HEADER COMPLEX (SERINE PROTEASE/INHIBITOR) 07-FEB-96 1SLX
TITLE RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; ZINC-BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECOTIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRYPSIN INHIBITOR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ANIONIC TRYPSIN;
COMPND 9 CHAIN: B;
COMPND 10 EC: 3.4.21.4;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: RAT ANIONIC TRYPSIN;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTACTAC;
SOURCE 8 EXPRESSION_SYSTEM_GENE: ECOTIN;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 11 ORGANISM_COMMON: NORWAY RAT;
SOURCE 12 ORGANISM_TAXID: 10116;
SOURCE 13 GENE: RAT ANIONIC TRYPSIN;
SOURCE 14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PST;
SOURCE 18 EXPRESSION_SYSTEM_GENE: RAT ANIONIC TRYPSIN
KEYWDS SERINE PROTEASE, INHIBITOR, COMPLEX, METAL BINDING SITES, PROTEIN
KEYWDS 2 ENGINEERING, PROTEASE-SUBSTRATE INTERACTIONS, METALLOPROTEINS,
KEYWDS 3 COMPLEX (SERINE PROTEASE-INHIBITOR) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.S.BRINEN,R.J.FLETTERICK
REVDAT 3 13-JUL-11 1SLX 1 VERSN
REVDAT 2 24-FEB-09 1SLX 1 VERSN
REVDAT 1 11-JUL-96 1SLX 0
JRNL AUTH L.S.BRINEN,W.S.WILLETT,C.S.CRAIK,R.J.FLETTERICK
JRNL TITL X-RAY STRUCTURES OF A DESIGNED BINDING SITE IN TRYPSIN SHOW
JRNL TITL 2 METAL-DEPENDENT GEOMETRY.
JRNL REF BIOCHEMISTRY V. 35 5999 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8634241
JRNL DOI 10.1021/BI9530200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.E.MCGRATH,T.ERPEL,C.BYSTROFF,R.J.FLETTERICK
REMARK 1 TITL MACROMOLECULAR CHELATION AS AN IMPROVED MECHANISM OF
REMARK 1 TITL 2 PROTEASE INHIBITION: STRUCTURE OF THE ECOTIN-TRYPSIN COMPLEX
REMARK 1 REF EMBO J. V. 13 1502 1994
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.4
REMARK 3 NUMBER OF REFLECTIONS : 6230
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) : 0.173
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
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 : 2674
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.64
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) : 0.24
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.02
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.07
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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SLX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-94
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46301
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06500
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 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 42.99000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.14000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 42.99000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.14000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -3.11387
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 81.80075
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 284 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 SITE DIRECTED MUTAGENESIS WAS PERFORMED IN ORDER TO
REMARK 400 DESIGN A METAL BINDING SITE AT THE INTERFACE OF TRYPSIN
REMARK 400 N143H,E151H AND ECOTIN A86H. METAL BINDING TAKES PLACE
REMARK 400 AT THE SITE OF THESE MUTATIONS.
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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 GLN A 5
REMARK 465 PRO A 6
REMARK 465 LEU A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 GLY A 90
REMARK 465 LYS A 91
REMARK 465 LEU B 114
REMARK 465 ASN B 115
REMARK 465 ALA B 116
REMARK 465 ARG B 117
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 ILE A 10 CG1 CG2 CD1
REMARK 470 LYS A 18 CG CD CE NZ
REMARK 470 TYR B 39 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 145 CG CD1 CD2
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 N VAL A 24 O VAL A 140 2556 2.07
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 ALA A 11 -64.65 -147.88
REMARK 500 ASP A 49 -108.16 -78.43
REMARK 500 TRP A 67 -38.61 -130.99
REMARK 500 MET A 84 47.62 -82.98
REMARK 500 ALA A 104 22.01 -73.83
REMARK 500 GLU A 134 30.18 -80.16
REMARK 500 SER B 37 -61.70 -103.59
REMARK 500 TYR B 39 173.52 175.03
REMARK 500 ASP B 49 26.93 -75.63
REMARK 500 GLN B 50 2.27 -169.30
REMARK 500 HIS B 71 -55.40 -134.85
REMARK 500 ASN B 74 -71.09 -93.41
REMARK 500 GLU B 77 -16.23 -173.55
REMARK 500 GLU B 80 -79.89 -95.76
REMARK 500 GLN B 81 75.03 51.78
REMARK 500 PRO B 111 170.08 -53.09
REMARK 500 HIS B 143 132.15 -38.89
REMARK 500 LEU B 145 82.04 64.16
REMARK 500 SER B 146 -67.85 -143.12
REMARK 500 ASN B 150 76.52 31.88
REMARK 500 SER B 214 -78.73 -123.76
REMARK 500 LYS B 230 97.74 -69.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 254 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH B 272 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH B 282 DISTANCE = 5.05 ANGSTROMS
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 CA B 246 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 72 O
REMARK 620 2 ACT B 247 C 164.6
REMARK 620 3 ACT B 247 O 152.4 38.8
REMARK 620 4 ACT B 247 OXT 127.6 38.0 76.3
REMARK 620 5 VAL B 75 O 92.6 102.7 73.2 134.3
REMARK 620 6 HOH B 249 O 87.6 98.0 105.6 94.5 62.9
REMARK 620 7 GLU B 70 OE1 79.4 89.6 95.7 76.6 139.1 154.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 248 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 86 NE2
REMARK 620 2 HIS B 143 NE2 101.2
REMARK 620 3 HIS B 151 NE2 107.7 94.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: METAL (ZN) BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 248
DBREF 1SLX A 1 142 UNP P23827 ECOT_ECOLI 21 162
DBREF 1SLX B 16 245 UNP P00763 TRY2_RAT 24 246
SEQADV 1SLX HIS A 86 UNP P23827 ALA 106 ENGINEERED
SEQADV 1SLX HIS B 143 UNP P00763 ASN 146 ENGINEERED
SEQADV 1SLX HIS B 151 UNP P00763 GLU 154 ENGINEERED
SEQRES 1 A 142 ALA GLU SER VAL GLN PRO LEU GLU LYS ILE ALA PRO TYR
SEQRES 2 A 142 PRO GLN ALA GLU LYS GLY MET LYS ARG GLN VAL ILE GLN
SEQRES 3 A 142 LEU THR PRO GLN GLU ASP GLU SER THR LEU LYS VAL GLU
SEQRES 4 A 142 LEU LEU ILE GLY GLN THR LEU GLU VAL ASP CYS ASN LEU
SEQRES 5 A 142 HIS ARG LEU GLY GLY LYS LEU GLU ASN LYS THR LEU GLU
SEQRES 6 A 142 GLY TRP GLY TYR ASP TYR TYR VAL PHE ASP LYS VAL SER
SEQRES 7 A 142 SER PRO VAL SER THR MET MET HIS CYS PRO ASP GLY LYS
SEQRES 8 A 142 LYS GLU LYS LYS PHE VAL THR ALA TYR LEU GLY ASP ALA
SEQRES 9 A 142 GLY MET LEU ARG TYR ASN SER LYS LEU PRO ILE VAL VAL
SEQRES 10 A 142 TYR THR PRO ASP ASN VAL ASP VAL LYS TYR ARG VAL TRP
SEQRES 11 A 142 LYS ALA GLU GLU LYS ILE ASP ASN ALA VAL VAL ARG
SEQRES 1 B 223 ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO
SEQRES 2 B 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 B 223 GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA
SEQRES 4 B 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 B 223 HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL
SEQRES 6 B 223 ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG
SEQRES 7 B 223 LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 B 223 SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA
SEQRES 9 B 223 LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU
SEQRES 10 B 223 ILE SER GLY TRP GLY HIS THR LEU SER SER GLY VAL ASN
SEQRES 11 B 223 HIS PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU
SEQRES 12 B 223 PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE
SEQRES 13 B 223 THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY
SEQRES 14 B 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 B 223 CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR
SEQRES 16 B 223 GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS
SEQRES 17 B 223 VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA
SEQRES 18 B 223 ALA ASN
HET CA B 246 1
HET ACT B 247 4
HET ZN B 248 1
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
FORMUL 3 CA CA 2+
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 ZN ZN 2+
FORMUL 6 HOH *63(H2 O)
HELIX 1 1 GLU A 33 THR A 35 5 3
HELIX 2 2 GLY A 102 GLY A 105 5 4
HELIX 3 3 ALA B 56 CYS B 58 5 3
HELIX 4 4 GLN B 165 SER B 171 1 7
HELIX 5 5 VAL B 231 ASN B 233 5 3
HELIX 6 6 VAL B 235 ILE B 242 1 8
SHEET 1 A 4 MET A 20 ILE A 25 0
SHEET 2 A 4 ILE A 115 PRO A 120 -1 N THR A 119 O LYS A 21
SHEET 3 A 4 TYR A 69 ASP A 75 1 N TYR A 72 O VAL A 116
SHEET 4 A 4 LYS A 58 LEU A 64 -1 N LEU A 64 O TYR A 69
SHEET 1 B 3 ASP A 124 LYS A 131 0
SHEET 2 B 3 LEU A 36 GLY A 43 -1 N GLY A 43 O ASP A 124
SHEET 3 B 3 MET A 106 ARG A 108 -1 N LEU A 107 O VAL A 38
SHEET 1 C 2 GLY A 43 VAL A 48 0
SHEET 2 C 2 GLU A 93 THR A 98 -1 N VAL A 97 O GLN A 44
SHEET 1 D 7 PHE B 82 ASN B 84 0
SHEET 2 D 7 GLN B 64 ARG B 66 -1 N VAL B 65 O VAL B 83
SHEET 3 D 7 GLN B 30 ASN B 34 -1 N ASN B 34 O GLN B 64
SHEET 4 D 7 HIS B 40 ASN B 48 -1 N GLY B 44 O VAL B 31
SHEET 5 D 7 TRP B 51 SER B 54 -1 N VAL B 53 O SER B 45
SHEET 6 D 7 MET B 104 LEU B 108 -1 N ILE B 106 O VAL B 52
SHEET 7 D 7 ALA B 85 LYS B 90 -1 N ILE B 89 O LEU B 105
SHEET 1 E 2 GLN B 135 GLY B 140 0
SHEET 2 E 2 GLN B 156 PRO B 161 -1 N ALA B 160 O CYS B 136
SHEET 1 F 4 MET B 180 VAL B 183 0
SHEET 2 F 4 GLY B 226 THR B 229 -1 N TYR B 228 O VAL B 181
SHEET 3 F 4 GLU B 204 TRP B 215 -1 N TRP B 215 O VAL B 227
SHEET 4 F 4 PRO B 198 CYS B 201 -1 N CYS B 201 O GLU B 204
SSBOND 1 CYS A 50 CYS A 87 1555 1555 2.03
SSBOND 2 CYS B 22 CYS B 157 1555 1555 2.03
SSBOND 3 CYS B 42 CYS B 58 1555 1555 2.03
SSBOND 4 CYS B 128 CYS B 232 1555 1555 2.03
SSBOND 5 CYS B 136 CYS B 201 1555 1555 2.03
SSBOND 6 CYS B 168 CYS B 182 1555 1555 2.03
SSBOND 7 CYS B 191 CYS B 220 1555 1555 2.03
LINK CA CA B 246 O ASN B 72 1555 1555 1.78
LINK CA CA B 246 C ACT B 247 1555 1555 1.97
LINK CA CA B 246 O ACT B 247 1555 1555 1.72
LINK CA CA B 246 OXT ACT B 247 1555 1555 1.83
LINK ZN ZN B 248 NE2 HIS A 86 1555 1555 2.10
LINK ZN ZN B 248 NE2 HIS B 143 1555 1555 2.30
LINK ZN ZN B 248 NE2 HIS B 151 1555 1555 1.87
LINK CA CA B 246 O VAL B 75 1555 1555 2.67
LINK CA CA B 246 O HOH B 249 1555 1555 1.73
LINK CA CA B 246 OE1 GLU B 70 1555 1555 2.47
SITE 1 ZN1 3 HIS A 86 HIS B 143 HIS B 151
SITE 1 AC1 6 GLU B 70 ASN B 72 VAL B 75 GLU B 77
SITE 2 AC1 6 ACT B 247 HOH B 249
SITE 1 AC2 9 GLU B 70 ASN B 72 VAL B 75 LEU B 76
SITE 2 AC2 9 GLU B 77 ASN B 79 GLU B 80 CA B 246
SITE 3 AC2 9 HOH B 249
SITE 1 AC3 3 HIS A 86 HIS B 143 HIS B 151
CRYST1 85.980 56.280 81.860 90.00 92.18 90.00 C 1 2 1 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 0.011631 0.000000 0.000443 0.00000
SCALE2 0.000000 0.017768 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012225 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
