HEADER HYDROLASE 18-DEC-01 1KN6
TITLE SOLUTION STRUCTURE OF THE MOUSE PROHORMONE CONVERTASE 1 PRO-DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROHORMONE CONVERTASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL PRO-DOMAIN;
COMPND 5 SYNONYM: NEUROENDOCRINE CONVERTASE 1;
COMPND 6 EC: 3.4.21.93;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PG5
KEYWDS BETA-ALPHA-BETA-BETA-ALPHA-BETA, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.TANGREA,P.N.BRYAN,N.SARI,J.ORBAN
REVDAT 5 21-DEC-22 1KN6 1 SEQADV
REVDAT 4 23-FEB-22 1KN6 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1KN6 1 VERSN
REVDAT 2 01-APR-03 1KN6 1 JRNL
REVDAT 1 17-JUL-02 1KN6 0
JRNL AUTH M.A.TANGREA,P.N.BRYAN,N.SARI,J.ORBAN
JRNL TITL SOLUTION STRUCTURE OF THE PRO-HORMONE CONVERTASE 1
JRNL TITL 2 PRO-DOMAIN FROM MUS MUSCULUS.
JRNL REF J.MOL.BIOL. V. 320 801 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12095256
JRNL DOI 10.1016/S0022-2836(02)00543-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.8
REMARK 3 AUTHORS : DELAGLIO, F., ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KN6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015133.
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 : 2MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 100MM PHOSPHATE BUFFER; UNIFORM
REMARK 210 (RANDOM) LABELING WITH 15N, 13C;
REMARK 210 100MM PHOSPHATE BUFFER; UNIFORM
REMARK 210 (RANDOM) LABELING WITH 15N, 13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 280
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 : 3
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 LYS A 1
REMARK 465 ARG A 2
REMARK 465 GLN A 3
REMARK 465 GLU A 77
REMARK 465 LYS A 78
REMARK 465 GLU A 79
REMARK 465 ARG A 80
REMARK 465 SER A 81
REMARK 465 LYS A 82
REMARK 465 ARG A 83
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 H LEU A 31 O LEU A 42 1.54
REMARK 500 O GLY A 15 H ALA A 19 1.59
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 VAL A 5 -86.10 -129.36
REMARK 500 1 ASN A 6 129.76 158.00
REMARK 500 1 GLU A 38 74.04 32.78
REMARK 500 1 ASN A 39 -31.11 174.86
REMARK 500 1 LYS A 46 -32.78 -156.97
REMARK 500 1 HIS A 48 52.33 -168.84
REMARK 500 1 SER A 52 37.61 176.43
REMARK 500 1 SER A 55 -139.45 -167.28
REMARK 500 1 ALA A 56 63.93 60.95
REMARK 500 1 LYS A 61 -78.28 -129.44
REMARK 500 1 THR A 70 -74.14 -158.70
REMARK 500 2 VAL A 5 -77.51 -138.08
REMARK 500 2 ASN A 6 -139.31 38.80
REMARK 500 2 GLN A 33 62.92 -150.87
REMARK 500 2 GLU A 38 98.92 40.68
REMARK 500 2 ASN A 39 -35.42 165.81
REMARK 500 2 LYS A 46 78.53 -66.54
REMARK 500 2 SER A 47 -46.94 -152.40
REMARK 500 2 ARG A 50 31.93 -97.44
REMARK 500 2 ARG A 51 106.08 75.66
REMARK 500 2 SER A 52 31.76 78.54
REMARK 500 2 SER A 55 -175.87 -64.72
REMARK 500 2 LEU A 57 -81.13 -141.40
REMARK 500 2 LYS A 61 -58.83 -132.89
REMARK 500 2 THR A 70 -77.12 -156.95
REMARK 500 3 VAL A 5 -42.20 -141.77
REMARK 500 3 ASN A 6 -121.43 -58.65
REMARK 500 3 GLN A 16 -73.56 -62.30
REMARK 500 3 GLU A 25 -75.27 -80.26
REMARK 500 3 LEU A 37 -159.39 -160.30
REMARK 500 3 ASN A 39 -27.32 -176.63
REMARK 500 3 HIS A 45 64.72 -167.38
REMARK 500 3 LYS A 46 85.66 -159.64
REMARK 500 3 HIS A 48 -68.32 -92.31
REMARK 500 3 PRO A 49 -166.97 -68.45
REMARK 500 3 ARG A 51 110.48 -177.30
REMARK 500 3 ALA A 56 -157.08 -60.75
REMARK 500 3 LEU A 57 -67.48 -161.58
REMARK 500 3 LYS A 61 -64.22 -135.26
REMARK 500 3 THR A 70 -77.24 -155.57
REMARK 500 4 ASN A 6 -78.24 -173.51
REMARK 500 4 PRO A 13 60.80 -66.57
REMARK 500 4 GLN A 16 -76.35 -65.14
REMARK 500 4 GLN A 33 73.66 -151.64
REMARK 500 4 SER A 36 -60.80 -109.85
REMARK 500 4 LEU A 37 -113.18 -124.03
REMARK 500 4 GLU A 38 63.06 -157.47
REMARK 500 4 HIS A 45 97.70 -172.64
REMARK 500 4 LYS A 46 -77.66 -91.81
REMARK 500 4 HIS A 48 -41.56 178.39
REMARK 500
REMARK 500 THIS ENTRY HAS 284 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KN6 A 1 83 UNP P63239 NEC1_MOUSE 28 110
SEQADV 1KN6 MET A -6 UNP P63239 INITIATING METHIONINE
SEQADV 1KN6 HIS A -5 UNP P63239 EXPRESSION TAG
SEQADV 1KN6 HIS A -4 UNP P63239 EXPRESSION TAG
SEQADV 1KN6 HIS A -3 UNP P63239 EXPRESSION TAG
SEQADV 1KN6 HIS A -2 UNP P63239 EXPRESSION TAG
SEQADV 1KN6 HIS A -1 UNP P63239 EXPRESSION TAG
SEQADV 1KN6 HIS A 0 UNP P63239 EXPRESSION TAG
SEQRES 1 A 90 MET HIS HIS HIS HIS HIS HIS LYS ARG GLN PHE VAL ASN
SEQRES 2 A 90 GLU TRP ALA ALA GLU ILE PRO GLY GLY GLN GLU ALA ALA
SEQRES 3 A 90 SER ALA ILE ALA GLU GLU LEU GLY TYR ASP LEU LEU GLY
SEQRES 4 A 90 GLN ILE GLY SER LEU GLU ASN HIS TYR LEU PHE LYS HIS
SEQRES 5 A 90 LYS SER HIS PRO ARG ARG SER ARG ARG SER ALA LEU HIS
SEQRES 6 A 90 ILE THR LYS ARG LEU SER ASP ASP ASP ARG VAL THR TRP
SEQRES 7 A 90 ALA GLU GLN GLN TYR GLU LYS GLU ARG SER LYS ARG
HELIX 1 1 GLY A 15 GLY A 27 1 13
HELIX 2 2 LYS A 61 ARG A 68 1 8
SHEET 1 A 4 ASP A 29 LEU A 30 0
SHEET 2 A 4 HIS A 40 LYS A 44 -1 O LYS A 44 N ASP A 29
SHEET 3 A 4 TRP A 8 GLU A 11 -1 N ALA A 10 O TYR A 41
SHEET 4 A 4 TRP A 71 GLU A 73 -1 O GLU A 73 N ALA A 9
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
(ATOM LINES ARE NOT SHOWN.)
END
