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HEADER HYDROLASE 14-FEB-22 7YWP
TITLE CLOSED CONFORMATION OF OLIGOPEPTIDASE B FROM SERRATIA PROTEOMACULANS
TITLE 2 WITH COVALENTLY BOUND TCK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGOPEPTIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.83;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA PROTEAMACULANS;
SOURCE 3 ORGANISM_TAXID: 28151;
SOURCE 4 GENE: OPDB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.PETRENKO,K.M.BOYKO,A.Y.NIKOLAEVA,A.V.VLASKINA,A.G.MIKHAILOVA,
AUTHOR 2 V.I.TIMOFEEV,T.V.RAKITINA
REVDAT 1 22-FEB-23 7YWP 0
JRNL AUTH D.E.PETRENKO,D.M.KARLINSKY,V.D.GORDEEVA,G.P.ARAPIDI,
JRNL AUTH 2 E.V.BRITIKOVA,V.V.BRITIKOV,A.Y.NIKOLAEVA,K.M.BOYKO,
JRNL AUTH 3 V.I.TIMOFEEV,I.P.KURANOVA,A.G.MIKHAILOVA,E.V.BOCHAROV,
JRNL AUTH 4 T.V.RAKITINA
JRNL TITL CRYSTAL STRUCTURE OF INHIBITOR-BOUND BACTERIAL
JRNL TITL 2 OLIGOPEPTIDASE B IN THE CLOSED STATE: SIMILARITY AND
JRNL TITL 3 DIFFERENCE BETWEEN PROTOZOAN AND BACTERIAL ENZYMES
JRNL REF INT J MOL SCI 2023
JRNL REFN ESSN 1422-0067
JRNL DOI 10.3390/IJMS24032286
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 35605
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1877
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2610
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5531
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 417
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.01000
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): 0.296
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.226
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5697 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5125 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7744 ; 1.566 ; 1.656
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11790 ; 1.257 ; 1.585
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 675 ; 7.807 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;33.703 ;22.422
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 922 ;16.747 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;18.611 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 704 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6555 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1404 ; 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 : 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 ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7YWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292121052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37524
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.140
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6952
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.27
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 7OB1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM LITHIUM SULFATE, 100 MM BIS
REMARK 280 -TRIS PH 5.5, 23% PEG 3350, VAPOR DIFFUSION, HANGING 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 37.76450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.32500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.83000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.32500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.76450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.83000
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 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: 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 OG SER A 532 C TCK A 701 1.88
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 1120 O HOH A 1188 4455 2.18
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 A 86 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 658 NE - CZ - NH2 ANGL. DEV. = -4.3 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 A 3 105.34 72.95
REMARK 500 ARG A 33 76.29 91.10
REMARK 500 THR A 34 24.54 -141.94
REMARK 500 SER A 108 -42.40 -140.22
REMARK 500 GLN A 123 -27.39 88.88
REMARK 500 SER A 149 5.58 114.90
REMARK 500 TYR A 199 -9.25 -141.74
REMARK 500 PHE A 264 -81.82 -86.29
REMARK 500 PHE A 293 150.36 72.96
REMARK 500 ASP A 302 118.39 -39.45
REMARK 500 ARG A 325 -61.91 -27.61
REMARK 500 GLN A 346 -72.81 -87.38
REMARK 500 THR A 359 58.61 -154.67
REMARK 500 ASP A 396 -4.01 76.37
REMARK 500 TYR A 452 -81.68 -129.53
REMARK 500 LEU A 498 -129.12 52.20
REMARK 500 SER A 532 -113.59 65.93
REMARK 500 VAL A 556 55.48 29.54
REMARK 500 ASP A 560 50.46 -91.01
REMARK 500 LEU A 572 -7.48 85.34
REMARK 500 GLU A 579 -68.57 -108.33
REMARK 500 SER A 596 106.99 -50.28
REMARK 500 ALA A 603 89.88 -68.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: N-[(1S)-5-AMINO-1-(CHLOROACETYL)PENTYL]-4-
REMARK 630 METHYLBENZENESULFONAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 TCK A 701
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: TSU LYS 0QE
REMARK 630 DETAILS: NULL
DBREF 7YWP A 2 677 UNP B3VI58 B3VI58_9GAMM 2 677
SEQRES 1 A 676 MET THR PRO PRO LYS ALA GLU LYS ARG PRO TYR PRO ILE
SEQRES 2 A 676 THR THR HIS GLY ASP THR ARG VAL ASP ASP TYR TYR TRP
SEQRES 3 A 676 LEU ARG ASP ASP GLU ARG THR ASP PRO GLN VAL LEU ASP
SEQRES 4 A 676 TYR LEU GLN ALA GLU ASN ALA PHE THR ASP ALA ALA LEU
SEQRES 5 A 676 LYS PRO GLN GLN ALA LEU ARG GLU THR LEU TYR GLU GLU
SEQRES 6 A 676 MET VAL ALA ARG ILE PRO GLN GLN GLU HIS SER VAL PRO
SEQRES 7 A 676 TYR VAL ARG HIS GLY TYR ARG TYR GLN THR ARG PHE GLU
SEQRES 8 A 676 PRO GLY ASN GLU TYR ALA ILE TYR VAL ARG GLN PRO GLN
SEQRES 9 A 676 ALA GLU SER GLU HIS TRP ASP THR LEU ILE ASP GLY ASN
SEQRES 10 A 676 GLN ARG ALA GLU GLN ARG GLU PHE TYR THR LEU GLY GLY
SEQRES 11 A 676 LEU GLU VAL SER PRO ASP ASN GLN LYS LEU ALA VAL ALA
SEQRES 12 A 676 GLU ASP PHE LEU SER ARG ARG GLN TYR ASP ILE ARG PHE
SEQRES 13 A 676 LYS ASN LEU SER ASP ASP SER TRP THR ASP GLU VAL LEU
SEQRES 14 A 676 GLU ASN THR SER GLY SER PHE GLU TRP ALA ASN ASP SER
SEQRES 15 A 676 ALA THR VAL TYR TYR VAL ARG LYS HIS ALA LYS THR LEU
SEQRES 16 A 676 LEU PRO TYR GLN VAL TYR ARG HIS VAL VAL GLY THR ASP
SEQRES 17 A 676 PRO GLN LEU ASP GLU LEU ILE TYR GLU GLU GLN ASP ASP
SEQRES 18 A 676 THR PHE TYR VAL GLY LEU GLU LYS THR THR SER ASP ARG
SEQRES 19 A 676 PHE ILE LEU ILE HIS LEU SER SER THR THR THR SER GLU
SEQRES 20 A 676 ILE LEU LEU LEU ASP ALA ASP ARG ALA ASP SER THR PRO
SEQRES 21 A 676 GLN MET PHE VAL PRO ARG ARG LYS ASP HIS GLU TYR GLY
SEQRES 22 A 676 ILE ASP HIS TYR HIS GLN HIS PHE TYR ILE ARG SER ASN
SEQRES 23 A 676 LYS ASP GLY LYS ASN PHE GLY LEU TYR GLN SER GLU GLN
SEQRES 24 A 676 ALA ASP GLU ALA GLN TRP GLN THR LEU ILE ALA PRO ARG
SEQRES 25 A 676 ILE GLU VAL MET LEU GLU GLY PHE SER LEU PHE ARG ASP
SEQRES 26 A 676 TRP LEU VAL VAL GLU GLU ARG SER GLU GLY LEU THR GLN
SEQRES 27 A 676 LEU ARG GLN ILE HIS TRP GLN SER GLY GLU VAL LYS ARG
SEQRES 28 A 676 ILE ALA PHE ASP ASP PRO THR TYR THR THR TRP LEU ALA
SEQRES 29 A 676 TYR ASN PRO GLU PRO GLU THR GLU LEU LEU ARG TYR GLY
SEQRES 30 A 676 TYR SER SER MET THR THR PRO THR THR LEU TYR GLU LEU
SEQRES 31 A 676 ASN LEU ASP SER ASP GLU ARG VAL MET LEU LYS GLN GLN
SEQRES 32 A 676 GLU VAL LYS ASN PHE THR PRO GLU ASN TYR ARG SER GLU
SEQRES 33 A 676 ARG VAL TRP VAL LYS ALA ARG ASP GLY VAL GLU VAL PRO
SEQRES 34 A 676 VAL SER LEU VAL TYR ARG HIS ASP SER PHE ALA ARG GLY
SEQRES 35 A 676 THR ASN PRO LEU MET VAL TYR GLY TYR GLY SER TYR GLY
SEQRES 36 A 676 SER SER MET ASP PRO ALA PHE SER ALA SER ARG LEU SER
SEQRES 37 A 676 LEU LEU ASP ARG GLY PHE VAL PHE VAL LEU ALA HIS ILE
SEQRES 38 A 676 ARG GLY GLY GLY GLU LEU GLY GLN LEU TRP TYR GLU ASP
SEQRES 39 A 676 GLY LYS LEU PHE LYS LYS GLN ASN THR PHE ASN ASP PHE
SEQRES 40 A 676 ILE ASP VAL THR GLU ALA LEU ILE ALA GLN GLY TYR GLY
SEQRES 41 A 676 ASP ALA LYS ARG VAL PHE ALA MET GLY GLY SER ALA GLY
SEQRES 42 A 676 GLY LEU LEU MET GLY ALA VAL ILE ASN GLN ALA PRO GLU
SEQRES 43 A 676 LEU PHE ASN GLY ILE VAL ALA GLN VAL PRO PHE VAL ASP
SEQRES 44 A 676 VAL VAL THR THR MET LEU ASP GLU SER ILE PRO LEU THR
SEQRES 45 A 676 THR GLY GLU TYR ASP GLU TRP GLY ASN PRO ASN GLN GLN
SEQRES 46 A 676 ALA TYR TYR ASP TYR ILE LEU GLN TYR SER PRO TYR ASP
SEQRES 47 A 676 GLN VAL LYS ALA GLN ASP TYR PRO HIS MET LEU VAL THR
SEQRES 48 A 676 THR GLY LEU HIS ASP SER GLN VAL GLN TYR TRP GLU PRO
SEQRES 49 A 676 ALA LYS TRP VAL ALA LYS LEU ARG GLU LEU LYS THR ASP
SEQRES 50 A 676 ASP ARG GLN LEU LEU LEU TYR THR ASP MET ASP SER GLY
SEQRES 51 A 676 HIS GLY GLY LYS SER GLY ARG PHE LYS ALA TYR GLU ASP
SEQRES 52 A 676 ILE ALA LEU GLU TYR ALA PHE ILE LEU ALA LEU ALA GLU
HET TCK A 701 20
HETNAM TCK N-[(1S)-5-AMINO-1-(CHLOROACETYL)PENTYL]-4-
HETNAM 2 TCK METHYLBENZENESULFONAMIDE
HETSYN TCK TOS-LYS-CH2CL
FORMUL 2 TCK C14 H21 CL N2 O3 S
FORMUL 3 HOH *417(H2 O)
HELIX 1 AA1 TYR A 25 ARG A 29 5 5
HELIX 2 AA2 ASP A 35 LEU A 53 1 19
HELIX 3 AA3 GLN A 56 ARG A 70 1 15
HELIX 4 AA4 GLY A 117 GLU A 122 1 6
HELIX 5 AA5 ASP A 209 ASP A 213 5 5
HELIX 6 AA6 ASP A 302 TRP A 306 5 5
HELIX 7 AA7 THR A 410 GLU A 412 5 3
HELIX 8 AA8 ASP A 438 PHE A 440 5 3
HELIX 9 AA9 ARG A 467 ASP A 472 1 6
HELIX 10 AB1 GLY A 489 ASP A 495 1 7
HELIX 11 AB2 GLY A 496 LYS A 500 5 5
HELIX 12 AB3 LYS A 501 GLN A 518 1 18
HELIX 13 AB4 SER A 532 ALA A 545 1 14
HELIX 14 AB5 PRO A 546 PHE A 549 5 4
HELIX 15 AB6 ASP A 560 LEU A 566 1 7
HELIX 16 AB7 GLN A 585 GLN A 594 1 10
HELIX 17 AB8 SER A 596 VAL A 601 1 6
HELIX 18 AB9 TYR A 622 LYS A 636 1 15
HELIX 19 AC1 LYS A 660 ALA A 676 1 17
SHEET 1 AA1 2 TYR A 12 THR A 16 0
SHEET 2 AA1 2 ASP A 19 ASP A 23 -1 O ASP A 23 N TYR A 12
SHEET 1 AA2 3 GLU A 75 HIS A 76 0
SHEET 2 AA2 3 TYR A 85 PHE A 91 -1 O PHE A 91 N GLU A 75
SHEET 3 AA2 3 TYR A 80 ARG A 82 -1 N TYR A 80 O TYR A 87
SHEET 1 AA3 4 GLU A 75 HIS A 76 0
SHEET 2 AA3 4 TYR A 85 PHE A 91 -1 O PHE A 91 N GLU A 75
SHEET 3 AA3 4 ILE A 99 PRO A 104 -1 O ILE A 99 N ARG A 90
SHEET 4 AA3 4 ASP A 112 ASP A 116 -1 O ASP A 112 N ARG A 102
SHEET 1 AA4 4 THR A 128 VAL A 134 0
SHEET 2 AA4 4 LYS A 140 ASP A 146 -1 O ASP A 146 N THR A 128
SHEET 3 AA4 4 TYR A 153 ASN A 159 -1 O LYS A 158 N LEU A 141
SHEET 4 AA4 4 SER A 164 TRP A 165 -1 O SER A 164 N ASN A 159
SHEET 1 AA5 7 THR A 128 VAL A 134 0
SHEET 2 AA5 7 LYS A 140 ASP A 146 -1 O ASP A 146 N THR A 128
SHEET 3 AA5 7 TYR A 153 ASN A 159 -1 O LYS A 158 N LEU A 141
SHEET 4 AA5 7 LEU A 170 TRP A 179 -1 O LEU A 170 N ILE A 155
SHEET 5 AA5 7 THR A 185 LYS A 191 -1 O LYS A 191 N ASN A 172
SHEET 6 AA5 7 PRO A 198 VAL A 205 -1 O HIS A 204 N VAL A 186
SHEET 7 AA5 7 GLU A 214 GLU A 218 -1 O ILE A 216 N VAL A 201
SHEET 1 AA6 4 TYR A 225 LYS A 230 0
SHEET 2 AA6 4 PHE A 236 SER A 242 -1 O SER A 242 N TYR A 225
SHEET 3 AA6 4 SER A 247 ASP A 253 -1 O GLU A 248 N LEU A 241
SHEET 4 AA6 4 GLN A 262 MET A 263 -1 O GLN A 262 N LEU A 251
SHEET 1 AA7 4 TYR A 273 TYR A 278 0
SHEET 2 AA7 4 HIS A 281 SER A 286 -1 O HIS A 281 N TYR A 278
SHEET 3 AA7 4 GLY A 294 SER A 298 -1 O TYR A 296 N ILE A 284
SHEET 4 AA7 4 GLN A 307 ILE A 310 -1 O LEU A 309 N LEU A 295
SHEET 1 AA8 4 MET A 317 LEU A 323 0
SHEET 2 AA8 4 TRP A 327 SER A 334 -1 O GLU A 331 N GLU A 319
SHEET 3 AA8 4 LEU A 337 HIS A 344 -1 O ARG A 341 N VAL A 330
SHEET 4 AA8 4 VAL A 350 ARG A 352 -1 O LYS A 351 N GLN A 342
SHEET 1 AA9 4 TYR A 360 LEU A 364 0
SHEET 2 AA9 4 LEU A 374 SER A 381 -1 O SER A 380 N THR A 361
SHEET 3 AA9 4 THR A 387 ASN A 392 -1 O THR A 387 N TYR A 379
SHEET 4 AA9 4 ARG A 398 GLN A 403 -1 O LYS A 402 N LEU A 388
SHEET 1 AB1 8 TYR A 414 LYS A 422 0
SHEET 2 AB1 8 GLU A 428 ARG A 436 -1 O VAL A 429 N VAL A 421
SHEET 3 AB1 8 VAL A 476 ALA A 480 -1 O LEU A 479 N SER A 432
SHEET 4 AB1 8 LEU A 447 TYR A 450 1 N TYR A 450 O VAL A 478
SHEET 5 AB1 8 VAL A 526 GLY A 531 1 O PHE A 527 N VAL A 449
SHEET 6 AB1 8 GLY A 551 GLN A 555 1 O GLN A 555 N GLY A 530
SHEET 7 AB1 8 HIS A 608 GLY A 614 1 O LEU A 610 N ALA A 554
SHEET 8 AB1 8 LEU A 642 ASP A 647 1 O LEU A 643 N VAL A 611
LINK NE2 HIS A 652 CM TCK A 701 1555 1555 1.47
CRYST1 75.529 89.660 108.650 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 0.013240 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011153 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009204 0.00000
TER 5532 GLU A 677
MASTER 338 0 1 19 44 0 0 6 5968 1 21 52
END |