HEADER HYDROLASE/HYDROLASE INHIBITOR 03-APR-98 1A86
TITLE MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MMP-8;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.24.34;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS COLLAGENASE, MATRIX METALLOPROTEINASE, MALONIC ACID, MMP8, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.BRANDSTETTER,E.G.V.ROEDERN,F.GRAMS,R.A.ENGH
REVDAT 4 07-FEB-24 1A86 1 REMARK LINK
REVDAT 3 13-JUL-11 1A86 1 VERSN
REVDAT 2 24-FEB-09 1A86 1 VERSN
REVDAT 1 04-MAY-99 1A86 0
JRNL AUTH H.BRANDSTETTER,R.A.ENGH,E.G.VON ROEDERN,L.MORODER,R.HUBER,
JRNL AUTH 2 W.BODE,F.GRAMS
JRNL TITL STRUCTURE OF MALONIC ACID-BASED INHIBITORS BOUND TO HUMAN
JRNL TITL 2 NEUTROPHIL COLLAGENASE. A NEW BINDING MODE EXPLAINS
JRNL TITL 3 APPARENTLY ANOMALOUS DATA.
JRNL REF PROTEIN SCI. V. 7 1303 1998
JRNL REFN ISSN 0961-8368
JRNL PMID 9655333
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
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 : NULL
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) : NULL
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 : 1247
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 0
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 1A86 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_1000170513.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-95
REMARK 200 TEMPERATURE (KELVIN) : 283
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) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
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 16.57000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.31000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.71500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.31000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.57000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.71500
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLY A 242 O
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 ARG A 145 -118.33 34.00
REMARK 500 HIS A 147 46.07 -148.43
REMARK 500 SER A 151 74.48 -154.95
REMARK 500 ASN A 157 -157.91 60.89
REMARK 500 THR A 185 -161.31 -126.53
REMARK 500 TYR A 241 -107.44 -107.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 0ZB A 1
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 0ZB A 1 O1
REMARK 620 2 HIS A 197 NE2 111.8
REMARK 620 3 HIS A 201 NE2 139.6 100.2
REMARK 620 4 HIS A 207 NE2 96.9 111.8 93.3
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 163.7
REMARK 620 3 GLY A 171 O 105.4 91.0
REMARK 620 4 ASP A 173 OD1 83.7 98.2 84.9
REMARK 620 N 1 2 3
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 109.2
REMARK 620 3 HIS A 162 NE2 113.9 111.7
REMARK 620 4 HIS A 175 ND1 113.2 97.1 110.6
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 95.0
REMARK 620 3 ASN A 157 O 94.1 89.4
REMARK 620 4 ILE A 159 O 79.4 173.9 93.6
REMARK 620 5 ASP A 177 OD2 89.4 87.7 175.6 89.6
REMARK 620 6 GLU A 180 OE2 173.5 91.3 84.8 94.3 91.9
REMARK 620 N 1 2 3 4 5
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N-BENZYL-N~2~-[(2R)-2-(HYDROXYCARBAMOYL)-4-
REMARK 630 METHYLPENTANOYL]-L-ALPHA-ASPARAGINE
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 0ZB A 1
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: HMI ASP ABN
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 0ZB A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 996
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
DBREF 1A86 A 85 242 UNP P22894 MM08_HUMAN 105 262
SEQRES 1 A 158 ASN PRO LYS TRP GLU ARG THR ASN LEU THR TYR ARG ILE
SEQRES 2 A 158 ARG ASN TYR THR PRO GLN LEU SER GLU ALA GLU VAL GLU
SEQRES 3 A 158 ARG ALA ILE LYS ASP ALA PHE GLU LEU TRP SER VAL ALA
SEQRES 4 A 158 SER PRO LEU ILE PHE THR ARG ILE SER GLN GLY GLU ALA
SEQRES 5 A 158 ASP ILE ASN ILE ALA PHE TYR GLN ARG ASP HIS GLY ASP
SEQRES 6 A 158 ASN SER PRO PHE ASP GLY PRO ASN GLY ILE LEU ALA HIS
SEQRES 7 A 158 ALA PHE GLN PRO GLY GLN GLY ILE GLY GLY ASP ALA HIS
SEQRES 8 A 158 PHE ASP ALA GLU GLU THR TRP THR ASN THR SER ALA ASN
SEQRES 9 A 158 TYR ASN LEU PHE LEU VAL ALA ALA HIS GLU PHE GLY HIS
SEQRES 10 A 158 SER LEU GLY LEU ALA HIS SER SER ASP PRO GLY ALA LEU
SEQRES 11 A 158 MET TYR PRO ASN TYR ALA PHE ARG GLU THR SER ASN TYR
SEQRES 12 A 158 SER LEU PRO GLN ASP ASP ILE ASP GLY ILE GLN ALA ILE
SEQRES 13 A 158 TYR GLY
HET 0ZB A 1 31
HET CA A 996 1
HET CA A 997 1
HET ZN A 998 1
HET ZN A 999 1
HETNAM 0ZB N-BENZYL-N~2~-[(2R)-2-(HYDROXYCARBAMOYL)-4-
HETNAM 2 0ZB METHYLPENTANOYL]-L-ALPHA-ASPARAGINE
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
FORMUL 2 0ZB C18 H25 N3 O6
FORMUL 3 CA 2(CA 2+)
FORMUL 5 ZN 2(ZN 2+)
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 O1 0ZB A 1 ZN ZN A 999 1555 1555 1.87
LINK O ASP A 137 CA CA A 996 1555 1555 2.25
LINK NE2 HIS A 147 ZN ZN A 998 1555 1555 2.11
LINK OD2 ASP A 149 ZN ZN A 998 1555 1555 1.98
LINK OD1 ASP A 154 CA CA A 997 1555 1555 2.52
LINK O GLY A 155 CA CA A 997 1555 1555 2.14
LINK O ASN A 157 CA CA A 997 1555 1555 2.21
LINK O ILE A 159 CA CA A 997 1555 1555 2.20
LINK NE2 HIS A 162 ZN ZN A 998 1555 1555 2.10
LINK O GLY A 169 CA CA A 996 1555 1555 2.14
LINK O GLY A 171 CA CA A 996 1555 1555 2.20
LINK OD1 ASP A 173 CA CA A 996 1555 1555 2.42
LINK ND1 HIS A 175 ZN ZN A 998 1555 1555 2.15
LINK OD2 ASP A 177 CA CA A 997 1555 1555 2.41
LINK OE2 GLU A 180 CA CA A 997 1555 1555 2.19
LINK NE2 HIS A 197 ZN ZN A 999 1555 1555 1.99
LINK NE2 HIS A 201 ZN ZN A 999 1555 1555 2.19
LINK NE2 HIS A 207 ZN ZN A 999 1555 1555 1.95
CISPEP 1 ASN A 188 TYR A 189 0 -0.80
SITE 1 AC1 14 THR A 129 ILE A 159 LEU A 160 ALA A 161
SITE 2 AC1 14 HIS A 197 GLU A 198 HIS A 201 HIS A 207
SITE 3 AC1 14 LEU A 214 TYR A 216 PRO A 217 ASN A 218
SITE 4 AC1 14 TYR A 219 ZN A 999
SITE 1 AC2 4 ASP A 137 GLY A 169 GLY A 171 ASP A 173
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 0ZB A 1 HIS A 197 HIS A 201 HIS A 207
CRYST1 33.140 69.430 72.620 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 0.030175 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013770 0.00000
(ATOM LINES ARE NOT SHOWN.)
END