HEADER HYDROLASE/HYDROLASE INHIBITOR 11-MAR-96 1JAQ
TITLE COMPLEX OF 1-HYDROXYLAMINE-2-ISOBUTYLMALONYL-ALA-GLY-NH2 WITH THE
TITLE 2 CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATRIX METALLO PROTEINASE-8 (MET80 FORM);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 80 - 242;
COMPND 5 SYNONYM: MMP-8-MET80 FORM;
COMPND 6 EC: 3.4.24.34;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: MMP-8 IS IDENTICAL TO THE HUMAN NEUTROPHIL COLLAGENASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: NEUTROPHILS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS METALLOPROTEASE, ZINC-ENDOPEPTIDASE, METZINCINS, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.GRAMS,P.REINEMER,J.C.POWERS,T.KLEINE,M.PIPER,H.TSCHESCHE,R.HUBER,
AUTHOR 2 W.BODE
REVDAT 4 07-FEB-24 1JAQ 1 REMARK LINK
REVDAT 3 13-JUL-11 1JAQ 1 VERSN
REVDAT 2 24-FEB-09 1JAQ 1 VERSN
REVDAT 1 11-JUL-96 1JAQ 0
JRNL AUTH F.GRAMS,P.REINEMER,J.C.POWERS,T.KLEINE,M.PIEPER,H.TSCHESCHE,
JRNL AUTH 2 R.HUBER,W.BODE
JRNL TITL X-RAY STRUCTURES OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED
JRNL TITL 2 WITH PEPTIDE HYDROXAMATE AND PEPTIDE THIOL INHIBITORS.
JRNL TITL 3 IMPLICATIONS FOR SUBSTRATE BINDING AND RATIONAL DRUG DESIGN.
JRNL REF EUR.J.BIOCHEM. V. 228 830 1995
JRNL REFN ISSN 0014-2956
JRNL PMID 7737183
JRNL DOI 10.1111/J.1432-1033.1995.TB20329.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.BODE,P.REINEMER,R.HUBER,T.KLEINE,S.SCHNIERER,H.TSCHESCHE
REMARK 1 TITL THE X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN
REMARK 1 TITL 2 NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE ANALOGUE
REMARK 1 TITL 3 REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY
REMARK 1 REF EMBO J. V. 13 1263 1994
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.REINEMER,F.GRAMS,R.HUBER,T.KLEINE,S.SCHNIERER,M.PIPER,
REMARK 1 AUTH 2 H.TSCHESCHE,W.BODE
REMARK 1 TITL STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N TERMINUS IN
REMARK 1 TITL 2 THE 'SUPERACTIVATION' OF COLLAGENASES. A CRYSTALLOGRAPHIC
REMARK 1 TITL 3 STUDY
REMARK 1 REF FEBS LETT. V. 338 227 1994
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 7202
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1249
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.022
REMARK 3 BOND ANGLES (DEGREES) : 2.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, CCP4
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 16.56500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.15500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.68500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.15500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.56500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.68500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 80
REMARK 465 LEU A 81
REMARK 465 THR A 82
REMARK 465 PRO A 83
REMARK 465 GLY A 84
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HOH A 1019 H1 HOH A 1035 1.51
REMARK 500 O HOH A 1008 H2 HOH A 1087 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ASN A 188 O HOH A 1049 4566 1.12
REMARK 500 O ASN A 188 H2 HOH A 1049 4566 1.27
REMARK 500 HG1 THR A 129 HD21 ASN A 218 1455 1.33
REMARK 500 O HOH A 1009 H1 HOH A 1088 4466 1.54
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 PRO A 102 C - N - CA ANGL. DEV. = 9.2 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 GLU A 89 33.90 -99.30
REMARK 500 ARG A 145 -114.40 41.20
REMARK 500 PRO A 156 152.47 -47.80
REMARK 500 ASN A 157 -154.97 49.56
REMARK 500 THR A 185 -163.16 -106.28
REMARK 500 ALA A 206 -169.79 -104.41
REMARK 500 TYR A 241 -122.80 -110.07
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 999 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 01S A 1 OH
REMARK 620 2 HIS A 197 NE2 111.9
REMARK 620 3 HIS A 201 NE2 88.5 100.9
REMARK 620 4 HIS A 207 NE2 148.4 98.8 93.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 996 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 137 O
REMARK 620 2 GLY A 169 O 160.2
REMARK 620 3 GLY A 171 O 104.9 94.8
REMARK 620 4 ASP A 173 OD1 88.7 92.4 90.8
REMARK 620 5 HOH A1026 O 78.9 81.2 174.7 92.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 998 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 147 NE2
REMARK 620 2 ASP A 149 OD2 109.8
REMARK 620 3 HIS A 162 NE2 114.7 105.4
REMARK 620 4 HIS A 175 ND1 118.7 97.3 108.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 997 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 154 OD1
REMARK 620 2 GLY A 155 O 86.5
REMARK 620 3 ASN A 157 O 91.9 85.7
REMARK 620 4 ILE A 159 O 89.6 176.1 94.3
REMARK 620 5 ASP A 177 OD2 89.6 91.9 177.0 88.3
REMARK 620 6 GLU A 180 OE2 178.5 93.0 86.7 90.9 91.8
REMARK 620 N 1 2 3 4 5
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N-[(2R)-2-(HYDROXYCARBAMOYL)-4-METHYLPENTANOYL]-L-
REMARK 630 ALANYLGLYCINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 01S A 1
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: HMI ALA GLY NH2
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 996
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 01S A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JAO RELATED DB: PDB
DBREF 1JAQ A 80 242 UNP P22894 MM08_HUMAN 100 262
SEQRES 1 A 163 MET LEU THR PRO GLY ASN PRO LYS TRP GLU ARG THR ASN
SEQRES 2 A 163 LEU THR TYR ARG ILE ARG ASN TYR THR PRO GLN LEU SER
SEQRES 3 A 163 GLU ALA GLU VAL GLU ARG ALA ILE LYS ASP ALA PHE GLU
SEQRES 4 A 163 LEU TRP SER VAL ALA SER PRO LEU ILE PHE THR ARG ILE
SEQRES 5 A 163 SER GLN GLY GLU ALA ASP ILE ASN ILE ALA PHE TYR GLN
SEQRES 6 A 163 ARG ASP HIS GLY ASP ASN SER PRO PHE ASP GLY PRO ASN
SEQRES 7 A 163 GLY ILE LEU ALA HIS ALA PHE GLN PRO GLY GLN GLY ILE
SEQRES 8 A 163 GLY GLY ASP ALA HIS PHE ASP ALA GLU GLU THR TRP THR
SEQRES 9 A 163 ASN THR SER ALA ASN TYR ASN LEU PHE LEU VAL ALA ALA
SEQRES 10 A 163 HIS GLU PHE GLY HIS SER LEU GLY LEU ALA HIS SER SER
SEQRES 11 A 163 ASP PRO GLY ALA LEU MET TYR PRO ASN TYR ALA PHE ARG
SEQRES 12 A 163 GLU THR SER ASN TYR SER LEU PRO GLN ASP ASP ILE ASP
SEQRES 13 A 163 GLY ILE GLN ALA ILE TYR GLY
HET CA A 996 1
HET 01S A 1 27
HET CA A 997 1
HET ZN A 998 1
HET ZN A 999 1
HETNAM CA CALCIUM ION
HETNAM 01S N-[(2R)-2-(HYDROXYCARBAMOYL)-4-METHYLPENTANOYL]-L-
HETNAM 2 01S ALANYLGLYCINAMIDE
HETNAM ZN ZINC ION
FORMUL 2 CA 2(CA 2+)
FORMUL 3 01S C12 H22 N4 O5
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *89(H2 O)
HELIX 1 1 GLU A 106 ALA A 123 1 18
HELIX 2 2 LEU A 191 SER A 202 1 12
HELIX 3 3 GLN A 231 ILE A 240 1 10
SHEET 1 A 5 ILE A 127 ARG A 130 0
SHEET 2 A 5 ASN A 92 ILE A 97 1 N LEU A 93 O ILE A 127
SHEET 3 A 5 ILE A 138 TYR A 143 1 N ILE A 138 O ARG A 96
SHEET 4 A 5 ALA A 174 ASP A 177 1 N ALA A 174 O ALA A 141
SHEET 5 A 5 ALA A 161 ALA A 163 -1 N HIS A 162 O HIS A 175
LINK OH 01S A 1 ZN ZN A 999 1555 1555 2.10
LINK O ASP A 137 CA CA A 996 1555 1555 2.21
LINK NE2 HIS A 147 ZN ZN A 998 1555 1555 1.96
LINK OD2 ASP A 149 ZN ZN A 998 1555 1555 1.82
LINK OD1 ASP A 154 CA CA A 997 1555 1555 2.20
LINK O GLY A 155 CA CA A 997 1555 1555 2.36
LINK O ASN A 157 CA CA A 997 1555 1555 2.32
LINK O ILE A 159 CA CA A 997 1555 1555 2.32
LINK NE2 HIS A 162 ZN ZN A 998 1555 1555 2.19
LINK O GLY A 169 CA CA A 996 1555 1555 2.30
LINK O GLY A 171 CA CA A 996 1555 1555 2.34
LINK OD1 ASP A 173 CA CA A 996 1555 1555 2.60
LINK ND1 HIS A 175 ZN ZN A 998 1555 1555 2.26
LINK OD2 ASP A 177 CA CA A 997 1555 1555 2.65
LINK OE2 GLU A 180 CA CA A 997 1555 1555 2.16
LINK NE2 HIS A 197 ZN ZN A 999 1555 1555 1.87
LINK NE2 HIS A 201 ZN ZN A 999 1555 1555 2.27
LINK NE2 HIS A 207 ZN ZN A 999 1555 1555 2.05
LINK CA CA A 996 O HOH A1026 1555 1555 2.41
CISPEP 1 ASN A 188 TYR A 189 0 -0.42
SITE 1 AC1 5 ASP A 137 GLY A 169 GLY A 171 ASP A 173
SITE 2 AC1 5 HOH A1026
SITE 1 AC2 15 ILE A 159 LEU A 160 ALA A 161 HIS A 197
SITE 2 AC2 15 GLU A 198 HIS A 201 HIS A 207 TYR A 216
SITE 3 AC2 15 PRO A 217 ASN A 218 TYR A 219 ZN A 999
SITE 4 AC2 15 HOH A1020 HOH A1038 HOH A1076
SITE 1 AC3 6 ASP A 154 GLY A 155 ASN A 157 ILE A 159
SITE 2 AC3 6 ASP A 177 GLU A 180
SITE 1 AC4 4 HIS A 147 ASP A 149 HIS A 162 HIS A 175
SITE 1 AC5 4 01S A 1 HIS A 197 HIS A 201 HIS A 207
CRYST1 33.130 69.370 72.310 90.00 90.00 90.00 P 21 21 21 4
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 0.030184 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013829 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
