Header list of 1bf0.pdb file
Complete list - t 27 2 Bytes
HEADER CALCIUM CHANNEL BLOCKER 26-MAY-98 1BF0
TITLE CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCICLUDINE;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;
SOURCE 3 ORGANISM_COMMON: EASTERN GREEN MAMBA;
SOURCE 4 ORGANISM_TAXID: 8618;
SOURCE 5 OTHER_DETAILS: VENOM
KEYWDS CALCIUM CHANNEL BLOCKER
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.GILQUIN,A.LECOQ,F.DESNE,M.GUENNEUGUES,S.ZINN-JUSTIN,A.MENEZ
REVDAT 3 27-OCT-21 1BF0 1 COMPND SOURCE REMARK
REVDAT 2 24-FEB-09 1BF0 1 VERSN
REVDAT 1 13-JAN-99 1BF0 0
JRNL AUTH B.GILQUIN,A.LECOQ,F.DESNE,M.GUENNEUGUES,S.ZINN-JUSTIN,
JRNL AUTH 2 A.MENEZ
JRNL TITL CONFORMATIONAL AND FUNCTIONAL VARIABILITY SUPPORTED BY THE
JRNL TITL 2 BPTI FOLD: SOLUTION STRUCTURE OF THE CA2+ CHANNEL BLOCKER
JRNL TITL 3 CALCICLUDINE.
JRNL REF PROTEINS V. 34 520 1999
JRNL REFN ISSN 0887-3585
JRNL PMID 10081964
JRNL DOI 10.1002/(SICI)1097-0134(19990301)34:4<520::AID-PROT11>3.3.CO
JRNL DOI 2 ;2-E
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DETAILS ON THE STRUCTURE CALCULATION
REMARK 3 CAN BE FOUND IN THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1BF0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171677.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 30
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : MD- BASED SIMULATED ANNEALING
REMARK 210 WITH AMBIGOUS DISTANCE
REMARK 210 CONSTRAINTS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: COLLECTION OF ANGLE AND DISTANCE CONSTRAINTS WERE DERIVED
REMARK 210 FROM DQF-COSY AND NOESY EXPERIMENT RESPECTIVELY, CARRIED OUT IN
REMARK 210 H2O AND D2O. MIXING TIME OF 50, 75, 100 AND 150 MS WERE USED IN
REMARK 210 THE NOESY EXPERIMENTS. DISTANCE CONSTRAINTS WERE DERIVED FROM
REMARK 210 THE BUILD-UP CURVES RATES BY APPLYING AN AUTOMATED ITERATIVE
REMARK 210 ASSIGNMENT PROCEDURE.
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: 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 12 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 1 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 2 TRP A 5 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
REMARK 500 2 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 3 VAL A 11 CG1 - CB - CG2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 3 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 3 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 4 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 PHE A 47 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 5 TYR A 6 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 5 ARG A 12 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 6 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 6 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 6 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 7 PHE A 37 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 7 CYS A 40 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 7 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 7 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 8 CYS A 40 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 8 ARG A 46 NH1 - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 8 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 8 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 9 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 9 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 9 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 10 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 10 PHE A 37 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 10 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 10 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 10 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 11 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 11 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 11 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 11 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 12 PHE A 37 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 12 PHE A 37 CB - CG - CD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 12 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 12 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 12 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 64 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 PRO A 4 -113.93 -92.07
REMARK 500 1 TRP A 5 -70.46 -85.55
REMARK 500 1 LYS A 17 44.36 -77.74
REMARK 500 1 LYS A 30 19.42 89.30
REMARK 500 1 ASN A 43 -106.60 -136.93
REMARK 500 1 ALA A 44 29.32 -167.75
REMARK 500 2 PRO A 4 -115.88 -77.76
REMARK 500 2 SER A 15 76.03 -171.24
REMARK 500 2 CYS A 16 -71.76 -125.13
REMARK 500 2 LYS A 17 -80.08 -96.70
REMARK 500 2 LYS A 18 -145.61 -146.87
REMARK 500 2 SER A 22 -167.11 -120.26
REMARK 500 2 LYS A 30 26.39 80.01
REMARK 500 2 ASN A 43 -99.81 -134.37
REMARK 500 2 ALA A 44 24.40 -150.79
REMARK 500 2 ASN A 45 48.20 -101.70
REMARK 500 2 LYS A 56 -47.03 -167.77
REMARK 500 3 PRO A 4 -113.22 -94.46
REMARK 500 3 LYS A 17 58.27 -111.05
REMARK 500 3 CYS A 40 56.22 -114.12
REMARK 500 3 ASN A 43 -112.88 -113.07
REMARK 500 3 ALA A 44 -9.31 -141.64
REMARK 500 3 ASN A 45 57.20 -101.53
REMARK 500 3 LYS A 56 -39.81 -179.62
REMARK 500 3 LEU A 58 -8.97 -140.58
REMARK 500 4 PRO A 4 -123.15 -91.78
REMARK 500 4 TRP A 5 -74.14 -73.09
REMARK 500 4 CYS A 16 -127.55 -125.89
REMARK 500 4 LYS A 17 -99.40 -79.90
REMARK 500 4 LYS A 30 23.59 84.36
REMARK 500 4 PHE A 35 -159.24 -149.55
REMARK 500 4 ASN A 43 -92.98 -127.31
REMARK 500 4 ALA A 44 -30.00 -136.52
REMARK 500 5 PRO A 4 -116.92 -94.11
REMARK 500 5 TYR A 6 -7.77 -48.44
REMARK 500 5 ILE A 13 -55.42 -155.49
REMARK 500 5 SER A 15 134.73 -176.66
REMARK 500 5 CYS A 16 -63.77 -176.03
REMARK 500 5 LYS A 17 -98.46 -105.29
REMARK 500 5 SER A 22 -159.62 -125.50
REMARK 500 5 ASN A 43 -78.49 -88.48
REMARK 500 5 ASN A 45 78.49 -109.45
REMARK 500 5 LEU A 58 -32.41 -136.54
REMARK 500 6 PRO A 4 -114.38 -96.59
REMARK 500 6 ILE A 13 -54.03 -125.18
REMARK 500 6 SER A 15 52.65 -150.66
REMARK 500 6 LYS A 30 22.28 81.96
REMARK 500 6 CYS A 40 34.23 -79.45
REMARK 500 6 ALA A 44 -21.95 -177.35
REMARK 500 7 PRO A 4 -110.31 -73.79
REMARK 500
REMARK 500 THIS ENTRY HAS 125 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 2 ARG A 46 0.17 SIDE CHAIN
REMARK 500 2 ARG A 54 0.15 SIDE CHAIN
REMARK 500 5 ARG A 12 0.18 SIDE CHAIN
REMARK 500 5 ARG A 46 0.08 SIDE CHAIN
REMARK 500 5 ARG A 54 0.08 SIDE CHAIN
REMARK 500 7 ARG A 46 0.07 SIDE CHAIN
REMARK 500 8 ARG A 12 0.12 SIDE CHAIN
REMARK 500 8 ARG A 46 0.09 SIDE CHAIN
REMARK 500 10 ARG A 46 0.10 SIDE CHAIN
REMARK 500 12 ARG A 12 0.09 SIDE CHAIN
REMARK 500 12 ARG A 54 0.10 SIDE CHAIN
REMARK 500 14 ARG A 46 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BF0 A 1 60 UNP P81658 TXCA_DENAN 1 60
SEQRES 1 A 60 TRP GLN PRO PRO TRP TYR CYS LYS GLU PRO VAL ARG ILE
SEQRES 2 A 60 GLY SER CYS LYS LYS GLN PHE SER SER PHE TYR PHE LYS
SEQRES 3 A 60 TRP THR ALA LYS LYS CYS LEU PRO PHE LEU PHE SER GLY
SEQRES 4 A 60 CYS GLY GLY ASN ALA ASN ARG PHE GLN THR ILE GLY GLU
SEQRES 5 A 60 CYS ARG LYS LYS CYS LEU GLY LYS
HELIX 1 H1 TRP A 5 LYS A 8 5 4
HELIX 2 H2 ILE A 50 LEU A 58 5 9
SHEET 1 S2 2 PHE A 20 LYS A 26 0
SHEET 2 S2 2 LYS A 31 PHE A 37 -1 N PHE A 37 O PHE A 20
SSBOND 1 CYS A 7 CYS A 57 1555 1555 2.03
SSBOND 2 CYS A 16 CYS A 40 1555 1555 2.06
SSBOND 3 CYS A 32 CYS A 53 1555 1555 2.00
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 - t 27 2 Bytes