Header list of 3ayk.pdb file
Complete list - 30 20 Bytes
HEADER MATRIX METALLOPROTEINASE 01-FEB-99 3AYK
TITLE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-
TITLE 2 27023A, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (COLLAGENASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC FRAGMENT;
COMPND 5 SYNONYM: MMP-1, FIBROBLAST COLLAGENASE;
COMPND 6 EC: 3.4.24.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: HETEROGEN: N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)
COMPND 9 SULFONYL](3-PICOLYL)AMINO]-3- METHYLBUTANAMIDE HYDROCHLORIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL21 (DE3);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-21A(+);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNOT-3A
KEYWDS MATRIX METALLOPROTEINASE, HYDROLASE, METALLOPROTEASE, GLYCOPROTEIN
EXPDTA SOLUTION NMR
AUTHOR R.POWERS,F.J.MOY
REVDAT 3 30-OCT-19 3AYK 1 JRNL REMARK
REVDAT 2 24-FEB-09 3AYK 1 VERSN
REVDAT 1 07-JUN-99 3AYK 0
JRNL AUTH F.J.MOY,P.K.CHANDA,J.M.CHEN,S.COSMI,W.EDRIS,J.S.SKOTNICKI,
JRNL AUTH 2 J.WILHELM,R.POWERS
JRNL TITL NMR SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMAN
JRNL TITL 2 FIBROBLAST COLLAGENASE COMPLEXED WITH A SULFONAMIDE
JRNL TITL 3 DERIVATIVE OF A HYDROXAMIC ACID COMPOUND.
JRNL REF BIOCHEMISTRY V. 38 7085 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10353819
JRNL DOI 10.1021/BI982576V
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.MOY,P.K.CHANDA,S.COSMI,M.R.PISANO,C.URBANO,J.WILHELM,
REMARK 1 AUTH 2 R.POWERS
REMARK 1 TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE INHIBITOR-FREE
REMARK 1 TITL 2 CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE
REMARK 1 TITL 3 DETERMINED BY MULTIDIMENSIONAL NMR.
REMARK 1 REF BIOCHEMISTRY V. 37 1495 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9484219
REMARK 1 DOI 10.1021/BI972181W
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.J.MOY,M.R.PISANO,P.K.CHANDA,C.URBANO,L.M.KILLAR,M.L.SUNG,
REMARK 1 AUTH 2 R.POWERS
REMARK 1 TITL ASSIGNMENTS, SECONDARY STRUCTURE AND DYNAMICS OF THE
REMARK 1 TITL 2 INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST
REMARK 1 TITL 3 COLLAGENASE.
REMARK 1 REF J.BIOMOL.NMR V. 10 9 1997
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 9335112
REMARK 1 DOI 10.1023/A:1018362914316
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 3AYK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000423.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.00
REMARK 210 PH : 6.50
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; TRIPLE
REMARK 210 -RESONANCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX2600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 -DYNAMICAL SIMULATED ANNEALING
REMARK 210 METHOD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY, LOWEST
REMARK 210 VIOLATIONS, CONSISTENT FOLD
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: RESTRAINED MINIMIZED MEAN STRUCTURE. THE STRUCTURE WAS
REMARK 210 DETERMINED USING TRIPLE- RESONANCE NMR SPECTROSCOPY ON 13C, 15N-
REMARK 210 LABELED MMP-1.
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 RES C SSSEQI
REMARK 465 VAL A 1
REMARK 465 LEU A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 GLY A 5
REMARK 465 ASN A 6
REMARK 465 GLN A 164
REMARK 465 ASN A 165
REMARK 465 PRO A 166
REMARK 465 VAL A 167
REMARK 465 GLN A 168
REMARK 465 PRO A 169
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 ASN A 106 H ARG A 108 1.54
REMARK 500 O TRP A 41 HG1 THR A 45 1.58
REMARK 500 O ARG A 27 H ASP A 31 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 PRO A 26 -177.05 -60.17
REMARK 500 PRO A 46 6.13 -62.57
REMARK 500 ASP A 75 72.92 -112.20
REMARK 500 PRO A 87 100.68 -58.01
REMARK 500 PHE A 107 34.35 -61.98
REMARK 500 ARG A 108 -161.39 -74.88
REMARK 500 MET A 136 47.48 -73.51
REMARK 500 SER A 143 -128.69 -109.75
REMARK 500 TYR A 160 -68.08 -99.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 171 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 68 NE2
REMARK 620 2 HIS A 83 NE2 130.2
REMARK 620 3 HIS A 96 ND1 114.1 108.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 172 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 77 O
REMARK 620 2 GLY A 78 O 71.6
REMARK 620 3 ASP A 98 OD2 140.1 135.7
REMARK 620 4 ASN A 80 O 133.9 88.5 82.5
REMARK 620 5 GLY A 76 O 76.6 58.1 94.3 127.4
REMARK 620 6 GLU A 101 OE2 55.7 126.9 93.4 122.7 109.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 170 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 118 NE2
REMARK 620 2 HIS A 122 NE2 80.1
REMARK 620 3 HIS A 128 NE2 103.4 95.4
REMARK 620 4 CGS A 173 O47 123.0 151.8 94.4
REMARK 620 5 CGS A 173 O48 72.4 101.5 161.4 74.2
REMARK 620 6 CGS A 173 N35 101.3 112.4 145.5 51.6 29.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZNA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CGS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CGS-27023A BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 172
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CGS A 173
DBREF 3AYK A 1 169 UNP P03956 MMP1_HUMAN 101 269
SEQRES 1 A 169 VAL LEU THR GLU GLY ASN PRO ARG TRP GLU GLN THR HIS
SEQRES 2 A 169 LEU THR TYR ARG ILE GLU ASN TYR THR PRO ASP LEU PRO
SEQRES 3 A 169 ARG ALA ASP VAL ASP HIS ALA ILE GLU LYS ALA PHE GLN
SEQRES 4 A 169 LEU TRP SER ASN VAL THR PRO LEU THR PHE THR LYS VAL
SEQRES 5 A 169 SER GLU GLY GLN ALA ASP ILE MET ILE SER PHE VAL ARG
SEQRES 6 A 169 GLY ASP HIS ARG ASP ASN SER PRO PHE ASP GLY PRO GLY
SEQRES 7 A 169 GLY ASN LEU ALA HIS ALA PHE GLN PRO GLY PRO GLY ILE
SEQRES 8 A 169 GLY GLY ASP ALA HIS PHE ASP GLU ASP GLU ARG TRP THR
SEQRES 9 A 169 ASN ASN PHE ARG GLU TYR ASN LEU HIS ARG VAL ALA ALA
SEQRES 10 A 169 HIS GLU LEU GLY HIS SER LEU GLY LEU SER HIS SER THR
SEQRES 11 A 169 ASP ILE GLY ALA LEU MET TYR PRO SER TYR THR PHE SER
SEQRES 12 A 169 GLY ASP VAL GLN LEU ALA GLN ASP ASP ILE ASP GLY ILE
SEQRES 13 A 169 GLN ALA ILE TYR GLY ARG SER GLN ASN PRO VAL GLN PRO
HET ZN A 170 1
HET ZN A 171 1
HET CA A 172 1
HET CGS A 173 50
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CGS N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)
HETNAM 2 CGS AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE
HETSYN CGS CGS-27023A
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA CA 2+
FORMUL 5 CGS C18 H23 N3 O5 S
HELIX 1 1 ARG A 27 ASN A 43 1 17
HELIX 2 2 LEU A 112 SER A 123 1 12
HELIX 3 3 GLN A 150 ILE A 159 1 10
SHEET 1 A 5 THR A 48 LYS A 51 0
SHEET 2 A 5 HIS A 13 ILE A 18 1 N LEU A 14 O THR A 48
SHEET 3 A 5 ILE A 59 VAL A 64 1 N ILE A 59 O ARG A 17
SHEET 4 A 5 ALA A 95 ASP A 98 1 N ALA A 95 O SER A 62
SHEET 5 A 5 ALA A 82 ALA A 84 -1 N HIS A 83 O HIS A 96
LINK NE2 HIS A 68 ZN ZN A 171 1555 1555 2.02
LINK O PRO A 77 CA CA A 172 1555 1555 3.00
LINK O GLY A 78 CA CA A 172 1555 1555 3.00
LINK NE2 HIS A 83 ZN ZN A 171 1555 1555 2.21
LINK ND1 HIS A 96 ZN ZN A 171 1555 1555 1.99
LINK OD2 ASP A 98 CA CA A 172 1555 1555 2.99
LINK NE2 HIS A 118 ZN ZN A 170 1555 1555 2.15
LINK NE2 HIS A 122 ZN ZN A 170 1555 1555 2.07
LINK NE2 HIS A 128 ZN ZN A 170 1555 1555 1.97
LINK ZN ZN A 170 O47 CGS A 173 1555 1555 2.30
LINK ZN ZN A 170 O48 CGS A 173 1555 1555 2.08
LINK ZN ZN A 170 N35 CGS A 173 1555 1555 2.74
LINK CA CA A 172 O ASN A 80 1555 1555 3.20
LINK CA CA A 172 O GLY A 76 1555 1555 3.20
LINK CA CA A 172 OE2 GLU A 101 1555 1555 3.02
SITE 1 ZNA 3 HIS A 118 HIS A 122 HIS A 128
SITE 1 ZNB 3 HIS A 68 HIS A 83 HIS A 96
SITE 1 CAB 3 GLY A 76 GLY A 78 ASN A 80
SITE 1 CGS 12 ASN A 80 LEU A 81 ALA A 82 HIS A 83
SITE 2 CGS 12 ARG A 114 VAL A 115 HIS A 118 GLU A 119
SITE 3 CGS 12 LEU A 135 PRO A 138 TYR A 137 SER A 139
SITE 1 AC1 4 HIS A 118 HIS A 122 HIS A 128 CGS A 173
SITE 1 AC2 5 VAL A 64 HIS A 68 ASP A 70 HIS A 83
SITE 2 AC2 5 HIS A 96
SITE 1 AC3 7 GLY A 76 PRO A 77 GLY A 78 ASN A 80
SITE 2 AC3 7 LEU A 81 ASP A 98 GLU A 101
SITE 1 AC4 10 ASN A 80 LEU A 81 ALA A 82 HIS A 118
SITE 2 AC4 10 HIS A 122 HIS A 128 PRO A 138 SER A 139
SITE 3 AC4 10 TYR A 140 ZN A 170
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
Complete list - 30 20 Bytes