HEADER HYDROLASE 22-JUL-11 3T2I
TITLE TETRAGONAL THERMOLYSIN IN THE PRESENCE OF SARCOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOLYSIN;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;
COMPND 5 EC: 3.4.24.27
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1427
KEYWDS ALPHA/BETA, ZINC PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CAHN,N.S.HTI LAR SENG,D.JUERS
REVDAT 4 13-SEP-23 3T2I 1 REMARK LINK
REVDAT 3 04-FEB-15 3T2I 1 HETATM
REVDAT 2 11-JAN-12 3T2I 1 JRNL
REVDAT 1 28-DEC-11 3T2I 0
JRNL AUTH H.MARSHALL,M.VENKAT,N.S.HTI LAR SENG,J.CAHN,D.H.JUERS
JRNL TITL THE USE OF TRIMETHYLAMINE N-OXIDE AS A PRIMARY PRECIPITATING
JRNL TITL 2 AGENT AND RELATED METHYLAMINE OSMOLYTES AS CRYOPROTECTIVE
JRNL TITL 3 AGENTS FOR MACROMOLECULAR CRYSTALLOGRAPHY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 68 69 2012
JRNL REFN ISSN 0907-4449
JRNL PMID 22194335
JRNL DOI 10.1107/S0907444911050360
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 28165
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1505
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2056
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 100
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2428
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27000
REMARK 3 B22 (A**2) : -0.27000
REMARK 3 B33 (A**2) : 0.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.144
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.419
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2508 ; 0.022 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3410 ; 1.735 ; 1.930
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 315 ; 5.896 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;34.136 ;24.435
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 352 ;12.943 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;24.254 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 363 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1990 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1569 ; 0.934 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2498 ; 1.625 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 939 ; 2.913 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 912 ; 4.407 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3T2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066954.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD ONYX CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.221
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : 0.59000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1L3F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MG/ML PROTEIN IN 45% DMSO, MIXING
REMARK 280 SOLUTION 45% DMSO, 1 M NACL, 1 M ZNCL2, 0.1 M MES PH 6.0, WELL
REMARK 280 30% SATURATED AMSO4, SOAK DONE IN 4 M SARCOSINE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 52.93750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.17300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.17300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.46875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.17300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.17300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.40625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.17300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.17300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.46875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.17300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.17300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.40625
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 52.93750
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: E
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 LYS E 316 CG CD CE NZ
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 CL CL E 324 O HOH E 499 1.70
REMARK 500 O HOH E 587 O HOH E 588 1.84
REMARK 500 NE2 HIS E 231 O HOH E 499 2.17
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 HOH E 471 O HOH E 579 5555 2.09
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 VAL E 256 CB VAL E 256 CG2 0.133
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 ARG E 47 NE - CZ - NH1 ANGL. DEV. = 3.5 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 THR E 26 -58.64 70.45
REMARK 500 SER E 92 -173.70 60.64
REMARK 500 SER E 107 -162.51 57.40
REMARK 500 ASN E 111 54.41 -92.29
REMARK 500 THR E 152 -97.95 -127.49
REMARK 500 ASN E 159 -142.02 56.78
REMARK 500 LYS E 182 -61.46 -93.93
REMARK 500 THR E 194 75.77 42.32
REMARK 500 ASP E 207 78.05 -150.61
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 E 319 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 57 OD1
REMARK 620 2 ASP E 57 OD2 52.2
REMARK 620 3 ASP E 59 OD1 124.7 72.6
REMARK 620 4 GLN E 61 O 94.6 91.1 89.6
REMARK 620 5 HOH E 447 O 80.4 130.6 153.1 78.0
REMARK 620 6 HOH E 463 O 158.8 147.9 75.5 91.8 81.2
REMARK 620 7 HOH E 467 O 86.8 89.3 89.1 178.5 102.9 87.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 317 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 138 OD2
REMARK 620 2 GLU E 177 OE1 81.0
REMARK 620 3 GLU E 177 OE2 130.2 49.3
REMARK 620 4 ASP E 185 OD1 159.9 118.9 69.6
REMARK 620 5 GLU E 187 O 83.3 150.6 141.5 79.9
REMARK 620 6 GLU E 190 OE1 86.4 126.9 118.1 79.0 76.4
REMARK 620 7 GLU E 190 OE2 102.0 80.1 70.1 79.9 127.7 52.5
REMARK 620 8 HOH E 414 O 98.8 81.9 79.8 87.9 76.1 151.2 149.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 321 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 142 NE2
REMARK 620 2 HIS E 146 NE2 105.1
REMARK 620 3 GLU E 166 OE2 121.9 94.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 318 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 177 OE2
REMARK 620 2 ASN E 183 O 93.9
REMARK 620 3 ASP E 185 OD2 89.8 90.1
REMARK 620 4 GLU E 190 OE2 93.1 172.7 91.8
REMARK 620 5 HOH E 421 O 92.5 85.4 175.1 92.4
REMARK 620 6 HOH E 457 O 174.4 80.7 92.0 92.2 85.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 320 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR E 193 O
REMARK 620 2 THR E 194 OG1 74.1
REMARK 620 3 THR E 194 O 73.0 64.0
REMARK 620 4 ILE E 197 O 155.6 102.8 83.8
REMARK 620 5 ASP E 200 OD1 123.1 77.0 131.8 78.2
REMARK 620 6 HOH E 422 O 86.8 125.9 154.4 113.0 72.4
REMARK 620 7 HOH E 462 O 93.4 150.7 87.2 77.6 130.5 78.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E 326 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR E 211 O
REMARK 620 2 HOH E 472 O 100.2
REMARK 620 3 HOH E 503 O 91.9 90.5
REMARK 620 4 HOH E 518 O 93.6 96.4 170.3
REMARK 620 5 HOH E 519 O 77.9 177.8 88.5 84.8
REMARK 620 6 HOH E 572 O 160.8 80.7 68.9 105.4 100.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 322 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 250 ND1
REMARK 620 2 HOH E 401 O 104.6
REMARK 620 3 HOH E 402 O 100.0 115.3
REMARK 620 4 HOH E 403 O 100.4 128.4 103.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAR E 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAR E 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAR E 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS E 2011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS E 2012
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3T25 RELATED DB: PDB
REMARK 900 TMAO-GROWN ORTHORHOMBIC TRYPSIN (BOVINE)
REMARK 900 RELATED ID: 3T26 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC TRYPSIN (BOVINE) IN THE PRESENCE OF SARCOSINE
REMARK 900 RELATED ID: 3T27 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC TRYPSIN (BOVINE) IN THE PRESENCE OF BETAINE
REMARK 900 RELATED ID: 3T28 RELATED DB: PDB
REMARK 900 TMAO-GROWN TRYPSIN (BOVINE)-PREVIOUSLY UNREPORTED TETRAGONAL
REMARK 900 CRYSTAL FORM
REMARK 900 RELATED ID: 3T29 RELATED DB: PDB
REMARK 900 TMAO-GROWN TRIGONAL TRYPSIN (BOVINE)
REMARK 900 RELATED ID: 3T2A RELATED DB: PDB
REMARK 900 TMAO-GROWN CUBIC INSULIN (PORCINE)
REMARK 900 RELATED ID: 3T2H RELATED DB: PDB
REMARK 900 TETRAGONAL THERMOLYSIN IN THE PRESENCE OF TMAO
REMARK 900 RELATED ID: 3T2J RELATED DB: PDB
REMARK 900 TETRAGONAL THERMOLYSIN IN THE PRESENCE OF BETAINE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N269D, Q351E CONFLICT IN UNP ENTRY P00800
DBREF 3T2I E 1 316 UNP P00800 THER_BACTH 233 548
SEQADV 3T2I ASP E 37 UNP P00800 ASN 269 SEE REMARK 999
SEQADV 3T2I GLU E 119 UNP P00800 GLN 351 SEE REMARK 999
SEQRES 1 E 316 ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES 2 E 316 LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES 3 E 316 TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE
SEQRES 4 E 316 PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES 5 E 316 SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES 6 E 316 TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES 7 E 316 VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES 8 E 316 SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES 9 E 316 HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES 10 E 316 SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES 11 E 316 ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES 12 E 316 LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES 13 E 316 TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES 14 E 316 ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES 15 E 316 ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES 16 E 316 GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES 17 E 316 ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES 18 E 316 THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES 19 E 316 GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES 20 E 316 GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES 21 E 316 ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES 22 E 316 TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES 23 E 316 ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES 24 E 316 SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES 25 E 316 VAL GLY VAL LYS
HET CA E 317 1
HET CA E 318 1
HET CA E 319 1
HET CA E 320 1
HET ZN E 321 1
HET ZN E 322 1
HET CL E 323 1
HET CL E 324 1
HET CL E 325 1
HET NA E 326 1
HET SAR E2001 6
HET SAR E2002 6
HET SAR E2003 6
HET DMS E2011 4
HET DMS E2012 4
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM SAR SARCOSINE
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 CA 4(CA 2+)
FORMUL 6 ZN 2(ZN 2+)
FORMUL 8 CL 3(CL 1-)
FORMUL 11 NA NA 1+
FORMUL 12 SAR 3(C3 H7 N O2)
FORMUL 15 DMS 2(C2 H6 O S)
FORMUL 17 HOH *194(H2 O)
HELIX 1 1 ALA E 64 TYR E 66 5 3
HELIX 2 2 ASP E 67 ASN E 89 1 23
HELIX 3 3 PRO E 132 GLY E 135 5 4
HELIX 4 4 GLY E 136 TYR E 151 1 16
HELIX 5 5 GLN E 158 ASN E 181 1 24
HELIX 6 6 ASP E 207 GLY E 212 5 6
HELIX 7 7 HIS E 216 ARG E 220 5 5
HELIX 8 8 THR E 224 VAL E 230 1 7
HELIX 9 9 ASN E 233 GLY E 247 1 15
HELIX 10 10 GLY E 259 TYR E 274 1 16
HELIX 11 11 ASN E 280 GLY E 297 1 18
HELIX 12 12 SER E 300 VAL E 313 1 14
SHEET 1 A 5 ALA E 56 ASP E 57 0
SHEET 2 A 5 TYR E 28 TYR E 29 -1 N TYR E 28 O ASP E 57
SHEET 3 A 5 GLN E 17 TYR E 24 -1 N THR E 23 O TYR E 29
SHEET 4 A 5 THR E 4 ARG E 11 -1 N THR E 4 O TYR E 24
SHEET 5 A 5 GLN E 61 PHE E 62 1 O PHE E 62 N VAL E 9
SHEET 1 B 3 GLN E 31 ASP E 32 0
SHEET 2 B 3 ILE E 39 ASP E 43 -1 O ILE E 39 N ASP E 32
SHEET 3 B 3 SER E 53 LEU E 54 -1 O SER E 53 N ASP E 43
SHEET 1 C 5 GLN E 31 ASP E 32 0
SHEET 2 C 5 ILE E 39 ASP E 43 -1 O ILE E 39 N ASP E 32
SHEET 3 C 5 ILE E 100 TYR E 106 1 O SER E 102 N TYR E 42
SHEET 4 C 5 MET E 120 GLY E 123 1 O MET E 120 N ARG E 101
SHEET 5 C 5 ALA E 113 TRP E 115 -1 N PHE E 114 O VAL E 121
SHEET 1 D 2 GLU E 187 ILE E 188 0
SHEET 2 D 2 ARG E 203 SER E 204 -1 O ARG E 203 N ILE E 188
SHEET 1 E 2 GLY E 248 HIS E 250 0
SHEET 2 E 2 VAL E 253 VAL E 255 -1 O VAL E 255 N GLY E 248
LINK OD1 ASP E 57 CA CA E 319 1555 1555 2.33
LINK OD2 ASP E 57 CA CA E 319 1555 1555 2.50
LINK OD1 ASP E 59 CA CA E 319 1555 1555 2.28
LINK O GLN E 61 CA CA E 319 1555 1555 2.29
LINK OD2 ASP E 138 CA CA E 317 1555 1555 2.39
LINK NE2 HIS E 142 ZN ZN E 321 1555 1555 2.04
LINK NE2 HIS E 146 ZN ZN E 321 1555 1555 2.03
LINK OE2 GLU E 166 ZN ZN E 321 1555 1555 1.92
LINK OE1 GLU E 177 CA CA E 317 1555 1555 2.45
LINK OE2 GLU E 177 CA CA E 317 1555 1555 2.72
LINK OE2 GLU E 177 CA CA E 318 1555 1555 2.25
LINK O ASN E 183 CA CA E 318 1555 1555 2.33
LINK OD1 ASP E 185 CA CA E 317 1555 1555 2.44
LINK OD2 ASP E 185 CA CA E 318 1555 1555 2.09
LINK O GLU E 187 CA CA E 317 1555 1555 2.27
LINK OE1 GLU E 190 CA CA E 317 1555 1555 2.47
LINK OE2 GLU E 190 CA CA E 317 1555 1555 2.57
LINK OE2 GLU E 190 CA CA E 318 1555 1555 1.93
LINK O TYR E 193 CA CA E 320 1555 1555 2.43
LINK OG1 THR E 194 CA CA E 320 1555 1555 2.35
LINK O THR E 194 CA CA E 320 1555 1555 2.38
LINK O ILE E 197 CA CA E 320 1555 1555 2.31
LINK OD1 ASP E 200 CA CA E 320 1555 1555 2.34
LINK O TYR E 211 NA NA E 326 1555 1555 2.52
LINK ND1 HIS E 250 ZN ZN E 322 1555 1555 2.22
LINK CA CA E 317 O HOH E 414 1555 1555 2.47
LINK CA CA E 318 O HOH E 421 1555 1555 2.01
LINK CA CA E 318 O HOH E 457 1555 1555 2.13
LINK CA CA E 319 O HOH E 447 1555 1555 2.31
LINK CA CA E 319 O HOH E 463 1555 1555 2.61
LINK CA CA E 319 O HOH E 467 1555 1555 2.29
LINK CA CA E 320 O HOH E 422 1555 1555 2.42
LINK CA CA E 320 O HOH E 462 1555 1555 2.13
LINK ZN ZN E 322 O HOH E 401 1555 1555 2.39
LINK ZN ZN E 322 O HOH E 402 1555 1555 2.66
LINK ZN ZN E 322 O HOH E 403 1555 1555 2.57
LINK NA NA E 326 O HOH E 472 1555 1555 2.37
LINK NA NA E 326 O HOH E 503 1555 1555 2.41
LINK NA NA E 326 O HOH E 518 1555 1555 2.27
LINK NA NA E 326 O HOH E 519 1555 1555 2.40
LINK NA NA E 326 O HOH E 572 1555 1555 2.57
CISPEP 1 LEU E 50 PRO E 51 0 6.98
SITE 1 AC1 7 ASP E 138 GLU E 177 ASP E 185 GLU E 187
SITE 2 AC1 7 GLU E 190 CA E 318 HOH E 414
SITE 1 AC2 7 GLU E 177 ASN E 183 ASP E 185 GLU E 190
SITE 2 AC2 7 CA E 317 HOH E 421 HOH E 457
SITE 1 AC3 6 ASP E 57 ASP E 59 GLN E 61 HOH E 447
SITE 2 AC3 6 HOH E 463 HOH E 467
SITE 1 AC4 6 TYR E 193 THR E 194 ILE E 197 ASP E 200
SITE 2 AC4 6 HOH E 422 HOH E 462
SITE 1 AC5 4 HIS E 142 HIS E 146 GLU E 166 CL E 324
SITE 1 AC6 4 HIS E 250 HOH E 401 HOH E 402 HOH E 403
SITE 1 AC7 5 GLY E 12 LEU E 14 GLY E 15 ASP E 16
SITE 2 AC7 5 LYS E 18
SITE 1 AC8 8 HIS E 142 GLU E 143 HIS E 146 TYR E 157
SITE 2 AC8 8 GLU E 166 HIS E 231 ZN E 321 HOH E 499
SITE 1 AC9 2 ARG E 285 HOH E 517
SITE 1 BC1 6 TYR E 211 HOH E 472 HOH E 503 HOH E 518
SITE 2 BC1 6 HOH E 519 HOH E 572
SITE 1 BC2 5 ALA E 209 LYS E 210 TYR E 211 GLY E 212
SITE 2 BC2 5 HOH E 519
SITE 1 BC3 5 ASN E 19 ASN E 21 ARG E 35 HOH E 419
SITE 2 BC3 5 HOH E 456
SITE 1 BC4 5 TYR E 179 ALA E 180 ASN E 181 ARG E 269
SITE 2 BC4 5 HOH E 584
SITE 1 BC5 4 TYR E 66 HIS E 216 HOH E 543 HOH E 578
SITE 1 BC6 2 SER E 206 TYR E 242
CRYST1 96.346 96.346 105.875 90.00 90.00 90.00 P 41 21 2 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 0.010379 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010379 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009445 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
