HEADER HYDROLASE 10-JAN-02 1KS0
TITLE THE FIRST FIBRONECTIN TYPE II MODULE FROM HUMAN MATRIX
TITLE 2 METALLOPROTEINASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATRIX METALLOPROTEINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST FIBRONECTIN TYPE II MODULE;
COMPND 5 SYNONYM: 72 KDA TYPE IV COLLAGENASE, MMP-2;
COMPND 6 EC: 3.4.24.24;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA SHEET, ALPHA HELIX, 3/1 HELIX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 50
AUTHOR M.GEHRMANN,K.BRIKNAROVA,L.BANYAI,L.PATTHY,M.LLINAS
REVDAT 4 23-FEB-22 1KS0 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1KS0 1 VERSN
REVDAT 2 17-APR-02 1KS0 1 JRNL
REVDAT 1 20-FEB-02 1KS0 0
JRNL AUTH M.GEHRMANN,K.BRIKNAROVA,L.BANYAI,L.PATTHY,M.LLINAS
JRNL TITL THE COL-1 MODULE OF HUMAN MATRIX METALLOPROTEINASE-2
JRNL TITL 2 (MMP-2): STRUCTURAL/FUNCTIONAL RELATEDNESS BETWEEN
JRNL TITL 3 GELATIN-BINDING FIBRONECTIN TYPE II MODULES AND
JRNL TITL 4 LYSINE-BINDING KRINGLE DOMAINS.
JRNL REF BIOL.CHEM. V. 383 137 2002
JRNL REFN ISSN 1431-6730
JRNL PMID 11928808
JRNL DOI 10.1515/BC.2002.014
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KS0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015280.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 7.3; 6.0
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM COL-1; 90% H2O, 10% D6
REMARK 210 -ACETONE; 0.5MM COL-1; 90% D2O,
REMARK 210 10% D6-ACETONE; 0.7MM COL-1 15N;
REMARK 210 90% H2O, 10% D6-ACETONE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING/MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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 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 1-50
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 60
REMARK 465 PHE A 61
REMARK 465 THR A 62
REMARK 465 MET A 63
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 ILE A 2 56.93 39.78
REMARK 500 1 LYS A 5 -79.24 -138.12
REMARK 500 1 ALA A 9 -73.51 -93.84
REMARK 500 1 ASP A 10 88.28 56.48
REMARK 500 1 TYR A 44 -77.15 -78.92
REMARK 500 1 HIS A 57 -84.80 -82.61
REMARK 500 2 PRO A 3 32.27 -78.93
REMARK 500 2 VAL A 4 160.23 70.96
REMARK 500 2 LYS A 5 -85.47 -107.08
REMARK 500 2 ASN A 21 18.26 57.79
REMARK 500 2 THR A 43 -167.37 -110.34
REMARK 500 2 ASP A 49 -62.05 -91.60
REMARK 500 2 GLU A 58 40.86 -85.75
REMARK 500 3 LYS A 5 -103.36 -89.11
REMARK 500 3 ASP A 10 82.22 45.21
REMARK 500 3 TYR A 44 -68.17 71.96
REMARK 500 3 ASP A 49 -63.45 -92.56
REMARK 500 4 ILE A 2 58.84 37.92
REMARK 500 4 LYS A 5 -78.62 -127.06
REMARK 500 4 ALA A 9 53.79 -94.98
REMARK 500 4 THR A 43 -146.90 -105.91
REMARK 500 4 GLU A 58 -156.65 -113.96
REMARK 500 5 ILE A 2 -24.14 -161.10
REMARK 500 5 LYS A 5 -85.14 -117.04
REMARK 500 5 ASP A 10 -125.73 64.92
REMARK 500 5 GLU A 12 -159.49 -83.55
REMARK 500 5 HIS A 57 -151.71 -155.07
REMARK 500 6 PRO A 3 4.07 -68.68
REMARK 500 6 VAL A 4 147.48 75.46
REMARK 500 6 LYS A 5 -126.10 -102.40
REMARK 500 6 GLU A 58 -125.78 -74.68
REMARK 500 7 ILE A 2 130.77 60.51
REMARK 500 7 LYS A 5 -72.44 -130.84
REMARK 500 7 ASP A 10 -71.94 -67.36
REMARK 500 7 ASN A 21 21.02 49.79
REMARK 500 7 SER A 34 34.51 -145.16
REMARK 500 7 PHE A 37 -153.40 -81.56
REMARK 500 7 LEU A 38 111.54 -162.47
REMARK 500 7 CYS A 55 -69.10 -100.25
REMARK 500 7 PRO A 56 49.88 -90.76
REMARK 500 7 HIS A 57 -152.29 -129.88
REMARK 500 8 VAL A 4 155.70 73.41
REMARK 500 8 LYS A 5 -77.87 -109.65
REMARK 500 8 ASP A 10 -90.45 -99.16
REMARK 500 8 ASP A 49 -65.19 -101.09
REMARK 500 8 GLU A 58 40.99 -103.56
REMARK 500 9 ILE A 2 63.84 -165.68
REMARK 500 9 LYS A 5 -71.95 -145.29
REMARK 500 9 GLU A 12 -159.53 -79.62
REMARK 500 10 PRO A 3 -90.04 -89.92
REMARK 500
REMARK 500 THIS ENTRY HAS 232 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J7M RELATED DB: PDB
REMARK 900 1J7M IS THE THIRD FIBRONECTIN TYPE II MODULE OF MMP-2
REMARK 900 RELATED ID: 1CXW RELATED DB: PDB
REMARK 900 1CXW IS THE SECOND FIBRONECTIN TYPE II MODULE OF MMP-2
DBREF 1KS0 A 4 63 UNP P08253 MMP2_HUMAN 223 282
SEQADV 1KS0 ARG A 1 UNP P08253 CLONING ARTIFACT
SEQADV 1KS0 ILE A 2 UNP P08253 CLONING ARTIFACT
SEQADV 1KS0 PRO A 3 UNP P08253 CLONING ARTIFACT
SEQRES 1 A 63 ARG ILE PRO VAL LYS TYR GLY ASN ALA ASP GLY GLU TYR
SEQRES 2 A 63 CYS LYS PHE PRO PHE LEU PHE ASN GLY LYS GLU TYR ASN
SEQRES 3 A 63 SER CYS THR ASP THR GLY ARG SER ASP GLY PHE LEU TRP
SEQRES 4 A 63 CYS SER THR THR TYR ASN PHE GLU LYS ASP GLY LYS TYR
SEQRES 5 A 63 GLY PHE CYS PRO HIS GLU ALA LEU PHE THR MET
HELIX 1 1 ASN A 45 GLY A 50 1 6
SHEET 1 A 2 PHE A 18 PHE A 20 0
SHEET 2 A 2 LYS A 23 TYR A 25 -1 O LYS A 23 N PHE A 20
SHEET 1 B 2 TRP A 39 SER A 41 0
SHEET 2 B 2 TYR A 52 PHE A 54 -1 O GLY A 53 N CYS A 40
SSBOND 1 CYS A 14 CYS A 40 1555 1555 2.03
SSBOND 2 CYS A 28 CYS A 55 1555 1555 2.03
CISPEP 1 PHE A 16 PRO A 17 1 0.14
CISPEP 2 PHE A 16 PRO A 17 2 -0.38
CISPEP 3 PHE A 16 PRO A 17 3 0.04
CISPEP 4 PHE A 16 PRO A 17 4 -0.42
CISPEP 5 PHE A 16 PRO A 17 5 -0.32
CISPEP 6 PHE A 16 PRO A 17 6 -0.04
CISPEP 7 PHE A 16 PRO A 17 7 -0.16
CISPEP 8 PHE A 16 PRO A 17 8 0.01
CISPEP 9 PHE A 16 PRO A 17 9 0.18
CISPEP 10 PHE A 16 PRO A 17 10 -0.24
CISPEP 11 PHE A 16 PRO A 17 11 -0.18
CISPEP 12 PHE A 16 PRO A 17 12 0.50
CISPEP 13 PHE A 16 PRO A 17 13 -0.09
CISPEP 14 PHE A 16 PRO A 17 14 -0.57
CISPEP 15 PHE A 16 PRO A 17 15 0.98
CISPEP 16 PHE A 16 PRO A 17 16 0.29
CISPEP 17 PHE A 16 PRO A 17 17 -0.14
CISPEP 18 PHE A 16 PRO A 17 18 -0.32
CISPEP 19 PHE A 16 PRO A 17 19 0.36
CISPEP 20 PHE A 16 PRO A 17 20 -0.48
CISPEP 21 PHE A 16 PRO A 17 21 0.70
CISPEP 22 PHE A 16 PRO A 17 22 -0.16
CISPEP 23 PHE A 16 PRO A 17 23 -0.19
CISPEP 24 PHE A 16 PRO A 17 24 0.10
CISPEP 25 PHE A 16 PRO A 17 25 -0.53
CISPEP 26 PHE A 16 PRO A 17 26 0.39
CISPEP 27 PHE A 16 PRO A 17 27 0.24
CISPEP 28 PHE A 16 PRO A 17 28 -0.33
CISPEP 29 PHE A 16 PRO A 17 29 -0.23
CISPEP 30 PHE A 16 PRO A 17 30 -0.33
CISPEP 31 PHE A 16 PRO A 17 31 0.32
CISPEP 32 PHE A 16 PRO A 17 32 -0.28
CISPEP 33 PHE A 16 PRO A 17 33 0.06
CISPEP 34 PHE A 16 PRO A 17 34 0.43
CISPEP 35 PHE A 16 PRO A 17 35 0.01
CISPEP 36 PHE A 16 PRO A 17 36 -0.09
CISPEP 37 PHE A 16 PRO A 17 37 0.05
CISPEP 38 PHE A 16 PRO A 17 38 0.14
CISPEP 39 PHE A 16 PRO A 17 39 0.25
CISPEP 40 PHE A 16 PRO A 17 40 -0.25
CISPEP 41 PHE A 16 PRO A 17 41 0.26
CISPEP 42 PHE A 16 PRO A 17 42 -0.41
CISPEP 43 PHE A 16 PRO A 17 43 -0.39
CISPEP 44 PHE A 16 PRO A 17 44 0.62
CISPEP 45 PHE A 16 PRO A 17 45 -0.18
CISPEP 46 PHE A 16 PRO A 17 46 0.29
CISPEP 47 PHE A 16 PRO A 17 47 -0.52
CISPEP 48 PHE A 16 PRO A 17 48 0.15
CISPEP 49 PHE A 16 PRO A 17 49 0.06
CISPEP 50 PHE A 16 PRO A 17 50 -0.11
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