 66.88
REMARK 500 1 GLU A 444 -177.76 -41.41
REMARK 500 1 LYS A 449 -100.58 -76.38
REMARK 500 1 ASP A 450 37.54 -165.87
REMARK 500 1 ASN A 451 -129.32 -101.82
REMARK 500 1 ARG A 467 114.07 -30.55
REMARK 500 1 ASN A 481 38.40 -91.22
REMARK 500 1 ARG A 506A 66.99 -119.88
REMARK 500 1 SER A 508 -143.43 39.34
REMARK 500 1 GLN A 517 67.85 -111.53
REMARK 500 1 GLU A 518 -70.55 159.39
REMARK 500 1 ALA A 519 -71.40 -48.41
REMARK 500 1 LYS A 521 -71.04 -50.66
REMARK 500 1 TYR A 522 -4.19 -58.56
REMARK 500 1 LYS A 523 -65.15 -90.43
REMARK 500 1 GLU A 527 62.75 92.91
REMARK 500 1 GLN A 529 -82.16 -14.71
REMARK 500 1 VAL A 533 -129.16 -142.92
REMARK 500 1 SER A 535 -73.93 -113.59
REMARK 500 1 LYS A 536 -95.62 -143.96
REMARK 500 1 ASN A 537 53.69 -100.02
REMARK 500 2 ASN A 385 -77.51 68.92
REMARK 500 2 ALA A 404 -89.36 55.82
REMARK 500 2 THR A 417 90.65 -69.74
REMARK 500 2 THR A 427 -149.32 -110.51
REMARK 500 2 ASN A 432 90.21 68.80
REMARK 500 2 GLN A 433 101.21 62.11
REMARK 500 2 PRO A 434 -61.71 -92.04
REMARK 500 2 GLU A 444 164.97 -2.76
REMARK 500 2 ARG A 445 -143.72 -68.38
REMARK 500 2 LYS A 449 -99.85 -81.58
REMARK 500 2 ASP A 450 29.84 -146.84
REMARK 500 2 ARG A 467 121.73 -35.09
REMARK 500 2 ASN A 481 41.14 -95.01
REMARK 500 2 ARG A 506A 67.23 -114.65
REMARK 500 2 SER A 508 -131.33 30.09
REMARK 500 2 VAL A 516 35.60 -84.56
REMARK 500 2 ALA A 519 -86.75 -58.57
REMARK 500 2 LYS A 521 -74.06 -55.80
REMARK 500 2 GLU A 527 62.41 95.28
REMARK 500 2 GLN A 529 -83.86 -19.37
REMARK 500 2 SER A 534 -121.02 59.20
REMARK 500 2 LYS A 536 -80.39 68.79
REMARK 500 3 THR A 403 -130.43 -105.45
REMARK 500 3 THR A 417 93.40 -69.18
REMARK 500 3 THR A 427 -157.20 -109.66
REMARK 500
REMARK 500 THIS ENTRY HAS 476 RAMACHANDRAN OUTLIERS.
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 1 TYR A 441 0.08 SIDE CHAIN
REMARK 500 2 TYR A 441 0.13 SIDE CHAIN
REMARK 500 2 ARG A 506A 0.13 SIDE CHAIN
REMARK 500 3 TYR A 441 0.17 SIDE CHAIN
REMARK 500 4 ARG A 445 0.09 SIDE CHAIN
REMARK 500 4 ARG A 506A 0.14 SIDE CHAIN
REMARK 500 5 PHE A 476 0.08 SIDE CHAIN
REMARK 500 6 ARG A 445 0.09 SIDE CHAIN
REMARK 500 6 PHE A 476 0.09 SIDE CHAIN
REMARK 500 6 ARG A 506A 0.14 SIDE CHAIN
REMARK 500 7 TYR A 441 0.07 SIDE CHAIN
REMARK 500 7 PHE A 476 0.09 SIDE CHAIN
REMARK 500 8 ARG A 506A 0.14 SIDE CHAIN
REMARK 500 9 ARG A 445 0.11 SIDE CHAIN
REMARK 500 9 PHE A 476 0.08 SIDE CHAIN
REMARK 500 9 ARG A 530 0.09 SIDE CHAIN
REMARK 500 10 ARG A 530 0.09 SIDE CHAIN
REMARK 500 11 TYR A 441 0.19 SIDE CHAIN
REMARK 500 11 ARG A 445 0.11 SIDE CHAIN
REMARK 500 11 ARG A 467 0.21 SIDE CHAIN
REMARK 500 11 PHE A 476 0.08 SIDE CHAIN
REMARK 500 11 ARG A 506A 0.12 SIDE CHAIN
REMARK 500 12 TYR A 441 0.06 SIDE CHAIN
REMARK 500 12 PHE A 476 0.09 SIDE CHAIN
REMARK 500 12 ARG A 506A 0.13 SIDE CHAIN
REMARK 500 13 PHE A 476 0.10 SIDE CHAIN
REMARK 500 13 ARG A 506A 0.09 SIDE CHAIN
REMARK 500 13 TYR A 522 0.17 SIDE CHAIN
REMARK 500 14 ARG A 506A 0.10 SIDE CHAIN
REMARK 500 15 TYR A 441 0.07 SIDE CHAIN
REMARK 500 15 ARG A 445 0.08 SIDE CHAIN
REMARK 500 15 PHE A 476 0.08 SIDE CHAIN
REMARK 500 15 ARG A 514 0.08 SIDE CHAIN
REMARK 500 16 ARG A 445 0.09 SIDE CHAIN
REMARK 500 17 TYR A 441 0.09 SIDE CHAIN
REMARK 500 17 ARG A 445 0.12 SIDE CHAIN
REMARK 500 18 TYR A 441 0.13 SIDE CHAIN
REMARK 500 18 PHE A 476 0.09 SIDE CHAIN
REMARK 500 18 TYR A 522 0.16 SIDE CHAIN
REMARK 500 19 ARG A 445 0.08 SIDE CHAIN
REMARK 500 20 TYR A 441 0.12 SIDE CHAIN
REMARK 500 20 PHE A 476 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 4 ASP A 450 -10.65
REMARK 500 7 LYS A 528 -10.11
REMARK 500 19 MET A 447 11.63
REMARK 500 20 MET A 447 10.77
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CKR A 383 540 UNP P63018 HSP7C_RAT 385 542
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 ALA A 519 ALA A 524 1 6
SHEET 1 A 4 VAL A 407 THR A 409 0
SHEET 2 A 4 LEU A 399 THR A 403 -1 N THR A 403 O VAL A 407
SHEET 3 A 4 VAL A 436 GLU A 442 -1 N TYR A 441 O GLY A 400
SHEET 4 A 4 LYS A 456 LEU A 459 -1 N LEU A 459 O VAL A 436
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
CISPEP 1 ILE A 418 PRO A 419 1 -3.24
CISPEP 2 ILE A 418 PRO A 419 2 -3.79
CISPEP 3 ILE A 418 PRO A 419 3 -3.43
CISPEP 4 ILE A 418 PRO A 419 4 -3.03
CISPEP 5 ILE A 418 PRO A 419 5 -4.24
CISPEP 6 ILE A 418 PRO A 419 6 -3.26
CISPEP 7 ILE A 418 PRO A 419 7 -3.88
CISPEP 8 ILE A 418 PRO A 419 8 -3.82
CISPEP 9 ILE A 418 PRO A 419 9 -3.28
CISPEP 10 ILE A 418 PRO A 419 10 -3.34
CISPEP 11 ILE A 418 PRO A 419 11 -3.27
CISPEP 12 ILE A 418 PRO A 419 12 -3.70
CISPEP 13 ILE A 418 PRO A 419 13 -2.75
CISPEP 14 ILE A 418 PRO A 419 14 -2.92
CISPEP 15 ILE A 418 PRO A 419 15 -3.96
CISPEP 16 ILE A 418 PRO A 419 16 -3.07
CISPEP 17 ILE A 418 PRO A 419 17 -3.01
CISPEP 18 ILE A 418 PRO A 419 18 -3.71
CISPEP 19 ILE A 418 PRO A 419 19 -3.59
CISPEP 20 ILE A 418 PRO A 419 20 -3.09
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 16 2 Bytes