HEADER HYDROLASE 10-JUN-04 1TM4
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILSIN BPN'WITH CHYMOTRYPSIN
TITLE 2 INHIBITOR 2 M59G MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN BPN' PRECURSOR;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: SUBTILISIN NOVO, ALKALINE PROTEASE;
COMPND 5 EC: 3.4.21.62;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CHYMOTRYPSIN INHIBITOR 2;
COMPND 10 CHAIN: I;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;
SOURCE 3 ORGANISM_TAXID: 1390;
SOURCE 4 GENE: APR;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BG2036;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSER25;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HORDEUM VULGARE SUBSP. VULGARE;
SOURCE 12 ORGANISM_COMMON: DOMESTICATED BARLEY;
SOURCE 13 ORGANISM_TAXID: 112509;
SOURCE 14 STRAIN: SUBSP. VULGARE;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PCI2M59G
KEYWDS SERINE PROTEASE, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.RADISKY,G.KWAN,C.J.KAREN LU,D.E.KOSHLAND JR.
REVDAT 6 23-AUG-23 1TM4 1 REMARK
REVDAT 5 27-OCT-21 1TM4 1 REMARK SEQADV LINK
REVDAT 4 29-NOV-17 1TM4 1 REMARK
REVDAT 3 11-OCT-17 1TM4 1 REMARK
REVDAT 2 24-FEB-09 1TM4 1 VERSN
REVDAT 1 09-NOV-04 1TM4 0
JRNL AUTH E.S.RADISKY,G.KWAN,C.J.KAREN LU,D.E.KOSHLAND JR.
JRNL TITL BINDING, PROTEOLYTIC, AND CRYSTALLOGRAPHIC ANALYSES OF
JRNL TITL 2 MUTATIONS AT THE PROTEASE-INHIBITOR INTERFACE OF THE
JRNL TITL 3 SUBTILISIN BPN'/CHYMOTRYPSIN INHIBITOR 2 COMPLEX(,).
JRNL REF BIOCHEMISTRY V. 43 13648 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15504027
JRNL DOI 10.1021/BI048797K
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 81.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 51323
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : INHERITED FROM 1TM3
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2697
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) : 3516
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 176
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2499
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 439
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35000
REMARK 3 B22 (A**2) : 0.35000
REMARK 3 B33 (A**2) : -0.52000
REMARK 3 B12 (A**2) : 0.17000
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.556
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2660 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3608 ; 1.731 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 345 ; 5.739 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 406 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1993 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1274 ; 0.212 ; 0.200
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): 298 ; 0.151 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 8 ; 0.057 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.422 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 0.131 ; 0.200
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): 1714 ; 0.887 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2763 ; 1.511 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 946 ; 2.696 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 844 ; 4.564 ; 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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 1TM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA, TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54020
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 81.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 17.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.7000
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: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1TM3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, ISOPROPANOL, PEG 400,
REMARK 280 PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 124.53733
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 62.26867
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 93.40300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.13433
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 155.67167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 124.53733
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 62.26867
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 31.13433
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 93.40300
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 155.67167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 141.15000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 81.49299
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.26867
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 MET I 20 N CA CB CG SD CE
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 O6 CIT E 452 O6 CIT E 453 2.14
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 C13 1PE E 454 C13 1PE E 454 9765 1.88
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 ASP E 259 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP I 64 CB - CG - OD2 ANGL. DEV. = 5.5 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 LYS E 12 30.33 71.24
REMARK 500 ASP E 32 -151.11 -169.85
REMARK 500 ASP E 36 98.30 -69.97
REMARK 500 SER E 63 -22.52 109.40
REMARK 500 ALA E 73 24.74 -150.88
REMARK 500 ASN E 77 -158.84 -161.48
REMARK 500 SER E 159 67.97 -156.15
REMARK 500 LEU E 257 -124.46 -118.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE E 454
REMARK 610 1PE E 456
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 450 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 2 OE1
REMARK 620 2 ASP E 41 OD1 161.7
REMARK 620 3 LEU E 75 O 76.6 88.7
REMARK 620 4 ASN E 77 OD1 84.7 85.0 92.2
REMARK 620 5 ILE E 79 O 99.8 93.2 171.7 79.9
REMARK 620 6 VAL E 81 O 92.2 99.2 91.7 174.3 95.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E 451 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 169 O
REMARK 620 2 TYR E 171 O 93.9
REMARK 620 3 VAL E 174 O 109.6 90.3
REMARK 620 4 HOH E 488 O 107.4 158.7 82.2
REMARK 620 5 HOH E 592 O 103.5 85.8 146.9 89.6
REMARK 620 N 1 2 3 4
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 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT E 452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT E 453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE E 454
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE E 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE E 456
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TM1 RELATED DB: PDB
REMARK 900 RELATED ID: 1TM3 RELATED DB: PDB
REMARK 900 RELATED ID: 1TM5 RELATED DB: PDB
REMARK 900 RELATED ID: 1TM7 RELATED DB: PDB
REMARK 900 RELATED ID: 1TMG RELATED DB: PDB
REMARK 900 RELATED ID: 1TO1 RELATED DB: PDB
REMARK 900 RELATED ID: 1TO2 RELATED DB: PDB
DBREF 1TM4 E 1 275 UNP P00782 SUBT_BACAM 108 382
DBREF 1TM4 I 21 83 UNP Q40059 Q40059_HORVU 22 84
SEQADV 1TM4 HIS E 276 UNP P00782 EXPRESSION TAG
SEQADV 1TM4 HIS E 277 UNP P00782 EXPRESSION TAG
SEQADV 1TM4 HIS E 278 UNP P00782 EXPRESSION TAG
SEQADV 1TM4 HIS E 279 UNP P00782 EXPRESSION TAG
SEQADV 1TM4 HIS E 280 UNP P00782 EXPRESSION TAG
SEQADV 1TM4 MET I 20 UNP Q40059 INITIATING METHIONINE
SEQADV 1TM4 GLY I 59 UNP Q40059 MET 60 ENGINEERED MUTATION
SEQRES 1 E 281 ALA GLN SER VAL PRO TYR GLY VAL SER GLN ILE LYS ALA
SEQRES 2 E 281 PRO ALA LEU HIS SER GLN GLY TYR THR GLY SER ASN VAL
SEQRES 3 E 281 LYS VAL ALA VAL ILE ASP SER GLY ILE ASP SER SER HIS
SEQRES 4 E 281 PRO ASP LEU LYS VAL ALA GLY GLY ALA SER MET VAL PRO
SEQRES 5 E 281 SER GLU THR ASN PRO PHE GLN ASP ASN ASN SER HIS GLY
SEQRES 6 E 281 THR HIS VAL ALA GLY THR VAL ALA ALA LEU ASN ASN SER
SEQRES 7 E 281 ILE GLY VAL LEU GLY VAL ALA PRO SER ALA SER LEU TYR
SEQRES 8 E 281 ALA VAL LYS VAL LEU GLY ALA ASP GLY SER GLY GLN TYR
SEQRES 9 E 281 SER TRP ILE ILE ASN GLY ILE GLU TRP ALA ILE ALA ASN
SEQRES 10 E 281 ASN MET ASP VAL ILE ASN MET SER LEU GLY GLY PRO SER
SEQRES 11 E 281 GLY SER ALA ALA LEU LYS ALA ALA VAL ASP LYS ALA VAL
SEQRES 12 E 281 ALA SER GLY VAL VAL VAL VAL ALA ALA ALA GLY ASN GLU
SEQRES 13 E 281 GLY THR SER GLY SER SER SER THR VAL GLY TYR PRO GLY
SEQRES 14 E 281 LYS TYR PRO SER VAL ILE ALA VAL GLY ALA VAL ASP SER
SEQRES 15 E 281 SER ASN GLN ARG ALA SER PHE SER SER VAL GLY PRO GLU
SEQRES 16 E 281 LEU ASP VAL MET ALA PRO GLY VAL SER ILE GLN SER THR
SEQRES 17 E 281 LEU PRO GLY ASN LYS TYR GLY ALA TYR ASN GLY THR SER
SEQRES 18 E 281 MET ALA SER PRO HIS VAL ALA GLY ALA ALA ALA LEU ILE
SEQRES 19 E 281 LEU SER LYS HIS PRO ASN TRP THR ASN THR GLN VAL ARG
SEQRES 20 E 281 SER SER LEU GLU ASN THR THR THR LYS LEU GLY ASP SER
SEQRES 21 E 281 PHE TYR TYR GLY LYS GLY LEU ILE ASN VAL GLN ALA ALA
SEQRES 22 E 281 ALA GLN HIS HIS HIS HIS HIS HIS
SEQRES 1 I 64 MET LYS THR GLU TRP PRO GLU LEU VAL GLY LYS SER VAL
SEQRES 2 I 64 GLU GLU ALA LYS LYS VAL ILE LEU GLN ASP LYS PRO ALA
SEQRES 3 I 64 ALA GLN ILE ILE VAL LEU PRO VAL GLY THR ILE VAL THR
SEQRES 4 I 64 GLY GLU TYR ARG ILE ASP ARG VAL ARG LEU PHE VAL ASP
SEQRES 5 I 64 ARG LEU ASP ASN ILE ALA GLN VAL PRO ARG VAL GLY
HET CA E 450 1
HET NA E 451 1
HET CIT E 452 13
HET CIT E 453 13
HET 1PE E 454 11
HET 1PE E 455 16
HET 1PE E 456 12
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CIT CITRIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 CA CA 2+
FORMUL 4 NA NA 1+
FORMUL 5 CIT 2(C6 H8 O7)
FORMUL 7 1PE 3(C10 H22 O6)
FORMUL 10 HOH *439(H2 O)
HELIX 1 1 PRO E 5 ILE E 11 1 7
HELIX 2 2 LYS E 12 GLY E 20 1 9
HELIX 3 3 SER E 63 ALA E 74 1 12
HELIX 4 4 GLN E 103 ASN E 117 1 15
HELIX 5 5 SER E 132 SER E 145 1 14
HELIX 6 6 GLY E 219 HIS E 238 1 20
HELIX 7 7 THR E 242 ASN E 252 1 11
HELIX 8 8 ASP E 259 GLY E 264 1 6
HELIX 9 9 ASN E 269 ALA E 274 1 6
HELIX 10 10 TRP I 24 VAL I 28 5 5
HELIX 11 11 SER I 31 LYS I 43 1 13
SHEET 1 A 7 VAL E 44 SER E 49 0
SHEET 2 A 7 SER E 89 LYS E 94 1 O LEU E 90 N ALA E 45
SHEET 3 A 7 LYS E 27 ASP E 32 1 N VAL E 28 O TYR E 91
SHEET 4 A 7 VAL E 121 MET E 124 1 O VAL E 121 N ALA E 29
SHEET 5 A 7 VAL E 148 ALA E 152 1 O VAL E 148 N ILE E 122
SHEET 6 A 7 ILE E 175 VAL E 180 1 O ILE E 175 N ALA E 151
SHEET 7 A 7 VAL E 198 PRO E 201 1 O VAL E 198 N GLY E 178
SHEET 1 B 3 SER E 101 GLY E 102 0
SHEET 2 B 3 ILE I 56 THR I 58 -1 O ILE I 56 N GLY E 102
SHEET 3 B 3 LEU E 126 GLY E 127 -1 N GLY E 127 O VAL I 57
SHEET 1 C 2 ILE E 205 LEU E 209 0
SHEET 2 C 2 LYS E 213 TYR E 217 -1 O TYR E 217 N ILE E 205
SHEET 1 D 3 GLN I 47 PRO I 52 0
SHEET 2 D 3 ARG I 62 VAL I 70 1 O ASP I 64 N GLN I 47
SHEET 3 D 3 ARG I 81 GLY I 83 -1 O GLY I 83 N ARG I 65
LINK OE1 GLN E 2 CA CA E 450 1555 1555 2.41
LINK OD1 ASP E 41 CA CA E 450 1555 1555 2.43
LINK O LEU E 75 CA CA E 450 1555 1555 2.36
LINK OD1 ASN E 77 CA CA E 450 1555 1555 2.38
LINK O ILE E 79 CA CA E 450 1555 1555 2.39
LINK O VAL E 81 CA CA E 450 1555 1555 2.41
LINK O GLY E 169 NA NA E 451 1555 1555 2.35
LINK O TYR E 171 NA NA E 451 1555 1555 2.33
LINK O VAL E 174 NA NA E 451 1555 1555 2.31
LINK NA NA E 451 O HOH E 488 1555 1555 2.55
LINK NA NA E 451 O HOH E 592 1555 1555 2.46
CISPEP 1 TYR E 167 PRO E 168 0 7.60
SITE 1 AC1 6 GLN E 2 ASP E 41 LEU E 75 ASN E 77
SITE 2 AC1 6 ILE E 79 VAL E 81
SITE 1 AC2 5 GLY E 169 TYR E 171 VAL E 174 HOH E 488
SITE 2 AC2 5 HOH E 592
SITE 1 AC3 13 ALA E 1 TYR E 21 LYS E 237 HIS E 238
SITE 2 AC3 13 ASN E 240 TRP E 241 HIS E 276 CIT E 453
SITE 3 AC3 13 HOH E 484 HOH E 539 HOH E 573 HOH E 778
SITE 4 AC3 13 HOH E 800
SITE 1 AC4 12 TRP E 241 GLN E 245 HIS E 276 CIT E 452
SITE 2 AC4 12 HOH E 516 HOH E 539 HOH E 674 HOH E 682
SITE 3 AC4 12 HOH E 760 HOH E 778 HOH E 800 HOH E 801
SITE 1 AC5 5 HIS E 17 THR E 22 ASN E 76 HOH E 530
SITE 2 AC5 5 HOH E 773
SITE 1 AC6 6 ILE E 115 ASN E 118 MET E 119 SER E 145
SITE 2 AC6 6 HOH E 617 HOH E 802
SITE 1 AC7 5 SER E 37 VAL E 44 ALA E 45 PHE E 58
SITE 2 AC7 5 HOH E 779
CRYST1 94.100 94.100 186.806 90.00 90.00 120.00 P 65 2 2 12
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 0.010627 0.006135 0.000000 0.00000
SCALE2 0.000000 0.012271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005353 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
