HEADER HYDROLASE (SERINE PROTEINASE) 21-OCT-87 1TRM
TITLE THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF
TITLE 2 ASP102 IN SERINE PROTEASE CATALYSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;
SOURCE 3 ORGANISM_COMMON: BLACK RAT;
SOURCE 4 ORGANISM_TAXID: 10117
KEYWDS HYDROLASE (SERINE PROTEINASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SPRANG,T.STANDING,R.J.FLETTERICK
REVDAT 5 29-NOV-17 1TRM 1 HELIX
REVDAT 4 24-FEB-09 1TRM 1 VERSN
REVDAT 3 01-APR-03 1TRM 1 JRNL
REVDAT 2 15-JUL-93 1TRM 1 REVDAT
REVDAT 1 16-JUL-88 1TRM 0
JRNL AUTH S.SPRANG,T.STANDING,R.J.FLETTERICK,R.M.STROUD,J.FINER-MOORE,
JRNL AUTH 2 N.H.XUONG,R.HAMLIN,W.J.RUTTER,C.S.CRAIK
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN:
JRNL TITL 2 ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS.
JRNL REF SCIENCE V. 237 905 1987
JRNL REFN ISSN 0036-8075
JRNL PMID 3112942
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.S.CRAIK,S.ROCZNIAK,C.LARGMAN,W.J.RUTTER
REMARK 1 TITL THE CATALYTIC ROLE OF THE ACTIVE SITE ASPARTIC ACID IN
REMARK 1 TITL 2 SERINE PROTEASES
REMARK 1 REF SCIENCE V. 237 909 1987
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 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 + TEST SET) : 0.160
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
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 230
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.030 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.050 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS:
REMARK 3 THE A AND B CONFORMATIONS OF THE RESIDUE HIS 57 IN BOTH
REMARK 3 CHAINS WERE OBSERVED IN DIFFERENCE MAPS AFTER REFINEMENT
REMARK 3 WITH THIS SIDE CHAIN OMITTED FROM THE MODEL. THE
REMARK 3 POSSIBILITY THAT ONE OF THE POSITIONS WOULD CORRESPOND TO
REMARK 3 AN ORDERED WATER MOLECULE WAS TESTED AND FOUND TO BE
REMARK 3 INCORRECT. THE RELATIVE OCCUPANCY OF THE TWO CONFORMATIONS
REMARK 3 WAS ESTIMATED BY COMPARING THE ELECTRON DENSITY AT
REMARK 3 POSITIONS WHERE THE TWO SIDE CHAINS DO NOT OVERLAP. THE
REMARK 3 OCCUPANCY OF THE TWO POSITIONS WAS NOT REFINED. THE B
REMARK 3 CONFORMATION CORRESPONDS TO THAT FOUND IN WILD TYPE
REMARK 3 TRYPSIN.
REMARK 4
REMARK 4 1TRM 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_1000176808.
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) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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) : 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) : 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 (%): 50.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
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 20.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.65000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.65000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.00000
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: DIMERIC
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 400
REMARK 400 COMPOUND
REMARK 400 THE CATALYTIC SITE, DIFFERS FROM THE CATALYTIC SITE OF NATIVE
REMARK 400 TRYPSIN BY REPLACEMENT OF ASP 102 WITH AN ASN. IN THE MUTANT, ND2
REMARK 400 ASN 102 IS A HYDROGEN BOND DONOR TO ND1 HIS 57. THIS HYDROGEN
REMARK 400 ARRANGEMENT PREVENTS HIS 57 FROM ACCEPTING A HYDROGEN BOND FROM SER
REMARK 400 195 AND RESULTS IN A LOSS OF NECLEOPHILICITY OF SER 195. THE MUTANT
REMARK 400 IS FOUR ORDERS OF MAGNITUDE LESS ACTIVE THAN NATIVE RAT TRYPSIN.
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 GLN A 239 CG CD OE1 NE2
REMARK 470 GLN B 239 CG CD OE1 NE2
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 HOH A 358 O HOH B 311 4466 0.28
REMARK 500 O HOH A 348 O HOH B 362 4566 0.60
REMARK 500 O HOH A 361 O HOH B 349 4466 0.89
REMARK 500 OE1 GLN B 23 NH2 ARG B 96 1655 1.07
REMARK 500 CD GLN B 23 NH2 ARG B 96 1655 1.34
REMARK 500 OE1 GLN A 23 NH2 ARG A 96 1655 1.39
REMARK 500 O HOH A 310 O HOH B 359 4566 1.44
REMARK 500 O HOH A 327 O HOH B 329 3546 1.51
REMARK 500 O HOH A 327 O HOH B 328 3546 1.58
REMARK 500 OE1 GLN A 23 CZ ARG A 96 1655 1.73
REMARK 500 OE1 GLN B 23 CZ ARG B 96 1655 1.73
REMARK 500 NE2 GLN B 23 NH2 ARG B 96 1655 1.77
REMARK 500 O HOH A 311 O HOH B 360 4566 1.78
REMARK 500 O HOH A 349 O HOH B 361 4566 1.83
REMARK 500 O HOH A 314 O HOH B 282 4566 1.93
REMARK 500 OD2 ASP A 236 O LEU B 114 4466 1.94
REMARK 500 CD GLN A 23 NH2 ARG A 96 1655 1.97
REMARK 500 O HOH A 360 O HOH B 350 4466 1.98
REMARK 500 OD1 ASP A 49 O HOH B 282 4566 2.01
REMARK 500 OE1 GLN A 23 NE ARG A 96 1655 2.05
REMARK 500 O HOH A 359 O HOH B 312 4466 2.10
REMARK 500 O HOH A 326 O HOH B 329 3546 2.11
REMARK 500 O LEU A 114 OD2 ASP B 236 4566 2.12
REMARK 500 OG SER A 147 O SER B 146 3546 2.17
REMARK 500 O HOH A 281 O HOH B 315 4466 2.18
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 SER A 45 CB SER A 45 OG -0.091
REMARK 500 TRP A 51 CE2 TRP A 51 CD2 0.085
REMARK 500 GLU A 70 CD GLU A 70 OE2 0.071
REMARK 500 GLU A 77 CD GLU A 77 OE2 0.078
REMARK 500 PRO A 111 CD PRO A 111 N 0.088
REMARK 500 PRO A 161 CD PRO A 161 N 0.099
REMARK 500 CYS A 182 CB CYS A 182 SG -0.097
REMARK 500 GLU A 186 CD GLU A 186 OE2 0.088
REMARK 500 GLU B 24 CD GLU B 24 OE2 0.071
REMARK 500 SER B 37 CA SER B 37 CB 0.095
REMARK 500 GLU B 151 CD GLU B 151 OE2 0.080
REMARK 500 PRO B 161 CD PRO B 161 N 0.093
REMARK 500 GLU B 169 CD GLU B 169 OE2 0.070
REMARK 500 GLU B 186 CD GLU B 186 OE2 0.081
REMARK 500 GLU B 204 CD GLU B 204 OE2 0.076
REMARK 500 ASN B 245 C ASN B 245 O 0.114
REMARK 500 ASN B 245 C ASN B 245 OXT 0.125
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 GLN A 23 CB - CG - CD ANGL. DEV. = 16.2 DEGREES
REMARK 500 GLU A 24 N - CA - CB ANGL. DEV. = 14.6 DEGREES
REMARK 500 GLU A 24 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 VAL A 27 CA - CB - CG2 ANGL. DEV. = 16.4 DEGREES
REMARK 500 GLN A 30 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 SER A 45 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 ASP A 49 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 HIS A 57 CA - CB - CG ANGL. DEV. = 12.2 DEGREES
REMARK 500 HIS A 57 O - C - N ANGL. DEV. = -12.6 DEGREES
REMARK 500 LYS A 60 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG A 62 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 65A NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ILE A 73 CG1 - CB - CG2 ANGL. DEV. = 14.7 DEGREES
REMARK 500 ILE A 73 CA - CB - CG2 ANGL. DEV. = 13.1 DEGREES
REMARK 500 GLU A 77 CG - CD - OE1 ANGL. DEV. = 13.5 DEGREES
REMARK 500 GLU A 77 CG - CD - OE2 ANGL. DEV. = -16.8 DEGREES
REMARK 500 GLU A 80 OE1 - CD - OE2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 PHE A 82 CB - CG - CD2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 VAL A 83 CG1 - CB - CG2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 PHE A 94 CB - CG - CD2 ANGL. DEV. = -11.0 DEGREES
REMARK 500 PHE A 94 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ASP A 95 CB - CG - OD1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ASP A 95 CB - CG - OD2 ANGL. DEV. = -12.1 DEGREES
REMARK 500 ARG A 96 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 96 CD - NE - CZ ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU A 99 CB - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 ASN A 102 CB - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 MET A 104 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 PRO A 124 C - N - CD ANGL. DEV. = -15.4 DEGREES
REMARK 500 PRO A 124 CA - N - CD ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO A 124 N - CA - CB ANGL. DEV. = -10.6 DEGREES
REMARK 500 SER A 127 CB - CA - C ANGL. DEV. = -11.8 DEGREES
REMARK 500 THR A 144 CA - CB - CG2 ANGL. DEV. = 12.6 DEGREES
REMARK 500 SER A 146 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 SER A 147 O - C - N ANGL. DEV. = -10.6 DEGREES
REMARK 500 ASP A 153 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 PRO A 161 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 TYR A 172 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 LYS A 175 CB - CA - C ANGL. DEV. = 15.8 DEGREES
REMARK 500 ILE A 176 CB - CG1 - CD1 ANGL. DEV. = 17.3 DEGREES
REMARK 500 ASP A 178 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 VAL A 181 CG1 - CB - CG2 ANGL. DEV. = -13.1 DEGREES
REMARK 500 LEU A 185 CB - CG - CD1 ANGL. DEV. = 12.6 DEGREES
REMARK 500 GLU A 186 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASP A 189 CB - CG - OD1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASP A 194 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 GLY A 203 C - N - CA ANGL. DEV. = 13.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 131 ANGLE DEVIATIONS.
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 SER A 54 -146.74 -151.64
REMARK 500 HIS A 71 -67.27 -136.04
REMARK 500 ASN A 150 96.47 -160.87
REMARK 500 PRO A 173 104.06 -32.06
REMARK 500 ASN A 202 73.85 47.33
REMARK 500 ILE A 238 -72.03 -39.89
REMARK 500 ASN B 25 13.72 57.06
REMARK 500 HIS B 71 -69.39 -136.42
REMARK 500 PHE B 94 108.88 -44.54
REMARK 500 ASN B 150 105.16 -160.23
REMARK 500 VAL B 235 -36.72 -20.37
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 65A 0.10 SIDE CHAIN
REMARK 500 ARG B 62 0.08 SIDE CHAIN
REMARK 500 ARG B 96 0.18 SIDE CHAIN
REMARK 500 ARG B 117 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 114 10.40
REMARK 500 MET B 104 -19.87
REMARK 500 VAL B 112 -13.64
REMARK 500 TYR B 234 11.82
REMARK 500 ILE B 238 13.75
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 CA A 247 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 81.3
REMARK 620 3 VAL A 75 O 161.7 82.2
REMARK 620 4 GLU A 80 OE2 105.2 173.2 91.6
REMARK 620 5 HOH A 271 O 77.6 102.8 98.3 81.0
REMARK 620 6 GLU A 77 OE1 91.3 76.4 92.6 101.0 168.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 247 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 72 O
REMARK 620 2 VAL B 75 O 83.4
REMARK 620 3 GLU B 80 OE2 169.1 86.7
REMARK 620 4 HOH B 272 O 98.7 87.2 76.3
REMARK 620 5 GLU B 77 OE1 98.6 102.2 87.9 161.2
REMARK 620 6 GLU B 70 OE1 91.0 166.0 97.6 81.0 91.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE IN CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE IN CHAIN B
REMARK 800
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 CA B 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 246
DBREF 1TRM A 16 245 UNP P00763 TRY2_RAT 24 246
DBREF 1TRM B 16 245 UNP P00763 TRY2_RAT 24 246
SEQADV 1TRM ASN A 102 UNP P00763 ASP 107 CONFLICT
SEQADV 1TRM ASN B 102 UNP P00763 ASP 107 CONFLICT
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER 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 ASP GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL
SEQRES 6 A 223 ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG
SEQRES 7 A 223 LYS THR LEU ASN ASN ASN ILE MET LEU ILE LYS LEU SER
SEQRES 8 A 223 SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA
SEQRES 9 A 223 LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN
SEQRES 11 A 223 GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU
SEQRES 12 A 223 PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE
SEQRES 13 A 223 THR ASP ASN MET VAL CYS VAL GLY PHE 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 ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR
SEQRES 16 A 223 GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA
SEQRES 18 A 223 ALA ASN
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 ASN 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 ASN THR LEU SER SER GLY VAL ASN
SEQRES 11 B 223 GLU 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 A 247 1
HET BEN A 246 9
HET CA B 247 1
HET BEN B 246 9
HETNAM CA CALCIUM ION
HETNAM BEN BENZAMIDINE
FORMUL 3 CA 2(CA 2+)
FORMUL 4 BEN 2(C7 H8 N2)
FORMUL 7 HOH *230(H2 O)
HELIX 1 SHA PRO A 164 TYR A 172 1IRREGULAR AFTER CYS 168 9
HELIX 2 31A LYS A 230 VAL A 235 5LEADS INTO TERMINAL ALPHA-HLX 6
HELIX 3 TEA TYR A 234 ASN A 245 1C-TERMINAL HELIX 12
HELIX 4 SHB PRO B 164 TYR B 172 1IRREGULAR AFTER CYS 168 9
HELIX 5 31B LYS B 230 VAL B 235 5LEADS INTO TERMINAL ALPHA-HLX 6
HELIX 6 TEB TYR B 234 ASN B 245 1C-TERMINAL HELIX 12
SHEET 1 S1A 7 TYR A 20 TYR A 20 0
SHEET 2 S1A 7 GLN A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 S1A 7 CYS A 136 GLY A 140 -1 O CYS A 136 N ALA A 160
SHEET 4 S1A 7 GLY A 197 CYS A 201 -1 N VAL A 200 O LEU A 137
SHEET 5 S1A 7 GLU A 204 TRP A 215 -1 N VAL A 213 O GLY A 197
SHEET 6 S1A 7 GLY A 226 VAL A 231 -1 N VAL A 227 O TRP A 215
SHEET 7 S1A 7 ASN A 179 VAL A 183 -1 N VAL A 183 O GLY A 226
SHEET 1 S2A 4 GLY A 43 SER A 45 0
SHEET 2 S2A 4 VAL A 52 ALA A 55 -1 N VAL A 53 O SER A 45
SHEET 3 S2A 4 ILE A 103 LYS A 107 -1 O MET A 104 N SER A 54
SHEET 4 S2A 4 LYS A 87 HIS A 91 -1 N HIS A 91 O ILE A 103
SHEET 1 S3A 2 ILE A 63 LEU A 66 0
SHEET 2 S3A 2 GLN A 81 ALA A 85 -1 N GLN A 81 O LEU A 66
SHEET 1 S1B 7 TYR B 20 TYR B 20 0
SHEET 2 S1B 7 GLN B 156 PRO B 161 -1 O CYS B 157 N TYR B 20
SHEET 3 S1B 7 CYS B 136 GLY B 140 -1 O CYS B 136 N ALA B 160
SHEET 4 S1B 7 GLY B 197 CYS B 201 -1 N VAL B 200 O LEU B 137
SHEET 5 S1B 7 GLU B 204 TRP B 215 -1 N VAL B 213 O GLY B 197
SHEET 6 S1B 7 GLY B 226 VAL B 231 -1 N VAL B 227 O TRP B 215
SHEET 7 S1B 7 ASN B 179 VAL B 183 -1 N VAL B 183 O GLY B 226
SHEET 1 S2B 4 GLY B 43 SER B 45 0
SHEET 2 S2B 4 VAL B 52 ALA B 55 -1 N VAL B 53 O SER B 45
SHEET 3 S2B 4 ILE B 103 LYS B 107 -1 O MET B 104 N SER B 54
SHEET 4 S2B 4 LYS B 87 HIS B 91 -1 N HIS B 91 O ILE B 103
SHEET 1 S3B 2 ILE B 63 LEU B 66 0
SHEET 2 S3B 2 GLN B 81 ALA B 85 -1 N GLN B 81 O LEU B 66
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.00
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.00
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.06
SSBOND 4 CYS A 136 CYS A 201 1555 1555 1.97
SSBOND 5 CYS A 168 CYS A 182 1555 1555 1.96
SSBOND 6 CYS A 191 CYS A 220 1555 1555 1.94
SSBOND 7 CYS B 22 CYS B 157 1555 1555 1.95
SSBOND 8 CYS B 42 CYS B 58 1555 1555 2.02
SSBOND 9 CYS B 128 CYS B 232 1555 1555 2.06
SSBOND 10 CYS B 136 CYS B 201 1555 1555 2.00
SSBOND 11 CYS B 168 CYS B 182 1555 1555 1.95
SSBOND 12 CYS B 191 CYS B 220 1555 1555 1.99
LINK CA CA A 247 OE1 GLU A 70 1555 1555 2.15
LINK CA CA A 247 O ASN A 72 1555 1555 2.37
LINK CA CA A 247 O VAL A 75 1555 1555 2.41
LINK CA CA A 247 OE2 GLU A 80 1555 1555 2.53
LINK CA CA A 247 O HOH A 271 1555 1555 2.38
LINK CA CA A 247 OE1 GLU A 77 1555 1555 2.00
LINK CA CA B 247 O ASN B 72 1555 1555 2.32
LINK CA CA B 247 O VAL B 75 1555 1555 2.31
LINK CA CA B 247 OE2 GLU B 80 1555 1555 2.48
LINK CA CA B 247 O HOH B 272 1555 1555 2.03
LINK CA CA B 247 OE1 GLU B 77 1555 1555 1.83
LINK CA CA B 247 OE1 GLU B 70 1555 1555 2.33
SITE 1 CTA 3 HIS A 57 ASN A 102 SER A 195
SITE 1 CTB 3 HIS B 57 ASN B 102 SER B 195
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 77
SITE 2 AC1 6 GLU A 80 HOH A 271
SITE 1 AC2 6 GLU B 70 ASN B 72 VAL B 75 GLU B 77
SITE 2 AC2 6 GLU B 80 HOH B 272
SITE 1 AC3 8 ASP A 189 SER A 190 GLN A 192 SER A 195
SITE 2 AC3 8 TRP A 215 GLY A 216 GLY A 219 GLY A 226
SITE 1 AC4 9 ASP B 189 SER B 190 GLN B 192 SER B 195
SITE 2 AC4 9 VAL B 213 GLY B 216 GLY B 219 CYS B 220
SITE 3 AC4 9 GLY B 226
CRYST1 40.400 92.000 127.300 90.00 90.00 90.00 P 21 21 21 8
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 0.024752 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010870 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007855 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
