HEADER HYDROLASE/HYDROLASE INHIBITOR 10-MAY-11 3RXM
TITLE CRYSTAL STRUCTURE OF TRYPSIN COMPLEXED WITH [2-(2-THIENYL)THIAZOL-4-
TITLE 2 YL]METHANAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN, ALPHA-TRYPSIN CHAIN 1, ALPHA-TRYPSIN CHAIN 2;
COMPND 5 EC: 3.4.21.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS TRYPSIN-LIKE SERINE PROTEASES, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YAMANE,M.YAO,Y.ZHOU,I.TANAKA
REVDAT 2 01-NOV-23 3RXM 1 REMARK LINK
REVDAT 1 24-AUG-11 3RXM 0
JRNL AUTH J.YAMANE,M.YAO,Y.ZHOU,Y.HIRAMATSU,K.FUJIWARA,T.YAMAGUCHI,
JRNL AUTH 2 H.YAMAGUCHI,H.TOGAME,H.TSUJISHITA,H.TAKEMOTO,I.TANAKA
JRNL TITL IN-CRYSTAL AFFINITY RANKING OF FRAGMENT HIT COMPOUNDS
JRNL TITL 2 REVEALS A RELATIONSHIP WITH THEIR INHIBITORY ACTIVITIES
JRNL REF J.APPL.CRYSTALLOGR. V. 44 798 2011
JRNL REFN ISSN 0021-8898
JRNL DOI 10.1107/S0021889811017717
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0091
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 22525
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1187
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1470
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.1920
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.2550
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 : 41
REMARK 3 SOLVENT ATOMS : 326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.11000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.535
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1701 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1115 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2303 ; 1.384 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2732 ; 0.821 ; 3.009
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 222 ; 6.078 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 58 ;38.186 ;25.862
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 269 ;10.340 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;19.267 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 260 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1894 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 309 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3RXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000065503.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 : RIGAKU MICROMAX-007
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 RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23840
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.03400
REMARK 200 R SYM (I) : 0.03400
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1S0R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 30% PEG 3350, 0.2M
REMARK 280 LITHIUM SULFATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 27.20250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.44750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.08600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.44750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.20250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.08600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -82.04 -117.36
REMARK 500 SER A 195 128.82 -34.76
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 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 16 O
REMARK 620 2 GLU A 70 OE1 78.1
REMARK 620 3 ASN A 72 O 108.0 92.7
REMARK 620 4 VAL A 75 O 90.3 163.2 79.2
REMARK 620 5 GLU A 80 OE2 92.5 105.6 155.0 86.8
REMARK 620 6 HOH A 327 O 158.9 88.6 88.7 105.8 75.3
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SW1 A 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RXA RELATED DB: PDB
REMARK 900 RELATED ID: 3RXB RELATED DB: PDB
REMARK 900 RELATED ID: 3RXC RELATED DB: PDB
REMARK 900 RELATED ID: 3RXD RELATED DB: PDB
REMARK 900 RELATED ID: 3RXE RELATED DB: PDB
REMARK 900 RELATED ID: 3RXF RELATED DB: PDB
REMARK 900 RELATED ID: 3RXG RELATED DB: PDB
REMARK 900 RELATED ID: 3RXH RELATED DB: PDB
REMARK 900 RELATED ID: 3RXI RELATED DB: PDB
REMARK 900 RELATED ID: 3RXJ RELATED DB: PDB
REMARK 900 RELATED ID: 3RXK RELATED DB: PDB
REMARK 900 RELATED ID: 3RXL RELATED DB: PDB
REMARK 900 RELATED ID: 3RXO RELATED DB: PDB
REMARK 900 RELATED ID: 3RXP RELATED DB: PDB
REMARK 900 RELATED ID: 3RXQ RELATED DB: PDB
REMARK 900 RELATED ID: 3RXR RELATED DB: PDB
REMARK 900 RELATED ID: 3RXS RELATED DB: PDB
REMARK 900 RELATED ID: 3RXT RELATED DB: PDB
REMARK 900 RELATED ID: 3RXU RELATED DB: PDB
REMARK 900 RELATED ID: 3RXV RELATED DB: PDB
REMARK 900 RELATED ID: 3ATI RELATED DB: PDB
REMARK 900 RELATED ID: 3ATK RELATED DB: PDB
REMARK 900 RELATED ID: 3ATL RELATED DB: PDB
REMARK 900 RELATED ID: 3ATM RELATED DB: PDB
DBREF 3RXM A 19 241 UNP P00760 TRY1_BOVIN 24 246
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 1 1
HET GOL A 2 6
HET GOL A 3 6
HET DMS A 4 4
HET DMS A 5 4
HET DMS A 6 4
HET DMS A 7 4
HET SW1 A 8 12
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM SW1 1-[2-(THIOPHEN-2-YL)-1,3-THIAZOL-4-YL]METHANAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CA CA 2+
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 DMS 4(C2 H6 O S)
FORMUL 9 SW1 C8 H8 N2 S2
FORMUL 10 HOH *326(H2 O)
HELIX 1 1 ALA A 56 TYR A 60 5 5
HELIX 2 2 SER A 162 TYR A 170 1 9
HELIX 3 3 TYR A 230 SER A 240 1 11
SHEET 1 A 7 TYR A 23 THR A 24 0
SHEET 2 A 7 LYS A 154 PRO A 159 -1 O CYS A 155 N TYR A 23
SHEET 3 A 7 GLN A 133 GLY A 138 -1 N ILE A 136 O LEU A 156
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 135
SHEET 5 A 7 LYS A 204 TRP A 211 -1 O LYS A 204 N CYS A 201
SHEET 6 A 7 GLY A 222 LYS A 226 -1 O VAL A 223 N TRP A 211
SHEET 7 A 7 MET A 178 ALA A 181 -1 N PHE A 179 O TYR A 224
SHEET 1 B 7 GLN A 33 ASN A 37 0
SHEET 2 B 7 HIS A 41 ASN A 49 -1 O CYS A 43 N LEU A 36
SHEET 3 B 7 TRP A 52 SER A 55 -1 O VAL A 54 N SER A 46
SHEET 4 B 7 MET A 104 LEU A 108 -1 O ILE A 106 N VAL A 53
SHEET 5 B 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 B 7 GLN A 65 LEU A 68 -1 N VAL A 66 O ILE A 83
SHEET 7 B 7 GLN A 33 ASN A 37 -1 N ASN A 37 O GLN A 65
SSBOND 1 CYS A 25 CYS A 155 1555 1555 2.03
SSBOND 2 CYS A 43 CYS A 59 1555 1555 2.03
SSBOND 3 CYS A 127 CYS A 228 1555 1555 2.04
SSBOND 4 CYS A 134 CYS A 201 1555 1555 2.03
SSBOND 5 CYS A 166 CYS A 180 1555 1555 2.03
SSBOND 6 CYS A 191 CYS A 215 1555 1555 2.03
LINK CA CA A 1 O HOH A 16 1555 1555 2.41
LINK CA CA A 1 OE1 GLU A 70 1555 1555 2.25
LINK CA CA A 1 O ASN A 72 1555 1555 2.34
LINK CA CA A 1 O VAL A 75 1555 1555 2.24
LINK CA CA A 1 OE2 GLU A 80 1555 1555 2.35
LINK CA CA A 1 O HOH A 327 1555 1555 2.34
SITE 1 AC1 6 HOH A 16 GLU A 70 ASN A 72 VAL A 75
SITE 2 AC1 6 GLU A 80 HOH A 327
SITE 1 AC2 9 CYS A 127 ALA A 128 ILE A 160 PHE A 179
SITE 2 AC2 9 GLN A 206 LYS A 226 CYS A 228 HOH A 348
SITE 3 AC2 9 HOH A 479
SITE 1 AC3 11 DMS A 4 TYR A 40 HIS A 41 ILE A 73
SITE 2 AC3 11 ASN A 74 SER A 88 ILE A 89 VAL A 90
SITE 3 AC3 11 HOH A 249 HOH A 339 HOH A 437
SITE 1 AC4 9 GOL A 3 HOH A 16 ARG A 67 ILE A 73
SITE 2 AC4 9 ASN A 74 PHE A 82 VAL A 90 HIS A 91
SITE 3 AC4 9 TYR A 94
SITE 1 AC5 5 VAL A 76 SER A 96 ASN A 97 HOH A 244
SITE 2 AC5 5 HOH A 553
SITE 1 AC6 6 ASN A 97 THR A 98 LYS A 157 GLN A 173
SITE 2 AC6 6 TRP A 211 HOH A 259
SITE 1 AC7 7 TYR A 23 CYS A 25 THR A 29 LEU A 135
SITE 2 AC7 7 GLN A 173 HOH A 259 HOH A 318
SITE 1 AC8 9 ASP A 189 SER A 190 GLN A 192 SER A 202
SITE 2 AC8 9 VAL A 209 TRP A 211 GLY A 214 HOH A 258
SITE 3 AC8 9 HOH A 300
CRYST1 54.405 58.172 66.895 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018381 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017190 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014949 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
