HEADER LYASE 11-FEB-04 1SBZ
TITLE CRYSTAL STRUCTURE OF DODECAMERIC FMN-DEPENDENT UBIX-LIKE DECARBOXYLASE
TITLE 2 FROM ESCHERICHIA COLI O157:H7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE AROMATIC ACID DECARBOXYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 4.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83334;
SOURCE 4 STRAIN: O157:H7;
SOURCE 5 GENE: PAD1, Z4047, ECS3593;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DL41 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFO4
KEYWDS FMN BINDING, PAD1, UBIX, MONTREAL-KINGSTON BACTERIAL STRUCTURAL
KEYWDS 2 GENOMICS INITIATIVE, BSGI, STRUCTURAL GENOMICS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.RANGARAJAN,Y.LI,P.IANNUZZI,A.TOCILJ,L.-W.HUNG,A.MATTE,M.CYGLER,
AUTHOR 2 MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE (BSGI)
REVDAT 6 24-JUL-19 1SBZ 1 REMARK LINK
REVDAT 5 31-JAN-18 1SBZ 1 REMARK
REVDAT 4 13-JUL-11 1SBZ 1 VERSN
REVDAT 3 24-FEB-09 1SBZ 1 VERSN
REVDAT 2 23-NOV-04 1SBZ 1 JRNL
REVDAT 1 26-OCT-04 1SBZ 0
JRNL AUTH E.S.RANGARAJAN,Y.LI,P.IANNUZZI,A.TOCILJ,L.-W.HUNG,A.MATTE,
JRNL AUTH 2 M.CYGLER
JRNL TITL CRYSTAL STRUCTURE OF A DODECAMERIC FMN-DEPENDENT UBIX-LIKE
JRNL TITL 2 DECARBOXYLASE (PAD1) FROM ESCHERICHIA COLI O157: H7.
JRNL REF PROTEIN SCI. V. 13 3006 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15459342
JRNL DOI 10.1110/PS.04953004
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 42181
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4137
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2268
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 144
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5426
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 458
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.210
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.315
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5666 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7721 ; 1.108 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 715 ; 5.110 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 932 ;16.708 ;15.000
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): 903 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4139 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2822 ; 0.214 ; 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): 456 ; 0.153 ; 0.200
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): 132 ; 0.179 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 48 ; 0.226 ; 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): 3704 ; 0.793 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5784 ; 0.942 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2352 ; 1.407 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1937 ; 2.092 ; 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 : 1.20
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 1SBZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021587.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786, 0.9792, 0.9643
REMARK 200 MONOCHROMATOR : SILICONE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46319
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
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) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37700
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4K, 0.2M LITHIUM SULPHATE,
REMARK 280 0.1M HEPES (7.0), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 22K,
REMARK 280 PH 7.0, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.68600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.53152
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 72.51267
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 47.68600
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 27.53152
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 72.51267
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 47.68600
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 27.53152
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.51267
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.06305
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 145.02533
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 55.06305
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 145.02533
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 55.06305
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 145.02533
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 300 REMARK: THE BIOLOGICAL UNIT IS A DODECAMER AND IS ASSEMBLED BY BY
REMARK 300 THE OPERATIONS : -Y, X-Y, Z & Y-X, -X, Z ALONG WITH TRANSLATION.
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 56090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -381.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 47.68600
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -82.59457
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 95.37200
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 TYR A 179
REMARK 465 ALA A 180
REMARK 465 ARG A 181
REMARK 465 PRO A 187
REMARK 465 GLN A 188
REMARK 465 ALA A 189
REMARK 465 ARG A 190
REMARK 465 ASN A 191
REMARK 465 PHE A 192
REMARK 465 SER A 193
REMARK 465 GLN A 194
REMARK 465 GLU A 195
REMARK 465 ASN A 196
REMARK 465 GLU A 197
REMARK 465 HIS B 177
REMARK 465 PRO B 178
REMARK 465 TYR B 179
REMARK 465 ALA B 180
REMARK 465 ARG B 181
REMARK 465 ARG B 182
REMARK 465 TRP B 183
REMARK 465 GLN B 184
REMARK 465 GLY B 185
REMARK 465 LEU B 186
REMARK 465 PRO B 187
REMARK 465 GLN B 188
REMARK 465 ALA B 189
REMARK 465 ARG B 190
REMARK 465 ASN B 191
REMARK 465 PHE B 192
REMARK 465 SER B 193
REMARK 465 GLN B 194
REMARK 465 GLU B 195
REMARK 465 ASN B 196
REMARK 465 GLU B 197
REMARK 465 HIS C 177
REMARK 465 PRO C 178
REMARK 465 TYR C 179
REMARK 465 ALA C 180
REMARK 465 ARG C 181
REMARK 465 ARG C 182
REMARK 465 TRP C 183
REMARK 465 GLN C 184
REMARK 465 GLY C 185
REMARK 465 LEU C 186
REMARK 465 PRO C 187
REMARK 465 GLN C 188
REMARK 465 ALA C 189
REMARK 465 ARG C 190
REMARK 465 ASN C 191
REMARK 465 PHE C 192
REMARK 465 SER C 193
REMARK 465 GLN C 194
REMARK 465 GLU C 195
REMARK 465 ASN C 196
REMARK 465 GLU C 197
REMARK 465 LEU D 186
REMARK 465 PRO D 187
REMARK 465 GLN D 188
REMARK 465 ALA D 189
REMARK 465 ARG D 190
REMARK 465 ASN D 191
REMARK 465 PHE D 192
REMARK 465 SER D 193
REMARK 465 GLN D 194
REMARK 465 GLU D 195
REMARK 465 ASN D 196
REMARK 465 GLU D 197
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 NE ARG B 139 O HOH B 1495 2.11
REMARK 500 NE ARG A 139 O HOH A 1492 2.15
REMARK 500 O HOH C 1436 O HOH C 1459 2.17
REMARK 500 NE ARG C 139 O HOH C 1466 2.18
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 A 1413 O HOH A 1460 2545 1.68
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 VAL A 120 75.41 -112.53
REMARK 500 HIS A 154 71.88 53.72
REMARK 500 GLN A 184 -102.19 -129.50
REMARK 500 VAL B 120 74.93 -112.22
REMARK 500 VAL C 120 76.78 -110.76
REMARK 500 VAL D 120 76.25 -116.86
REMARK 500 GLU D 123 147.50 -170.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN D 1404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PAD1_ECO57 RELATED DB: TARGETDB
DBREF 1SBZ A 1 197 UNP P69774 PAD1_ECOLI 1 197
DBREF 1SBZ B 1 197 UNP P69774 PAD1_ECOLI 1 197
DBREF 1SBZ C 1 197 UNP P69774 PAD1_ECOLI 1 197
DBREF 1SBZ D 1 197 UNP P69774 PAD1_ECOLI 1 197
SEQADV 1SBZ MSE A 1 UNP P69774 MET 1 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 7 UNP P69774 MET 7 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 26 UNP P69774 MET 26 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 35 UNP P69774 MET 35 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 81 UNP P69774 MET 81 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 88 UNP P69774 MET 88 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 124 UNP P69774 MET 124 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 134 UNP P69774 MET 134 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 140 UNP P69774 MET 140 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 144 UNP P69774 MET 144 MODIFIED RESIDUE
SEQADV 1SBZ MSE A 148 UNP P69774 MET 148 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 1 UNP P69774 MET 1 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 7 UNP P69774 MET 7 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 26 UNP P69774 MET 26 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 35 UNP P69774 MET 35 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 81 UNP P69774 MET 81 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 88 UNP P69774 MET 88 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 124 UNP P69774 MET 124 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 134 UNP P69774 MET 134 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 140 UNP P69774 MET 140 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 144 UNP P69774 MET 144 MODIFIED RESIDUE
SEQADV 1SBZ MSE B 148 UNP P69774 MET 148 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 1 UNP P69774 MET 1 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 7 UNP P69774 MET 7 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 26 UNP P69774 MET 26 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 35 UNP P69774 MET 35 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 81 UNP P69774 MET 81 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 88 UNP P69774 MET 88 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 124 UNP P69774 MET 124 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 134 UNP P69774 MET 134 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 140 UNP P69774 MET 140 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 144 UNP P69774 MET 144 MODIFIED RESIDUE
SEQADV 1SBZ MSE C 148 UNP P69774 MET 148 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 1 UNP P69774 MET 1 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 7 UNP P69774 MET 7 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 26 UNP P69774 MET 26 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 35 UNP P69774 MET 35 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 81 UNP P69774 MET 81 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 88 UNP P69774 MET 88 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 124 UNP P69774 MET 124 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 134 UNP P69774 MET 134 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 140 UNP P69774 MET 140 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 144 UNP P69774 MET 144 MODIFIED RESIDUE
SEQADV 1SBZ MSE D 148 UNP P69774 MET 148 MODIFIED RESIDUE
SEQRES 1 A 197 MSE LYS LEU ILE VAL GLY MSE THR GLY ALA THR GLY ALA
SEQRES 2 A 197 PRO LEU GLY VAL ALA LEU LEU GLN ALA LEU ARG GLU MSE
SEQRES 3 A 197 PRO ASN VAL GLU THR HIS LEU VAL MSE SER LYS TRP ALA
SEQRES 4 A 197 LYS THR THR ILE GLU LEU GLU THR PRO TYR SER ALA ARG
SEQRES 5 A 197 ASP VAL ALA ALA LEU ALA ASP PHE SER HIS ASN PRO ALA
SEQRES 6 A 197 ASP GLN ALA ALA THR ILE SER SER GLY SER PHE ARG THR
SEQRES 7 A 197 ASP GLY MSE ILE VAL ILE PRO CYS SER MSE LYS THR LEU
SEQRES 8 A 197 ALA GLY ILE ARG ALA GLY TYR ALA ASP GLY LEU VAL GLY
SEQRES 9 A 197 ARG ALA ALA ASP VAL VAL LEU LYS GLU GLY ARG LYS LEU
SEQRES 10 A 197 VAL LEU VAL PRO ARG GLU MSE PRO LEU SER THR ILE HIS
SEQRES 11 A 197 LEU GLU ASN MSE LEU ALA LEU SER ARG MSE GLY VAL ALA
SEQRES 12 A 197 MSE VAL PRO PRO MSE PRO ALA PHE TYR ASN HIS PRO GLU
SEQRES 13 A 197 THR VAL ASP ASP ILE VAL HIS HIS VAL VAL ALA ARG VAL
SEQRES 14 A 197 LEU ASP GLN PHE GLY LEU GLU HIS PRO TYR ALA ARG ARG
SEQRES 15 A 197 TRP GLN GLY LEU PRO GLN ALA ARG ASN PHE SER GLN GLU
SEQRES 16 A 197 ASN GLU
SEQRES 1 B 197 MSE LYS LEU ILE VAL GLY MSE THR GLY ALA THR GLY ALA
SEQRES 2 B 197 PRO LEU GLY VAL ALA LEU LEU GLN ALA LEU ARG GLU MSE
SEQRES 3 B 197 PRO ASN VAL GLU THR HIS LEU VAL MSE SER LYS TRP ALA
SEQRES 4 B 197 LYS THR THR ILE GLU LEU GLU THR PRO TYR SER ALA ARG
SEQRES 5 B 197 ASP VAL ALA ALA LEU ALA ASP PHE SER HIS ASN PRO ALA
SEQRES 6 B 197 ASP GLN ALA ALA THR ILE SER SER GLY SER PHE ARG THR
SEQRES 7 B 197 ASP GLY MSE ILE VAL ILE PRO CYS SER MSE LYS THR LEU
SEQRES 8 B 197 ALA GLY ILE ARG ALA GLY TYR ALA ASP GLY LEU VAL GLY
SEQRES 9 B 197 ARG ALA ALA ASP VAL VAL LEU LYS GLU GLY ARG LYS LEU
SEQRES 10 B 197 VAL LEU VAL PRO ARG GLU MSE PRO LEU SER THR ILE HIS
SEQRES 11 B 197 LEU GLU ASN MSE LEU ALA LEU SER ARG MSE GLY VAL ALA
SEQRES 12 B 197 MSE VAL PRO PRO MSE PRO ALA PHE TYR ASN HIS PRO GLU
SEQRES 13 B 197 THR VAL ASP ASP ILE VAL HIS HIS VAL VAL ALA ARG VAL
SEQRES 14 B 197 LEU ASP GLN PHE GLY LEU GLU HIS PRO TYR ALA ARG ARG
SEQRES 15 B 197 TRP GLN GLY LEU PRO GLN ALA ARG ASN PHE SER GLN GLU
SEQRES 16 B 197 ASN GLU
SEQRES 1 C 197 MSE LYS LEU ILE VAL GLY MSE THR GLY ALA THR GLY ALA
SEQRES 2 C 197 PRO LEU GLY VAL ALA LEU LEU GLN ALA LEU ARG GLU MSE
SEQRES 3 C 197 PRO ASN VAL GLU THR HIS LEU VAL MSE SER LYS TRP ALA
SEQRES 4 C 197 LYS THR THR ILE GLU LEU GLU THR PRO TYR SER ALA ARG
SEQRES 5 C 197 ASP VAL ALA ALA LEU ALA ASP PHE SER HIS ASN PRO ALA
SEQRES 6 C 197 ASP GLN ALA ALA THR ILE SER SER GLY SER PHE ARG THR
SEQRES 7 C 197 ASP GLY MSE ILE VAL ILE PRO CYS SER MSE LYS THR LEU
SEQRES 8 C 197 ALA GLY ILE ARG ALA GLY TYR ALA ASP GLY LEU VAL GLY
SEQRES 9 C 197 ARG ALA ALA ASP VAL VAL LEU LYS GLU GLY ARG LYS LEU
SEQRES 10 C 197 VAL LEU VAL PRO ARG GLU MSE PRO LEU SER THR ILE HIS
SEQRES 11 C 197 LEU GLU ASN MSE LEU ALA LEU SER ARG MSE GLY VAL ALA
SEQRES 12 C 197 MSE VAL PRO PRO MSE PRO ALA PHE TYR ASN HIS PRO GLU
SEQRES 13 C 197 THR VAL ASP ASP ILE VAL HIS HIS VAL VAL ALA ARG VAL
SEQRES 14 C 197 LEU ASP GLN PHE GLY LEU GLU HIS PRO TYR ALA ARG ARG
SEQRES 15 C 197 TRP GLN GLY LEU PRO GLN ALA ARG ASN PHE SER GLN GLU
SEQRES 16 C 197 ASN GLU
SEQRES 1 D 197 MSE LYS LEU ILE VAL GLY MSE THR GLY ALA THR GLY ALA
SEQRES 2 D 197 PRO LEU GLY VAL ALA LEU LEU GLN ALA LEU ARG GLU MSE
SEQRES 3 D 197 PRO ASN VAL GLU THR HIS LEU VAL MSE SER LYS TRP ALA
SEQRES 4 D 197 LYS THR THR ILE GLU LEU GLU THR PRO TYR SER ALA ARG
SEQRES 5 D 197 ASP VAL ALA ALA LEU ALA ASP PHE SER HIS ASN PRO ALA
SEQRES 6 D 197 ASP GLN ALA ALA THR ILE SER SER GLY SER PHE ARG THR
SEQRES 7 D 197 ASP GLY MSE ILE VAL ILE PRO CYS SER MSE LYS THR LEU
SEQRES 8 D 197 ALA GLY ILE ARG ALA GLY TYR ALA ASP GLY LEU VAL GLY
SEQRES 9 D 197 ARG ALA ALA ASP VAL VAL LEU LYS GLU GLY ARG LYS LEU
SEQRES 10 D 197 VAL LEU VAL PRO ARG GLU MSE PRO LEU SER THR ILE HIS
SEQRES 11 D 197 LEU GLU ASN MSE LEU ALA LEU SER ARG MSE GLY VAL ALA
SEQRES 12 D 197 MSE VAL PRO PRO MSE PRO ALA PHE TYR ASN HIS PRO GLU
SEQRES 13 D 197 THR VAL ASP ASP ILE VAL HIS HIS VAL VAL ALA ARG VAL
SEQRES 14 D 197 LEU ASP GLN PHE GLY LEU GLU HIS PRO TYR ALA ARG ARG
SEQRES 15 D 197 TRP GLN GLY LEU PRO GLN ALA ARG ASN PHE SER GLN GLU
SEQRES 16 D 197 ASN GLU
MODRES 1SBZ MSE A 1 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 7 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 26 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 35 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 81 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 88 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 124 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 134 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 140 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 144 MET SELENOMETHIONINE
MODRES 1SBZ MSE A 148 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 1 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 7 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 26 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 35 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 81 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 88 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 124 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 134 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 140 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 144 MET SELENOMETHIONINE
MODRES 1SBZ MSE B 148 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 1 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 7 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 26 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 35 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 81 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 88 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 124 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 134 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 140 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 144 MET SELENOMETHIONINE
MODRES 1SBZ MSE C 148 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 1 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 7 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 26 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 35 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 81 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 88 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 124 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 134 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 140 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 144 MET SELENOMETHIONINE
MODRES 1SBZ MSE D 148 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 7 8
HET MSE A 26 8
HET MSE A 35 8
HET MSE A 81 8
HET MSE A 88 8
HET MSE A 124 8
HET MSE A 134 8
HET MSE A 140 8
HET MSE A 144 8
HET MSE A 148 8
HET MSE B 1 8
HET MSE B 7 8
HET MSE B 26 8
HET MSE B 35 8
HET MSE B 81 8
HET MSE B 88 8
HET MSE B 124 8
HET MSE B 134 8
HET MSE B 140 8
HET MSE B 144 8
HET MSE B 148 8
HET MSE C 1 8
HET MSE C 7 8
HET MSE C 26 8
HET MSE C 35 8
HET MSE C 81 8
HET MSE C 88 8
HET MSE C 124 8
HET MSE C 134 8
HET MSE C 140 8
HET MSE C 144 8
HET MSE C 148 8
HET MSE D 1 8
HET MSE D 7 8
HET MSE D 26 8
HET MSE D 35 8
HET MSE D 81 8
HET MSE D 88 8
HET MSE D 124 8
HET MSE D 134 8
HET MSE D 140 8
HET MSE D 144 8
HET MSE D 148 8
HET FMN A1401 31
HET FMN B1402 31
HET FMN C1403 31
HET FMN D1404 31
HETNAM MSE SELENOMETHIONINE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 1 MSE 44(C5 H11 N O2 SE)
FORMUL 5 FMN 4(C17 H21 N4 O9 P)
FORMUL 9 HOH *458(H2 O)
HELIX 1 1 GLY A 12 GLU A 25 1 14
HELIX 2 2 SER A 36 THR A 47 1 12
HELIX 3 3 SER A 50 LEU A 57 1 8
HELIX 4 4 ALA A 69 SER A 73 5 5
HELIX 5 5 SER A 87 GLY A 97 1 11
HELIX 6 6 GLY A 101 GLY A 114 1 14
HELIX 7 7 SER A 127 ARG A 139 1 13
HELIX 8 8 THR A 157 ASP A 171 1 15
HELIX 9 9 GLN A 172 GLY A 174 5 3
HELIX 10 10 GLY B 12 GLU B 25 1 14
HELIX 11 11 SER B 36 THR B 47 1 12
HELIX 12 12 SER B 50 ALA B 56 1 7
HELIX 13 13 ALA B 69 SER B 73 5 5
HELIX 14 14 SER B 87 GLY B 97 1 11
HELIX 15 15 GLY B 101 GLU B 113 1 13
HELIX 16 16 SER B 127 MSE B 140 1 14
HELIX 17 17 THR B 157 GLN B 172 1 16
HELIX 18 18 GLY C 12 GLU C 25 1 14
HELIX 19 19 SER C 36 THR C 47 1 12
HELIX 20 20 SER C 50 ALA C 56 1 7
HELIX 21 21 ALA C 69 SER C 73 5 5
HELIX 22 22 SER C 87 GLY C 97 1 11
HELIX 23 23 GLY C 101 GLU C 113 1 13
HELIX 24 24 SER C 127 MSE C 140 1 14
HELIX 25 25 THR C 157 GLN C 172 1 16
HELIX 26 26 GLY D 12 GLU D 25 1 14
HELIX 27 27 SER D 36 THR D 47 1 12
HELIX 28 28 SER D 50 ALA D 56 1 7
HELIX 29 29 ALA D 69 SER D 73 5 5
HELIX 30 30 SER D 87 GLY D 97 1 11
HELIX 31 31 GLY D 101 GLU D 113 1 13
HELIX 32 32 SER D 127 MSE D 140 1 14
HELIX 33 33 THR D 157 ASP D 171 1 15
HELIX 34 34 GLN D 172 GLY D 174 5 3
SHEET 1 A 6 PHE A 60 HIS A 62 0
SHEET 2 A 6 GLU A 30 MSE A 35 1 N LEU A 33 O PHE A 60
SHEET 3 A 6 LYS A 2 MSE A 7 1 N VAL A 5 O HIS A 32
SHEET 4 A 6 GLY A 80 CYS A 86 1 O ILE A 82 N GLY A 6
SHEET 5 A 6 LYS A 116 PRO A 121 1 O VAL A 120 N CYS A 86
SHEET 6 A 6 ALA A 143 MSE A 144 1 O ALA A 143 N LEU A 119
SHEET 1 B 6 PHE B 60 HIS B 62 0
SHEET 2 B 6 GLU B 30 MSE B 35 1 N LEU B 33 O PHE B 60
SHEET 3 B 6 LYS B 2 MSE B 7 1 N MSE B 7 O VAL B 34
SHEET 4 B 6 GLY B 80 CYS B 86 1 O ILE B 82 N GLY B 6
SHEET 5 B 6 LYS B 116 PRO B 121 1 O VAL B 120 N CYS B 86
SHEET 6 B 6 ALA B 143 MSE B 144 1 O ALA B 143 N LEU B 119
SHEET 1 C 6 PHE C 60 SER C 61 0
SHEET 2 C 6 GLU C 30 MSE C 35 1 N LEU C 33 O PHE C 60
SHEET 3 C 6 LYS C 2 MSE C 7 1 N VAL C 5 O HIS C 32
SHEET 4 C 6 MSE C 81 CYS C 86 1 O ILE C 82 N GLY C 6
SHEET 5 C 6 LEU C 117 PRO C 121 1 O VAL C 120 N CYS C 86
SHEET 6 C 6 ALA C 143 MSE C 144 1 O ALA C 143 N LEU C 119
SHEET 1 D 6 PHE D 60 HIS D 62 0
SHEET 2 D 6 GLU D 30 MSE D 35 1 N LEU D 33 O HIS D 62
SHEET 3 D 6 LYS D 2 MSE D 7 1 N VAL D 5 O HIS D 32
SHEET 4 D 6 GLY D 80 CYS D 86 1 O ILE D 82 N GLY D 6
SHEET 5 D 6 LYS D 116 PRO D 121 1 O VAL D 120 N CYS D 86
SHEET 6 D 6 ALA D 143 MSE D 144 1 O ALA D 143 N LEU D 119
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C GLY A 6 N MSE A 7 1555 1555 1.33
LINK C MSE A 7 N THR A 8 1555 1555 1.32
LINK C GLU A 25 N MSE A 26 1555 1555 1.33
LINK C MSE A 26 N PRO A 27 1555 1555 1.34
LINK C VAL A 34 N MSE A 35 1555 1555 1.33
LINK C MSE A 35 N SER A 36 1555 1555 1.33
LINK C GLY A 80 N MSE A 81 1555 1555 1.33
LINK C MSE A 81 N ILE A 82 1555 1555 1.33
LINK C SER A 87 N MSE A 88 1555 1555 1.33
LINK C MSE A 88 N LYS A 89 1555 1555 1.33
LINK C GLU A 123 N MSE A 124 1555 1555 1.33
LINK C MSE A 124 N PRO A 125 1555 1555 1.34
LINK C ASN A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N LEU A 135 1555 1555 1.33
LINK C ARG A 139 N MSE A 140 1555 1555 1.33
LINK C MSE A 140 N GLY A 141 1555 1555 1.33
LINK C ALA A 143 N MSE A 144 1555 1555 1.33
LINK C MSE A 144 N VAL A 145 1555 1555 1.33
LINK C PRO A 147 N MSE A 148 1555 1555 1.33
LINK C MSE A 148 N PRO A 149 1555 1555 1.33
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C GLY B 6 N MSE B 7 1555 1555 1.33
LINK C MSE B 7 N THR B 8 1555 1555 1.32
LINK C GLU B 25 N MSE B 26 1555 1555 1.33
LINK C MSE B 26 N PRO B 27 1555 1555 1.34
LINK C VAL B 34 N MSE B 35 1555 1555 1.32
LINK C MSE B 35 N SER B 36 1555 1555 1.33
LINK C GLY B 80 N MSE B 81 1555 1555 1.33
LINK C MSE B 81 N ILE B 82 1555 1555 1.33
LINK C SER B 87 N MSE B 88 1555 1555 1.33
LINK C MSE B 88 N LYS B 89 1555 1555 1.33
LINK C GLU B 123 N MSE B 124 1555 1555 1.33
LINK C MSE B 124 N PRO B 125 1555 1555 1.34
LINK C ASN B 133 N MSE B 134 1555 1555 1.33
LINK C MSE B 134 N LEU B 135 1555 1555 1.33
LINK C ARG B 139 N MSE B 140 1555 1555 1.33
LINK C MSE B 140 N GLY B 141 1555 1555 1.33
LINK C ALA B 143 N MSE B 144 1555 1555 1.33
LINK C MSE B 144 N VAL B 145 1555 1555 1.33
LINK C PRO B 147 N MSE B 148 1555 1555 1.33
LINK C MSE B 148 N PRO B 149 1555 1555 1.34
LINK C MSE C 1 N LYS C 2 1555 1555 1.33
LINK C GLY C 6 N MSE C 7 1555 1555 1.33
LINK C MSE C 7 N THR C 8 1555 1555 1.32
LINK C GLU C 25 N MSE C 26 1555 1555 1.33
LINK C MSE C 26 N PRO C 27 1555 1555 1.33
LINK C VAL C 34 N MSE C 35 1555 1555 1.33
LINK C MSE C 35 N SER C 36 1555 1555 1.33
LINK C GLY C 80 N MSE C 81 1555 1555 1.33
LINK C MSE C 81 N ILE C 82 1555 1555 1.33
LINK C SER C 87 N MSE C 88 1555 1555 1.33
LINK C MSE C 88 N LYS C 89 1555 1555 1.33
LINK C GLU C 123 N MSE C 124 1555 1555 1.33
LINK C MSE C 124 N PRO C 125 1555 1555 1.33
LINK C ASN C 133 N MSE C 134 1555 1555 1.33
LINK C MSE C 134 N LEU C 135 1555 1555 1.33
LINK C ARG C 139 N MSE C 140 1555 1555 1.33
LINK C MSE C 140 N GLY C 141 1555 1555 1.33
LINK C ALA C 143 N MSE C 144 1555 1555 1.33
LINK C MSE C 144 N VAL C 145 1555 1555 1.33
LINK C PRO C 147 N MSE C 148 1555 1555 1.33
LINK C MSE C 148 N PRO C 149 1555 1555 1.33
LINK C MSE D 1 N LYS D 2 1555 1555 1.33
LINK C GLY D 6 N MSE D 7 1555 1555 1.33
LINK C MSE D 7 N THR D 8 1555 1555 1.32
LINK C GLU D 25 N MSE D 26 1555 1555 1.33
LINK C MSE D 26 N PRO D 27 1555 1555 1.34
LINK C VAL D 34 N MSE D 35 1555 1555 1.33
LINK C MSE D 35 N SER D 36 1555 1555 1.33
LINK C GLY D 80 N MSE D 81 1555 1555 1.33
LINK C MSE D 81 N ILE D 82 1555 1555 1.33
LINK C SER D 87 N MSE D 88 1555 1555 1.33
LINK C MSE D 88 N LYS D 89 1555 1555 1.33
LINK C GLU D 123 N MSE D 124 1555 1555 1.33
LINK C MSE D 124 N PRO D 125 1555 1555 1.34
LINK C ASN D 133 N MSE D 134 1555 1555 1.33
LINK C MSE D 134 N LEU D 135 1555 1555 1.33
LINK C ARG D 139 N MSE D 140 1555 1555 1.33
LINK C MSE D 140 N GLY D 141 1555 1555 1.33
LINK C ALA D 143 N MSE D 144 1555 1555 1.33
LINK C MSE D 144 N VAL D 145 1555 1555 1.33
LINK C PRO D 147 N MSE D 148 1555 1555 1.33
LINK C MSE D 148 N PRO D 149 1555 1555 1.34
CISPEP 1 ILE A 84 PRO A 85 0 -10.98
CISPEP 2 MSE A 124 PRO A 125 0 -8.24
CISPEP 3 ILE B 84 PRO B 85 0 -10.27
CISPEP 4 MSE B 124 PRO B 125 0 -7.53
CISPEP 5 ILE C 84 PRO C 85 0 -9.67
CISPEP 6 MSE C 124 PRO C 125 0 -10.33
CISPEP 7 ILE D 84 PRO D 85 0 -9.30
CISPEP 8 MSE D 124 PRO D 125 0 -9.48
SITE 1 AC1 18 THR A 8 GLY A 9 ALA A 10 THR A 11
SITE 2 AC1 18 SER A 36 SER A 87 MSE A 88 LYS A 89
SITE 3 AC1 18 THR A 90 ARG A 122 GLU A 123 HOH A1411
SITE 4 AC1 18 HOH A1414 HOH A1419 GLN D 67 ALA D 99
SITE 5 AC1 18 ARG D 105 HOH D1463
SITE 1 AC2 19 THR B 8 GLY B 9 ALA B 10 THR B 11
SITE 2 AC2 19 SER B 36 TRP B 38 GLN B 67 SER B 87
SITE 3 AC2 19 MSE B 88 LYS B 89 THR B 90 ALA B 99
SITE 4 AC2 19 ARG B 105 ARG B 122 GLU B 123 HOH B1408
SITE 5 AC2 19 HOH B1414 HOH B1422 HOH B1424
SITE 1 AC3 18 GLN A 67 ALA A 99 ARG A 105 THR C 8
SITE 2 AC3 18 GLY C 9 ALA C 10 THR C 11 SER C 36
SITE 3 AC3 18 SER C 87 MSE C 88 LYS C 89 THR C 90
SITE 4 AC3 18 ARG C 122 GLU C 123 HOH C1405 HOH C1413
SITE 5 AC3 18 HOH C1424 HOH C1429
SITE 1 AC4 19 GLN C 67 ALA C 99 ARG C 105 THR D 8
SITE 2 AC4 19 GLY D 9 ALA D 10 THR D 11 SER D 36
SITE 3 AC4 19 TRP D 38 SER D 87 MSE D 88 LYS D 89
SITE 4 AC4 19 THR D 90 ARG D 122 GLU D 123 HOH D1410
SITE 5 AC4 19 HOH D1414 HOH D1421 HOH D1425
CRYST1 95.372 95.372 217.538 90.00 90.00 120.00 H 3 36
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 0.010485 0.006054 0.000000 0.00000
SCALE2 0.000000 0.012107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004597 0.00000
HETATM 1 N MSE A 1 55.716 -17.711 46.813 1.00 45.71 N
HETATM 2 CA MSE A 1 55.526 -17.458 45.356 1.00 46.39 C
HETATM 3 C MSE A 1 56.588 -16.516 44.795 1.00 44.24 C
HETATM 4 O MSE A 1 56.884 -15.474 45.388 1.00 44.31 O
HETATM 5 CB MSE A 1 54.119 -16.906 45.087 1.00 46.16 C
HETATM 6 CG MSE A 1 53.840 -16.582 43.622 1.00 48.16 C
HETATM 7 SE MSE A 1 51.952 -16.736 43.117 1.00 52.05 SE
HETATM 8 CE MSE A 1 51.672 -18.675 43.463 1.00 50.88 C
(ATOM LINES ARE NOT SHOWN.)
END
