Header list of 1kbf.pdb file
Complete list - b 26 2 Bytes
HEADER SIGNALING PROTEIN 06-NOV-01 1KBF
TITLE SOLUTION STRUCTURE OF THE CYSTEINE-RICH C1 DOMAIN OF KINASE SUPPRESSOR
TITLE 2 OF RAS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINASE SUPPRESSOR OF RAS 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYSTEINE-RICH C1 DOMAIN;
COMPND 5 SYNONYM: MKSR1,PROTEIN HB,KSR;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: KSR1, KSR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-3X
KEYWDS CYSTEINE-RICH DOMAIN, ZINC-BINDING PROTEIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.ZHOU,D.A.HORITA,D.S.WAUGH,R.A.BYRD,D.K.MORRISON
REVDAT 4 26-FEB-20 1KBF 1 COMPND SOURCE KEYWDS REMARK
REVDAT 4 2 1 SEQADV SHEET LINK ATOM
REVDAT 3 25-DEC-19 1KBF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1KBF 1 VERSN
REVDAT 1 23-JAN-02 1KBF 0
JRNL AUTH M.ZHOU,D.A.HORITA,D.S.WAUGH,R.A.BYRD,D.K.MORRISON
JRNL TITL SOLUTION STRUCTURE AND FUNCTIONAL ANALYSIS OF THE
JRNL TITL 2 CYSTEINE-RICH C1 DOMAIN OF KINASE SUPPRESSOR OF RAS (KSR).
JRNL REF J.MOL.BIOL. V. 315 435 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11786023
JRNL DOI 10.1006/JMBI.2001.5263
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : STEIN ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KBF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014776.
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 : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-100% 13C; U-100% 15N]
REMARK 210 KINASE SUPPRESSOR OF RAS, 30 MM
REMARK 210 TRIS-ACETATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 100 MM NA2SO4, 0.1 MM
REMARK 210 SODIUM CITRATE, 0.1 MM TCEP, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; HNCACB; CBCA(CO)NH;
REMARK 210 C(CO)NH; HCCHTOCSY; 3D HNHB;
REMARK 210 HN(CO)HB; 3D 15N-EDITED NOESY-
REMARK 210 HSQC; 13C AND 15N-EDITED NOESY-
REMARK 210 HSQC; 3D 13C-EDITED NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 340 78.35 -158.29
REMARK 500 1 TRP A 341 -82.79 -57.40
REMARK 500 1 LEU A 342 -54.02 179.65
REMARK 500 1 VAL A 348 -69.70 -130.97
REMARK 500 1 GLN A 350 97.32 44.70
REMARK 500 1 SER A 352 97.32 -64.56
REMARK 500 1 MET A 353 178.55 177.84
REMARK 500 1 HIS A 361 -33.00 65.71
REMARK 500 1 ARG A 363 87.13 76.81
REMARK 500 1 HIS A 367 174.38 -44.94
REMARK 500 1 LYS A 369 -73.54 -151.92
REMARK 500 1 PRO A 375 -168.33 -75.93
REMARK 500 1 CYS A 377 103.58 -59.98
REMARK 500 2 SER A 331 32.98 -98.60
REMARK 500 2 GLN A 344 -161.98 -61.16
REMARK 500 2 CYS A 346 114.14 -39.75
REMARK 500 2 VAL A 348 -80.67 -86.31
REMARK 500 2 GLN A 350 93.48 44.15
REMARK 500 2 SER A 352 96.04 -63.92
REMARK 500 2 MET A 353 -177.42 -178.99
REMARK 500 2 LYS A 360 -168.81 -78.45
REMARK 500 2 HIS A 361 -33.54 67.47
REMARK 500 2 ARG A 363 72.98 78.22
REMARK 500 2 HIS A 367 170.05 -45.89
REMARK 500 2 LYS A 369 -68.33 -133.05
REMARK 500 2 CYS A 370 31.56 37.49
REMARK 500 2 GLU A 373 -60.75 -95.67
REMARK 500 3 SER A 331 -169.40 59.01
REMARK 500 3 SER A 340 -149.54 -118.67
REMARK 500 3 TRP A 341 -69.22 68.42
REMARK 500 3 LEU A 342 -84.46 -129.58
REMARK 500 3 SER A 343 26.35 46.18
REMARK 500 3 GLN A 344 -177.80 50.48
REMARK 500 3 CYS A 346 139.67 -37.61
REMARK 500 3 VAL A 348 -68.35 -131.91
REMARK 500 3 GLN A 350 83.13 63.48
REMARK 500 3 LYS A 351 -159.56 -140.46
REMARK 500 3 MET A 353 -178.59 -176.30
REMARK 500 3 HIS A 361 -34.87 68.19
REMARK 500 3 ARG A 363 93.58 76.78
REMARK 500 3 HIS A 367 175.55 -48.14
REMARK 500 3 LYS A 369 70.65 -178.73
REMARK 500 3 PRO A 375 -168.14 -77.38
REMARK 500 3 CYS A 377 -167.92 -57.77
REMARK 500 4 SER A 331 157.92 60.58
REMARK 500 4 VAL A 332 84.05 -68.89
REMARK 500 4 TRP A 341 -157.20 -61.25
REMARK 500 4 LEU A 342 43.61 -88.11
REMARK 500 4 SER A 343 -80.62 -66.84
REMARK 500 4 GLN A 344 -174.56 171.14
REMARK 500
REMARK 500 THIS ENTRY HAS 268 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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 334 ND1
REMARK 620 2 CYS A 359 SG 157.5
REMARK 620 3 LYS A 360 O 101.5 89.0
REMARK 620 4 CYS A 362 SG 94.1 105.4 92.3
REMARK 620 5 CYS A 377 SG 103.0 64.5 153.5 95.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 346 SG
REMARK 620 2 CYS A 349 SG 110.3
REMARK 620 3 HIS A 367 ND1 72.2 92.3
REMARK 620 4 CYS A 370 SG 130.2 119.1 99.7
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KBE RELATED DB: PDB
REMARK 900 1KBE IS THE STRUCTURE WITH THE LOWEST ENERGY
REMARK 900 RELATED ID: 5203 RELATED DB: BMRB
REMARK 900 SOLUTION STRUCTURE OF THE CYSTEINE-RICH C1 DOMAIN OF KINASE
REMARK 900 SUPPRESSOR OF RAS
DBREF 1KBF A 331 378 UNP Q61097 KSR1_MOUSE 331 378
SEQADV 1KBF GLY A 330 UNP Q61097 EXPRESSION TAG
SEQRES 1 A 49 GLY SER VAL THR HIS ARG PHE SER THR LYS SER TRP LEU
SEQRES 2 A 49 SER GLN VAL CYS ASN VAL CYS GLN LYS SER MET ILE PHE
SEQRES 3 A 49 GLY VAL LYS CYS LYS HIS CYS ARG LEU LYS CYS HIS ASN
SEQRES 4 A 49 LYS CYS THR LYS GLU ALA PRO ALA CYS ARG
HET ZN A 1 1
HET ZN A 2 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
SHEET 1 AA1 3 PHE A 336 LYS A 339 0
SHEET 2 AA1 3 GLY A 356 CYS A 359 -1 O GLY A 356 N LYS A 339
SHEET 3 AA1 3 LEU A 364 CYS A 366 -1 O LEU A 364 N CYS A 359
SSBOND 1 CYS A 359 CYS A 377 1555 1555 2.47
LINK ND1 HIS A 334 ZN ZN A 1 1555 1555 2.03
LINK SG CYS A 346 ZN ZN A 2 1555 1555 2.32
LINK SG CYS A 349 ZN ZN A 2 1555 1555 2.30
LINK SG CYS A 359 ZN ZN A 1 1555 1555 2.32
LINK O LYS A 360 ZN ZN A 1 1555 1555 2.41
LINK SG CYS A 362 ZN ZN A 1 1555 1555 2.34
LINK ND1 HIS A 367 ZN ZN A 2 1555 1555 2.00
LINK SG CYS A 370 ZN ZN A 2 1555 1555 2.34
LINK SG CYS A 377 ZN ZN A 1 1555 1555 2.30
SITE 1 AC1 5 HIS A 334 CYS A 359 LYS A 360 CYS A 362
SITE 2 AC1 5 CYS A 377
SITE 1 AC2 4 CYS A 346 CYS A 349 HIS A 367 CYS A 370
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 26 2 Bytes