HEADER HYDROLASE/HYDROLASE INHIBITOR 21-JUL-99 1C1R
TITLE RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE
TITLE 2 PROTEASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.4;
COMPND 5 OTHER_DETAILS: COMPLEXED WITH (5-AMIDINO-2-BENZIMIDAZOLYL)(2-
COMPND 6 BENZIMIDAZOLYL)METHANE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS ZN(II)-MEDIATED SERINE PROTEASE INHIBITORS, PH DEPENDENCE, ZN(II)
KEYWDS 2 AFFINITY STUCTURE-BASED DRUG DESIGN, SERINE PROTEASE SERINE
KEYWDS 3 PROTEASE/INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.KATZ,C.LUONG
REVDAT 7 27-DEC-23 1C1R 1 REMARK LINK
REVDAT 6 04-OCT-17 1C1R 1 REMARK
REVDAT 5 13-JUL-11 1C1R 1 VERSN
REVDAT 4 02-MAR-10 1C1R 1 REMARK HETATM
REVDAT 3 24-FEB-09 1C1R 1 VERSN
REVDAT 2 26-SEP-01 1C1R 3 ATOM
REVDAT 1 26-JUL-00 1C1R 0
JRNL AUTH B.A.KATZ,J.M.CLARK,J.S.FINER-MOORE,T.E.JENKINS,C.R.JOHNSON,
JRNL AUTH 2 M.J.ROSS,C.LUONG,W.R.MOORE,R.M.STROUD
JRNL TITL DESIGN OF POTENT SELECTIVE ZINC-MEDIATED SERINE PROTEASE
JRNL TITL 2 INHIBITORS.
JRNL REF NATURE V. 391 608 1998
JRNL REFN ISSN 0028-0836
JRNL PMID 9468142
JRNL DOI 10.1038/35422
REMARK 2
REMARK 2 RESOLUTION. 1.37 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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.800
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.0
REMARK 3 NUMBER OF REFLECTIONS : 33584
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : X-PLOR
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3341
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 36.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1623
REMARK 3 BIN R VALUE (WORKING SET) : 0.3910
REMARK 3 BIN FREE R VALUE : 0.3920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 180
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 : 1629
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 216
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) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 3.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.550
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 : PARMALLH3X_TR1706ZN.PRO
REMARK 3 PARAMETER FILE 2 : PARAM11_UCSF.WAT
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPALLH6X_TR1706ZN.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT TERMS INCLUDED IN FOB FILE
REMARK 3 CREATED WITH STANDARD X-PLOR SCRIPT.
REMARK 4
REMARK 4 1C1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000001264.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 8.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
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 : MSC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BIOTEX (MSC)
REMARK 200 DATA SCALING SOFTWARE : BIOTEX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34542
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330
REMARK 200 RESOLUTION RANGE LOW (A) : 28.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 36.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER PLUS
REMARK 200 REFINEMENT
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 (%): 18.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRYPSIN-BENZAMIDINE, P3(1) 2 1 WERE
REMARK 280 GROWN BY VAPOR DIFFUSION, AS DESCRIBED FOR P2(1) 2(1) 2(1)
REMARK 280 (LARGE CELL) (MANGEL, ET AL., BIOCHEMISTRY 29, 8351-8357, 1990)
REMARK 280 THE CRYSTAL WAS SOAKED IN A SOLUTION OF 0.24 M TRIS, 1.90 M
REMARK 280 MGSO4 . 7 H2O, 5.0 MM ZNSO4 . 7 H2O, PH 8.20 SATURATED IN HEMI-
REMARK 280 BABIM OVER A PERIOD OF SEVERAL DAYS WITH SEVERAL REPLACEMENTS OF
REMARK 280 THE SOAKING SOLUTION.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.59667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.19333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 73.19333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.59667
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 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 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 A 804 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 HIS40 AND HIS91 ARE MONOPROTONATED ON THE EPSILON NITROGEN.
REMARK 400 HIS57 IS MONOPROTONATED ON THE DELTA NITROGEN.
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 OH TYR A 94 H2 HOH A 314 1.56
REMARK 500 O GLN A 175 H2 HOH A 282 1.58
REMARK 500 OE1 GLN A 210 H1 HOH A 301 1.58
REMARK 500 O ARG A 117 H1 HOH A 258 1.60
REMARK 500 O HOH A 299 O HOH A 479 2.12
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 GLY A 216 H1 HOH A 753 2655 1.54
REMARK 500 O ASN A 74 H1 HOH A 321 5665 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 40 NE2 HIS A 40 CD2 -0.075
REMARK 500 HIS A 91 NE2 HIS A 91 CD2 -0.073
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 TRP A 51 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 TRP A 51 NE1 - CE2 - CZ2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TRP A 141 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP A 141 CD1 - NE1 - CE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 TRP A 141 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 TRP A 141 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 VAL A 199 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 TRP A 215 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 215 CD1 - NE1 - CE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 TRP A 215 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TYR A 228 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TRP A 237 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 237 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP A 237 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 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 ASP A 71 -74.98 -136.70
REMARK 500 SER A 195 130.21 -35.33
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 ARG A 66 0.09 SIDE CHAIN
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 MG A 263 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 30 OE1
REMARK 620 2 SER A 139 O 88.6
REMARK 620 3 ASP A 194 O 150.3 110.4
REMARK 620 4 HOH A 250 O 91.5 119.8 97.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 409 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 57 NE2
REMARK 620 2 SER A 195 OG 105.0
REMARK 620 3 BAI A 246 N3 128.2 111.5
REMARK 620 4 BAI A 246 N4' 116.0 109.7 84.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 247 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 88.2
REMARK 620 3 VAL A 75 O 170.6 92.1
REMARK 620 4 GLU A 80 OE2 92.4 165.5 89.6
REMARK 620 5 HOH A 271 O 84.0 104.8 86.9 89.7
REMARK 620 6 HOH A 309 O 83.0 91.5 106.4 74.2 158.8
REMARK 620 N 1 2 3 4 5
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 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BAI A 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 333
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C2D RELATED DB: PDB
REMARK 900 RELATED ID: 1C2F RELATED DB: PDB
REMARK 900 RELATED ID: 1C2G RELATED DB: PDB
REMARK 900 RELATED ID: 1C2H RELATED DB: PDB
REMARK 900 RELATED ID: 1C2I RELATED DB: PDB
REMARK 900 RELATED ID: 1C2L RELATED DB: PDB
REMARK 900 RELATED ID: 1C2M RELATED DB: PDB
REMARK 900 RELATED ID: 1C1N RELATED DB: PDB
REMARK 900 RELATED ID: 1C1O RELATED DB: PDB
REMARK 900 RELATED ID: 1C1P RELATED DB: PDB
REMARK 900 RELATED ID: 1C1Q RELATED DB: PDB
REMARK 900 RELATED ID: 1C2E RELATED DB: PDB
REMARK 900 RELATED ID: 1C1S RELATED DB: PDB
REMARK 900 RELATED ID: 1C1T RELATED DB: PDB
REMARK 900 RELATED ID: 1C1U RELATED DB: PDB
REMARK 900 RELATED ID: 1C1V RELATED DB: PDB
REMARK 900 RELATED ID: 1C1W RELATED DB: PDB
REMARK 900 RELATED ID: 1C2J RELATED DB: PDB
DBREF 1C1R A 16 245 UNP P00760 TRY1_BOVIN 21 243
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
HET CA A 247 1
HET MG A 263 1
HET SO4 A 355 5
HET ZN A 409 1
HET BAI A 246 37
HET DMS A 333 10
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETNAM BAI (5-AMIDINO-2-BENZIMIDAZOLYL)(2-BENZIMIDAZOLYL)METHANE
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN BAI HEMI-BABIM
FORMUL 2 CA CA 2+
FORMUL 3 MG MG 2+
FORMUL 4 SO4 O4 S 2-
FORMUL 5 ZN ZN 2+
FORMUL 6 BAI C16 H14 N6
FORMUL 7 DMS C2 H6 O S
FORMUL 8 HOH *216(H2 O)
HELIX 1 1 ALA A 55 TYR A 59 5 5
HELIX 2 2 SER A 164 TYR A 172 1 9
HELIX 3 3 TYR A 234 SER A 244 1 11
SHEET 1 A 7 TYR A 20 THR A 21 0
SHEET 2 A 7 LYS A 156 PRO A 161 -1 N CYS A 157 O TYR A 20
SHEET 3 A 7 GLN A 135 GLY A 140 -1 N CYS A 136 O ALA A 160
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O PRO A 198 N SER A 139
SHEET 5 A 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 A 7 GLY A 226 LYS A 230 -1 N VAL A 227 O TRP A 215
SHEET 7 A 7 MET A 180 ALA A 183 -1 O PHE A 181 N TYR A 228
SHEET 1 B 7 GLN A 30 ASN A 34 0
SHEET 2 B 7 HIS A 40 ASN A 48 -1 N PHE A 41 O LEU A 33
SHEET 3 B 7 GLN A 30 ASN A 34 -1 N VAL A 31 O GLY A 44
SHEET 4 B 7 GLN A 64 LEU A 67 -1 O GLN A 64 N ASN A 34
SHEET 5 B 7 GLN A 81 VAL A 90 -1 O GLN A 81 N LEU A 67
SHEET 6 B 7 MET A 104 LEU A 108 -1 O LEU A 105 N ILE A 89
SHEET 7 B 7 TRP A 51 SER A 54 -1 O VAL A 52 N ILE A 106
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.04
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.02
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.02
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.03
LINK OE1 GLN A 30 MG MG A 263 1555 1555 3.07
LINK NE2 HIS A 57 ZN ZN A 409 1555 1555 2.30
LINK OE1 GLU A 70 CA CA A 247 1555 1555 2.35
LINK O ASN A 72 CA CA A 247 1555 1555 2.21
LINK O VAL A 75 CA CA A 247 1555 1555 2.14
LINK OE2 GLU A 80 CA CA A 247 1555 1555 2.43
LINK O SER A 139 MG MG A 263 1555 1555 2.75
LINK O ASP A 194 MG MG A 263 1555 1555 2.82
LINK OG SER A 195 ZN ZN A 409 1555 1555 2.31
LINK N3 BAI A 246 ZN ZN A 409 1555 1555 2.34
LINK N4' BAI A 246 ZN ZN A 409 1555 1555 2.25
LINK CA CA A 247 O HOH A 271 1555 1555 2.35
LINK CA CA A 247 O HOH A 309 1555 1555 2.34
LINK O HOH A 250 MG MG A 263 1555 1555 2.97
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 HOH A 271 HOH A 309
SITE 1 AC2 6 GLN A 30 SER A 139 GLY A 140 ASP A 194
SITE 2 AC2 6 GLY A 197 HOH A 250
SITE 1 AC3 5 TYR A 20 SER A 116 ARG A 117 CYS A 157
SITE 2 AC3 5 LYS A 159
SITE 1 AC4 3 HIS A 57 SER A 195 BAI A 246
SITE 1 AC5 13 PHE A 41 ASP A 189 SER A 190 SER A 195
SITE 2 AC5 13 SER A 214 TRP A 215 GLY A 219 CYS A 220
SITE 3 AC5 13 GLY A 226 HOH A 325 HOH A 337 ZN A 409
SITE 4 AC5 13 HOH A 410
SITE 1 AC6 5 ASN A 97 THR A 98 SER A 127 GLN A 175
SITE 2 AC6 5 TRP A 215
CRYST1 54.860 54.860 109.790 90.00 90.00 120.00 P 31 2 1 6
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 0.018228 0.010524 0.000000 0.00000
SCALE2 0.000000 0.021048 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009108 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
