Header list of 3rpb.pdb file
Complete list - r 16 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 19-APR-99 3RPB
TITLE THE C2B-DOMAIN OF RABPHILIN: STRUCTURAL VARIATIONS IN A JANUS-FACED
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RABPHILIN 3-A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2B 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: DE3
KEYWDS C2-DOMAINS, C2B-DOMAIN, RABPHILIN, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.UBACH,J.GARCIA,M.P.NITTLER,T.C.SUDHOF,J.RIZO
REVDAT 3 16-MAR-22 3RPB 1 REMARK
REVDAT 2 24-FEB-09 3RPB 1 VERSN
REVDAT 1 23-DEC-99 3RPB 0
JRNL AUTH J.UBACH,J.GARCIA,M.P.NITTLER,T.C.SUDHOF,J.RIZO
JRNL TITL STRUCTURE OF THE JANUS-FACED C2B DOMAIN OF RABPHILIN.
JRNL REF NAT.CELL BIOL. V. 1 106 1999
JRNL REFN ISSN 1465-7392
JRNL PMID 10559882
JRNL DOI 10.1038/10076
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TORSION ANGLE SIMULATED ANNEALING
REMARK 4
REMARK 4 3RPB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000884.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 304.5
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 95% WATER/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS
REMARK 210 METHOD USED : TORSION ANGLE SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST OVERALL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 O VAL A 559 H PHE A 611 1.46
REMARK 500 H LEU A 545 O ARG A 563 1.52
REMARK 500 H SER A 547 O GLY A 560 1.54
REMARK 500 H LEU A 625 O LEU A 646 1.54
REMARK 500 O LEU A 557 H TYR A 613 1.55
REMARK 500 H LEU A 548 O ILE A 669 1.56
REMARK 500 O VAL A 580 H THR A 596 1.57
REMARK 500 O ASP A 577 H TYR A 632 1.57
REMARK 500 H VAL A 629 O GLY A 642 1.57
REMARK 500 O LEU A 625 H LEU A 646 1.57
REMARK 500 HE2 HIS A 617 O LEU A 662 1.57
REMARK 500 H HIS A 566 OD1 ASN A 604 1.58
REMARK 500 O LEU A 620 H LYS A 623 1.58
REMARK 500 H ASP A 631 O ASP A 639 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 MET A 549 127.16 171.74
REMARK 500 1 ILE A 562 -75.78 -70.87
REMARK 500 1 TYR A 575 -169.93 -125.95
REMARK 500 1 ASP A 587 167.90 88.13
REMARK 500 1 LYS A 595 119.44 -160.75
REMARK 500 1 THR A 602 143.06 -179.44
REMARK 500 1 ASP A 614 70.49 -108.75
REMARK 500 1 GLU A 653 -52.62 -150.38
REMARK 500 1 TRP A 658 -81.00 -60.05
REMARK 500 1 ASN A 664 60.52 -100.17
REMARK 500 1 LYS A 665 -81.88 -53.40
REMARK 500 1 GLU A 678 -74.72 -100.37
REMARK 500 2 MET A 549 128.28 174.36
REMARK 500 2 ILE A 562 -73.28 -73.28
REMARK 500 2 TYR A 575 -169.15 -124.64
REMARK 500 2 ASP A 577 58.32 -117.52
REMARK 500 2 ASP A 587 105.52 -5.02
REMARK 500 2 LYS A 590 -34.67 87.20
REMARK 500 2 LYS A 595 119.01 -160.56
REMARK 500 2 LYS A 601 76.63 31.66
REMARK 500 2 THR A 602 144.56 -179.00
REMARK 500 2 ASP A 614 69.85 -104.75
REMARK 500 2 ASP A 633 119.02 -160.11
REMARK 500 2 GLU A 653 -40.07 -163.65
REMARK 500 2 TRP A 658 -80.20 -59.63
REMARK 500 2 ASN A 664 66.22 -107.78
REMARK 500 2 LYS A 665 -73.23 -67.69
REMARK 500 2 ASP A 666 -31.39 -33.32
REMARK 500 3 MET A 549 125.77 175.67
REMARK 500 3 SER A 551 77.22 -104.09
REMARK 500 3 ILE A 562 -75.04 -72.84
REMARK 500 3 TYR A 575 -168.70 -119.95
REMARK 500 3 ASP A 587 111.28 5.94
REMARK 500 3 LYS A 590 -25.11 87.67
REMARK 500 3 LYS A 601 75.72 34.73
REMARK 500 3 THR A 602 143.45 179.01
REMARK 500 3 ASP A 614 65.26 -107.74
REMARK 500 3 ASN A 638 -162.93 -77.87
REMARK 500 3 TRP A 658 -77.01 -61.15
REMARK 500 3 ASN A 664 68.82 -100.11
REMARK 500 3 LYS A 665 -79.90 -58.57
REMARK 500 3 GLU A 678 -79.44 -90.19
REMARK 500 4 MET A 549 136.28 -179.53
REMARK 500 4 ILE A 562 -75.06 -75.81
REMARK 500 4 TYR A 575 -169.36 -123.26
REMARK 500 4 ASP A 577 64.25 -115.90
REMARK 500 4 ASP A 587 107.49 -24.34
REMARK 500 4 LYS A 595 119.78 -160.16
REMARK 500 4 LYS A 601 63.82 68.81
REMARK 500 4 THR A 602 149.62 178.71
REMARK 500
REMARK 500 THIS ENTRY HAS 281 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3RPB A 541 680 UNP P47709 RP3A_RAT 541 680
SEQRES 1 A 140 ARG GLY LYS ILE LEU VAL SER LEU MET TYR SER THR GLN
SEQRES 2 A 140 GLN GLY GLY LEU ILE VAL GLY ILE ILE ARG CYS VAL HIS
SEQRES 3 A 140 LEU ALA ALA MET ASP ALA ASN GLY TYR SER ASP PRO PHE
SEQRES 4 A 140 VAL LYS LEU TRP LEU LYS PRO ASP MET GLY LYS LYS ALA
SEQRES 5 A 140 LYS HIS LYS THR GLN ILE LYS LYS LYS THR LEU ASN PRO
SEQRES 6 A 140 GLU PHE ASN GLU GLU PHE PHE TYR ASP ILE LYS HIS SER
SEQRES 7 A 140 ASP LEU ALA LYS LYS SER LEU ASP ILE SER VAL TRP ASP
SEQRES 8 A 140 TYR ASP ILE GLY LYS SER ASN ASP TYR ILE GLY GLY CYS
SEQRES 9 A 140 GLN LEU GLY ILE SER ALA LYS GLY GLU ARG LEU LYS HIS
SEQRES 10 A 140 TRP TYR GLU CYS LEU LYS ASN LYS ASP LYS LYS ILE GLU
SEQRES 11 A 140 ARG TRP HIS GLN LEU GLN ASN GLU ASN HIS
HELIX 1 1 HIS A 617 LEU A 620 1 4
HELIX 2 2 ARG A 654 LYS A 663 1 10
SHEET 1 A 3 ILE A 669 GLN A 674 0
SHEET 2 A 3 LYS A 543 SER A 551 -1 N LEU A 548 O ILE A 669
SHEET 3 A 3 GLY A 556 VAL A 565 -1 N VAL A 565 O LYS A 543
SHEET 1 B 3 PRO A 578 LYS A 585 0
SHEET 2 B 3 SER A 624 ASP A 631 -1 N TRP A 630 O PHE A 579
SHEET 3 B 3 ASP A 639 GLY A 647 -1 N LEU A 646 O LEU A 625
CISPEP 1 LYS A 585 PRO A 586 1 -0.20
CISPEP 2 LYS A 585 PRO A 586 2 -0.09
CISPEP 3 LYS A 585 PRO A 586 3 0.16
CISPEP 4 LYS A 585 PRO A 586 4 0.09
CISPEP 5 LYS A 585 PRO A 586 5 -0.18
CISPEP 6 LYS A 585 PRO A 586 6 0.06
CISPEP 7 LYS A 585 PRO A 586 7 -0.03
CISPEP 8 LYS A 585 PRO A 586 8 0.10
CISPEP 9 LYS A 585 PRO A 586 9 -0.09
CISPEP 10 LYS A 585 PRO A 586 10 -0.02
CISPEP 11 LYS A 585 PRO A 586 11 -0.12
CISPEP 12 LYS A 585 PRO A 586 12 -0.03
CISPEP 13 LYS A 585 PRO A 586 13 -0.13
CISPEP 14 LYS A 585 PRO A 586 14 -0.28
CISPEP 15 LYS A 585 PRO A 586 15 0.24
CISPEP 16 LYS A 585 PRO A 586 16 -0.11
CISPEP 17 LYS A 585 PRO A 586 17 0.11
CISPEP 18 LYS A 585 PRO A 586 18 -0.04
CISPEP 19 LYS A 585 PRO A 586 19 -0.23
CISPEP 20 LYS A 585 PRO A 586 20 -0.07
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 16 2 Bytes