Header list of 1cxw.pdb file
Complete list - c 21 2 Bytes
HEADER HYDROLASE 31-AUG-99 1CXW
TITLE THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN MATRIX METALLOPROTEINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE SECOND TYPE II MODULE;
COMPND 5 SYNONYM: COL-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;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMED23
KEYWDS BETA SHEET, ALPHA HELIX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 50
AUTHOR K.BRIKNAROVA,A.GRISHAEV,L.BANYAI,H.TORDAI,L.PATTHY,M.LLINAS
REVDAT 4 21-DEC-22 1CXW 1 SEQADV
REVDAT 3 16-FEB-22 1CXW 1 REMARK
REVDAT 2 24-FEB-09 1CXW 1 VERSN
REVDAT 1 12-NOV-99 1CXW 0
JRNL AUTH K.BRIKNAROVA,A.GRISHAEV,L.BANYAI,H.TORDAI,L.PATTHY,M.LLINAS
JRNL TITL THE SECOND TYPE II MODULE FROM HUMAN MATRIX
JRNL TITL 2 METALLOPROTEINASE 2: STRUCTURE, FUNCTION AND DYNAMICS.
JRNL REF STRUCTURE FOLD.DES. V. 7 1235 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10545322
JRNL DOI 10.1016/S0969-2126(00)80057-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, QUANTA 96
REMARK 3 AUTHORS : BRUKER, GERMANY (XWINNMR), MOLECULAR SIMULATIONS,
REMARK 3 INC., SAN DIEGO, CA (QUANTA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CXW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009614.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 5.2; 5.1
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.3MM COL-2 NA; 90% H2O, 10%
REMARK 210 D2O; 1.3MM COL-2 NA; D2O; 1MM
REMARK 210 COL-2 U-15N; 90% H2O, 10% D2O;
REMARK 210 4MM COL-2 U-15N; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; E-COSY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95, X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
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 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 ASP A 48 HZ3 LYS A 51 1.60
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 2 TYR A 53 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 TYR A 53 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 4 CYS A 41 CB - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 5 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 7 TYR A 26 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 14 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 16 CYS A 29 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 23 LYS A 52 CB - CA - C ANGL. DEV. = 19.9 DEGREES
REMARK 500 23 TYR A 53 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 31 TYR A 26 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 47 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 48 ARG A 39 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
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 6 71.38 26.81
REMARK 500 1 GLU A 11 42.94 36.95
REMARK 500 2 MET A 6 66.21 24.88
REMARK 500 2 ALA A 10 29.84 -74.26
REMARK 500 2 LYS A 51 41.87 70.65
REMARK 500 2 CYS A 56 106.65 -55.49
REMARK 500 2 GLU A 58 -118.54 54.46
REMARK 500 2 THR A 59 -74.06 68.82
REMARK 500 3 ALA A 2 -145.35 67.66
REMARK 500 3 MET A 6 -61.13 77.31
REMARK 500 3 ALA A 10 47.62 -86.22
REMARK 500 4 ALA A 2 89.29 -67.22
REMARK 500 4 MET A 6 50.13 162.82
REMARK 500 4 GLU A 11 29.80 47.60
REMARK 500 4 CYS A 15 151.67 -49.82
REMARK 500 4 GLN A 22 16.19 58.25
REMARK 500 4 THR A 44 175.65 73.05
REMARK 500 4 GLU A 58 -158.24 -104.38
REMARK 500 5 ALA A 2 172.69 64.54
REMARK 500 5 MET A 6 -58.24 -172.85
REMARK 500 5 ASN A 9 -123.48 -116.80
REMARK 500 6 PHE A 4 -121.16 -79.15
REMARK 500 6 LYS A 51 35.24 74.68
REMARK 500 6 CYS A 56 -172.54 57.62
REMARK 500 6 GLU A 58 131.58 -20.27
REMARK 500 7 ALA A 2 -156.70 -154.42
REMARK 500 7 PHE A 4 -135.97 -82.33
REMARK 500 7 ALA A 10 22.63 -64.60
REMARK 500 7 GLU A 58 -167.68 -164.26
REMARK 500 8 ALA A 2 34.33 -152.81
REMARK 500 8 LEU A 3 71.90 -115.85
REMARK 500 8 MET A 6 -76.87 -106.89
REMARK 500 8 ALA A 10 49.75 -80.00
REMARK 500 8 GLU A 58 50.02 -99.93
REMARK 500 9 ALA A 2 -102.92 153.48
REMARK 500 9 MET A 6 73.62 23.82
REMARK 500 9 ALA A 10 28.37 -72.98
REMARK 500 9 PRO A 57 -167.39 -73.84
REMARK 500 10 ALA A 2 14.05 -156.93
REMARK 500 10 PHE A 4 -97.71 -83.88
REMARK 500 10 THR A 5 -51.63 -139.06
REMARK 500 10 ALA A 10 46.98 -74.31
REMARK 500 10 GLU A 11 48.01 36.17
REMARK 500 10 GLN A 22 16.58 54.82
REMARK 500 10 PRO A 57 -147.00 -78.97
REMARK 500 11 PHE A 4 -125.88 -82.53
REMARK 500 11 GLU A 11 38.35 36.22
REMARK 500 11 THR A 44 168.31 72.37
REMARK 500 12 MET A 6 -83.66 -148.30
REMARK 500 12 ALA A 10 23.51 -79.49
REMARK 500
REMARK 500 THIS ENTRY HAS 259 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 13 PRO A 14 35 143.32
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 34 0.09 SIDE CHAIN
REMARK 500 9 ARG A 34 0.08 SIDE CHAIN
REMARK 500 12 TYR A 38 0.07 SIDE CHAIN
REMARK 500 14 TYR A 26 0.07 SIDE CHAIN
REMARK 500 15 TYR A 38 0.07 SIDE CHAIN
REMARK 500 16 TYR A 38 0.12 SIDE CHAIN
REMARK 500 18 ARG A 20 0.12 SIDE CHAIN
REMARK 500 19 TYR A 26 0.07 SIDE CHAIN
REMARK 500 20 ARG A 49 0.09 SIDE CHAIN
REMARK 500 22 TYR A 38 0.07 SIDE CHAIN
REMARK 500 24 TYR A 38 0.11 SIDE CHAIN
REMARK 500 25 TYR A 38 0.07 SIDE CHAIN
REMARK 500 32 TYR A 38 0.07 SIDE CHAIN
REMARK 500 34 ARG A 34 0.08 SIDE CHAIN
REMARK 500 41 TYR A 38 0.07 SIDE CHAIN
REMARK 500 43 TYR A 38 0.07 SIDE CHAIN
REMARK 500 47 ARG A 34 0.13 SIDE CHAIN
REMARK 500 49 ARG A 34 0.11 SIDE CHAIN
REMARK 500 49 TYR A 38 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CXW A 2 60 UNP P08253 MMP2_HUMAN 278 336
SEQADV 1CXW THR A 1 UNP P08253 CLONING ARTIFACT
SEQRES 1 A 60 THR ALA LEU PHE THR MET GLY GLY ASN ALA GLU GLY GLN
SEQRES 2 A 60 PRO CYS LYS PHE PRO PHE ARG PHE GLN GLY THR SER TYR
SEQRES 3 A 60 ASP SER CYS THR THR GLU GLY ARG THR ASP GLY TYR ARG
SEQRES 4 A 60 TRP CYS GLY THR THR GLU ASP TYR ASP ARG ASP LYS LYS
SEQRES 5 A 60 TYR GLY PHE CYS PRO GLU THR ALA
HELIX 1 1 ASP A 46 LYS A 51 1 6
SHEET 1 A 2 PHE A 19 PHE A 21 0
SHEET 2 A 2 THR A 24 TYR A 26 -1 O THR A 24 N PHE A 21
SHEET 1 B 2 ARG A 39 GLY A 42 0
SHEET 2 B 2 TYR A 53 CYS A 56 -1 N GLY A 54 O CYS A 41
SSBOND 1 CYS A 15 CYS A 41 1555 1555 2.03
SSBOND 2 CYS A 29 CYS A 56 1555 1555 2.03
CISPEP 1 PHE A 17 PRO A 18 1 -18.28
CISPEP 2 PHE A 17 PRO A 18 2 -10.83
CISPEP 3 PHE A 17 PRO A 18 3 -7.36
CISPEP 4 PHE A 17 PRO A 18 4 -8.97
CISPEP 5 PHE A 17 PRO A 18 5 -6.46
CISPEP 6 PHE A 17 PRO A 18 6 -7.81
CISPEP 7 PHE A 17 PRO A 18 7 -12.14
CISPEP 8 PHE A 17 PRO A 18 8 -8.95
CISPEP 9 PHE A 17 PRO A 18 9 -7.39
CISPEP 10 PHE A 17 PRO A 18 10 -5.69
CISPEP 11 PHE A 17 PRO A 18 11 -12.56
CISPEP 12 PHE A 17 PRO A 18 12 -14.54
CISPEP 13 PHE A 17 PRO A 18 13 -4.29
CISPEP 14 PHE A 17 PRO A 18 14 -4.48
CISPEP 15 PHE A 17 PRO A 18 15 -7.78
CISPEP 16 PHE A 17 PRO A 18 16 -16.83
CISPEP 17 PHE A 17 PRO A 18 17 -8.29
CISPEP 18 PHE A 17 PRO A 18 18 -18.20
CISPEP 19 PHE A 17 PRO A 18 19 -8.05
CISPEP 20 PHE A 17 PRO A 18 20 -12.58
CISPEP 21 PHE A 17 PRO A 18 21 -19.03
CISPEP 22 PHE A 17 PRO A 18 22 -10.52
CISPEP 23 PHE A 17 PRO A 18 23 -11.07
CISPEP 24 PHE A 17 PRO A 18 24 -14.09
CISPEP 25 PHE A 17 PRO A 18 25 -9.94
CISPEP 26 PHE A 17 PRO A 18 26 -8.91
CISPEP 27 PHE A 17 PRO A 18 27 -18.66
CISPEP 28 PHE A 17 PRO A 18 28 -11.67
CISPEP 29 PHE A 17 PRO A 18 29 -10.10
CISPEP 30 PHE A 17 PRO A 18 30 -9.85
CISPEP 31 PHE A 17 PRO A 18 31 -7.07
CISPEP 32 PHE A 17 PRO A 18 32 -7.18
CISPEP 33 PHE A 17 PRO A 18 33 -7.39
CISPEP 34 PHE A 17 PRO A 18 34 -9.41
CISPEP 35 PHE A 17 PRO A 18 35 -8.07
CISPEP 36 PHE A 17 PRO A 18 36 -10.85
CISPEP 37 PHE A 17 PRO A 18 37 -18.09
CISPEP 38 PHE A 17 PRO A 18 38 -8.93
CISPEP 39 PHE A 17 PRO A 18 39 -12.65
CISPEP 40 PHE A 17 PRO A 18 40 -29.22
CISPEP 41 PHE A 17 PRO A 18 41 -11.83
CISPEP 42 PHE A 17 PRO A 18 42 -12.96
CISPEP 43 PHE A 17 PRO A 18 43 -9.97
CISPEP 44 PHE A 17 PRO A 18 44 -8.29
CISPEP 45 PHE A 17 PRO A 18 45 -6.31
CISPEP 46 PHE A 17 PRO A 18 46 -11.48
CISPEP 47 PHE A 17 PRO A 18 47 -13.68
CISPEP 48 PHE A 17 PRO A 18 48 -11.42
CISPEP 49 PHE A 17 PRO A 18 49 -12.28
CISPEP 50 PHE A 17 PRO A 18 50 -2.57
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 - c 21 2 Bytes