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HEADER HYDROLASE 15-FEB-22 7YX7
TITLE MODIFIED OLIGOPEPTIDASE B FROM S. PROTEOMACULANS IN INTERMEDIATE
TITLE 2 CONFORMATION WITH 1 SPERMINE MOLECULE AT 1.72 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGOPEPTIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 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 18-JAN-23 7YX7 0
JRNL AUTH V.V.BRITIKOV,V.I.TIMOFEEV,D.E.PETRENKO,E.V.BRITIKOVA,
JRNL AUTH 2 A.Y.NIKOLAEVA,A.V.VLASKINA,K.M.BOYKO,A.G.MIKHAILOVA,
JRNL AUTH 3 T.V.RAKITINA
JRNL TITL ELUCIDATION OF THE CONFORMATIONAL TRANSITION OF
JRNL TITL 2 OLIGOPEPTIDASE B BY AN INTEGRATIVE APPROACH BASED ON THE
JRNL TITL 3 COMBINATION OF X-RAY, SAXS, AND ESSENTIAL DYNAMICS SAMPLING
JRNL TITL 4 SIMULATION
JRNL REF CRYSTALS V. 12 2022
JRNL REFN ESSN 2073-4352
JRNL DOI 10.3390/CRYST12050712
REMARK 2
REMARK 2 RESOLUTION. 1.72 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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 74858
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3960
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) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5788
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 330
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5545
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 607
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
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): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.298
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5743 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5173 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7806 ; 1.634 ; 1.652
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11903 ; 1.427 ; 1.580
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 684 ; 7.284 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 356 ;31.875 ;22.360
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 932 ;14.985 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;20.064 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 707 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6616 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1420 ; 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 7YX7 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_1292121100.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-19
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 : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78927
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 30.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 200 DATA REDUNDANCY : 4.290
REMARK 200 R MERGE (I) : 0.17300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.3372
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.67
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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 (%): 51.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM LITHIUM SULFATE, 100 MM BIS
REMARK 280 -TRIS PH 5.5, 23% PEG 3350, COUNTER-DIFFUSION, 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 36.47500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.44000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.26500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.44000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.47500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.26500
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 OH TYR A 455 OE2 GLU A 576 2.12
REMARK 500 O HOH A 1162 O HOH A 1370 2.15
REMARK 500 O HOH A 966 O HOH A 1091 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1413 O HOH A 1469 2555 2.19
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 SER A 149 3.46 86.29
REMARK 500 LYS A 194 -64.81 -178.64
REMARK 500 TYR A 199 -14.67 -150.70
REMARK 500 PHE A 264 -91.23 -90.16
REMARK 500 PHE A 293 148.51 73.11
REMARK 500 ASP A 302 107.01 -42.33
REMARK 500 ALA A 365 -157.50 -96.92
REMARK 500 TYR A 452 -85.27 -126.13
REMARK 500 LEU A 498 -125.39 53.49
REMARK 500 SER A 532 -113.89 62.57
REMARK 500 VAL A 556 57.94 30.47
REMARK 500 ASP A 560 54.70 -92.93
REMARK 500 LEU A 572 -31.19 83.76
REMARK 500 GLU A 579 -62.39 -97.41
REMARK 500 SER A 596 105.42 -45.29
REMARK 500 SER A 618 145.77 -178.08
REMARK 500 HIS A 652 -167.50 -106.85
REMARK 500 LYS A 655 -6.17 77.13
REMARK 500 SER A 656 -48.03 176.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1507 DISTANCE = 6.46 ANGSTROMS
DBREF 7YX7 A 2 677 UNP B3VI58 B3VI58_9GAMM 2 677
SEQADV 7YX7 HIS A 1 UNP B3VI58 EXPRESSION TAG
SEQADV 7YX7 GLU A 71 UNP B3VI58 ILE 71 ENGINEERED MUTATION
SEQADV 7YX7 ASN A 72 UNP B3VI58 PRO 72 ENGINEERED MUTATION
SEQADV 7YX7 LEU A 73 UNP B3VI58 GLN 73 ENGINEERED MUTATION
SEQADV 7YX7 TYR A 74 UNP B3VI58 GLN 74 ENGINEERED MUTATION
SEQADV 7YX7 PHE A 75 UNP B3VI58 GLU 75 ENGINEERED MUTATION
SEQADV 7YX7 GLN A 76 UNP B3VI58 HIS 76 ENGINEERED MUTATION
SEQRES 1 A 677 HIS MET THR PRO PRO LYS ALA GLU LYS ARG PRO TYR PRO
SEQRES 2 A 677 ILE THR THR HIS GLY ASP THR ARG VAL ASP ASP TYR TYR
SEQRES 3 A 677 TRP LEU ARG ASP ASP GLU ARG THR ASP PRO GLN VAL LEU
SEQRES 4 A 677 ASP TYR LEU GLN ALA GLU ASN ALA PHE THR ASP ALA ALA
SEQRES 5 A 677 LEU LYS PRO GLN GLN ALA LEU ARG GLU THR LEU TYR GLU
SEQRES 6 A 677 GLU MET VAL ALA ARG GLU ASN LEU TYR PHE GLN SER VAL
SEQRES 7 A 677 PRO TYR VAL ARG HIS GLY TYR ARG TYR GLN THR ARG PHE
SEQRES 8 A 677 GLU PRO GLY ASN GLU TYR ALA ILE TYR VAL ARG GLN PRO
SEQRES 9 A 677 GLN ALA GLU SER GLU HIS TRP ASP THR LEU ILE ASP GLY
SEQRES 10 A 677 ASN GLN ARG ALA GLU GLN ARG GLU PHE TYR THR LEU GLY
SEQRES 11 A 677 GLY LEU GLU VAL SER PRO ASP ASN GLN LYS LEU ALA VAL
SEQRES 12 A 677 ALA GLU ASP PHE LEU SER ARG ARG GLN TYR ASP ILE ARG
SEQRES 13 A 677 PHE LYS ASN LEU SER ASP ASP SER TRP THR ASP GLU VAL
SEQRES 14 A 677 LEU GLU ASN THR SER GLY SER PHE GLU TRP ALA ASN ASP
SEQRES 15 A 677 SER ALA THR VAL TYR TYR VAL ARG LYS HIS ALA LYS THR
SEQRES 16 A 677 LEU LEU PRO TYR GLN VAL TYR ARG HIS VAL VAL GLY THR
SEQRES 17 A 677 ASP PRO GLN LEU ASP GLU LEU ILE TYR GLU GLU GLN ASP
SEQRES 18 A 677 ASP THR PHE TYR VAL GLY LEU GLU LYS THR THR SER ASP
SEQRES 19 A 677 ARG PHE ILE LEU ILE HIS LEU SER SER THR THR THR SER
SEQRES 20 A 677 GLU ILE LEU LEU LEU ASP ALA ASP ARG ALA ASP SER THR
SEQRES 21 A 677 PRO GLN MET PHE VAL PRO ARG ARG LYS ASP HIS GLU TYR
SEQRES 22 A 677 GLY ILE ASP HIS TYR HIS GLN HIS PHE TYR ILE ARG SER
SEQRES 23 A 677 ASN LYS ASP GLY LYS ASN PHE GLY LEU TYR GLN SER GLU
SEQRES 24 A 677 GLN ALA ASP GLU ALA GLN TRP GLN THR LEU ILE ALA PRO
SEQRES 25 A 677 ARG ILE GLU VAL MET LEU GLU GLY PHE SER LEU PHE ARG
SEQRES 26 A 677 ASP TRP LEU VAL VAL GLU GLU ARG SER GLU GLY LEU THR
SEQRES 27 A 677 GLN LEU ARG GLN ILE HIS TRP GLN SER GLY GLU VAL LYS
SEQRES 28 A 677 ARG ILE ALA PHE ASP ASP PRO THR TYR THR THR TRP LEU
SEQRES 29 A 677 ALA TYR ASN PRO GLU PRO GLU THR GLU LEU LEU ARG TYR
SEQRES 30 A 677 GLY TYR SER SER MET THR THR PRO THR THR LEU TYR GLU
SEQRES 31 A 677 LEU ASN LEU ASP SER ASP GLU ARG VAL MET LEU LYS GLN
SEQRES 32 A 677 GLN GLU VAL LYS ASN PHE THR PRO GLU ASN TYR ARG SER
SEQRES 33 A 677 GLU ARG VAL TRP VAL LYS ALA ARG ASP GLY VAL GLU VAL
SEQRES 34 A 677 PRO VAL SER LEU VAL TYR ARG HIS ASP SER PHE ALA ARG
SEQRES 35 A 677 GLY THR ASN PRO LEU MET VAL TYR GLY TYR GLY SER TYR
SEQRES 36 A 677 GLY SER SER MET ASP PRO ALA PHE SER ALA SER ARG LEU
SEQRES 37 A 677 SER LEU LEU ASP ARG GLY PHE VAL PHE VAL LEU ALA HIS
SEQRES 38 A 677 ILE ARG GLY GLY GLY GLU LEU GLY GLN LEU TRP TYR GLU
SEQRES 39 A 677 ASP GLY LYS LEU PHE LYS LYS GLN ASN THR PHE ASN ASP
SEQRES 40 A 677 PHE ILE ASP VAL THR GLU ALA LEU ILE ALA GLN GLY TYR
SEQRES 41 A 677 GLY ASP ALA LYS ARG VAL PHE ALA MET GLY GLY SER ALA
SEQRES 42 A 677 GLY GLY LEU LEU MET GLY ALA VAL ILE ASN GLN ALA PRO
SEQRES 43 A 677 GLU LEU PHE ASN GLY ILE VAL ALA GLN VAL PRO PHE VAL
SEQRES 44 A 677 ASP VAL VAL THR THR MET LEU ASP GLU SER ILE PRO LEU
SEQRES 45 A 677 THR THR GLY GLU TYR ASP GLU TRP GLY ASN PRO ASN GLN
SEQRES 46 A 677 GLN ALA TYR TYR ASP TYR ILE LEU GLN TYR SER PRO TYR
SEQRES 47 A 677 ASP GLN VAL LYS ALA GLN ASP TYR PRO HIS MET LEU VAL
SEQRES 48 A 677 THR THR GLY LEU HIS ASP SER GLN VAL GLN TYR TRP GLU
SEQRES 49 A 677 PRO ALA LYS TRP VAL ALA LYS LEU ARG GLU LEU LYS THR
SEQRES 50 A 677 ASP ASP ARG GLN LEU LEU LEU TYR THR ASP MET ASP SER
SEQRES 51 A 677 GLY HIS GLY GLY LYS SER GLY ARG PHE LYS ALA TYR GLU
SEQRES 52 A 677 ASP ILE ALA LEU GLU TYR ALA PHE ILE LEU ALA LEU ALA
SEQRES 53 A 677 GLU
HET SPM A 801 14
HETNAM SPM SPERMINE
FORMUL 2 SPM C10 H26 N4
FORMUL 3 HOH *607(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 ASP A 560 LEU A 566 1 7
HELIX 15 AB6 LEU A 572 GLU A 576 5 5
HELIX 16 AB7 GLN A 585 SER A 596 1 12
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 GLY A 657 GLU A 677 1 21
SHEET 1 AA1 2 TYR A 12 THR A 16 0
SHEET 2 AA1 2 ASP A 19 ASP A 23 -1 O ARG A 21 N ILE A 14
SHEET 1 AA2 3 PHE A 75 GLN A 76 0
SHEET 2 AA2 3 TYR A 85 PHE A 91 -1 O PHE A 91 N PHE 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 PHE A 75 GLN A 76 0
SHEET 2 AA3 4 TYR A 85 PHE A 91 -1 O PHE A 91 N PHE A 75
SHEET 3 AA3 4 ILE A 99 PRO A 104 -1 O GLN A 103 N ARG A 86
SHEET 4 AA3 4 ASP A 112 ASP A 116 -1 O ASP A 112 N ARG A 102
SHEET 1 AA4 7 THR A 128 VAL A 134 0
SHEET 2 AA4 7 LYS A 140 ASP A 146 -1 O ALA A 144 N GLY A 130
SHEET 3 AA4 7 TYR A 153 ASN A 159 -1 O ASP A 154 N GLU A 145
SHEET 4 AA4 7 LEU A 170 TRP A 179 -1 O THR A 173 N TYR A 153
SHEET 5 AA4 7 THR A 185 LYS A 191 -1 O TYR A 187 N GLU A 178
SHEET 6 AA4 7 PRO A 198 VAL A 205 -1 O HIS A 204 N VAL A 186
SHEET 7 AA4 7 GLU A 214 GLU A 218 -1 O ILE A 216 N VAL A 201
SHEET 1 AA5 4 TYR A 225 LYS A 230 0
SHEET 2 AA5 4 PHE A 236 SER A 242 -1 O HIS A 240 N GLY A 227
SHEET 3 AA5 4 SER A 247 ASP A 253 -1 O LEU A 252 N ILE A 237
SHEET 4 AA5 4 GLN A 262 MET A 263 -1 O GLN A 262 N LEU A 251
SHEET 1 AA6 4 TYR A 273 TYR A 278 0
SHEET 2 AA6 4 HIS A 281 SER A 286 -1 O TYR A 283 N ASP A 276
SHEET 3 AA6 4 GLY A 294 SER A 298 -1 O SER A 298 N PHE A 282
SHEET 4 AA6 4 GLN A 307 ILE A 310 -1 O GLN A 307 N GLN A 297
SHEET 1 AA7 4 MET A 317 LEU A 323 0
SHEET 2 AA7 4 TRP A 327 SER A 334 -1 O ARG A 333 N MET A 317
SHEET 3 AA7 4 LEU A 337 HIS A 344 -1 O ILE A 343 N LEU A 328
SHEET 4 AA7 4 VAL A 350 ARG A 352 -1 O LYS A 351 N GLN A 342
SHEET 1 AA8 4 TYR A 360 LEU A 364 0
SHEET 2 AA8 4 LEU A 374 SER A 381 -1 O SER A 380 N THR A 361
SHEET 3 AA8 4 THR A 387 ASN A 392 -1 O LEU A 391 N LEU A 375
SHEET 4 AA8 4 ARG A 398 GLN A 403 -1 O VAL A 399 N GLU A 390
SHEET 1 AA9 8 TYR A 414 LYS A 422 0
SHEET 2 AA9 8 GLU A 428 ARG A 436 -1 O VAL A 429 N VAL A 421
SHEET 3 AA9 8 VAL A 476 ALA A 480 -1 O LEU A 479 N SER A 432
SHEET 4 AA9 8 LEU A 447 TYR A 450 1 N TYR A 450 O VAL A 478
SHEET 5 AA9 8 VAL A 526 GLY A 531 1 O PHE A 527 N LEU A 447
SHEET 6 AA9 8 GLY A 551 GLN A 555 1 O GLN A 555 N GLY A 530
SHEET 7 AA9 8 HIS A 608 GLY A 614 1 O LEU A 610 N ALA A 554
SHEET 8 AA9 8 LEU A 642 ASP A 647 1 O LEU A 643 N VAL A 611
CRYST1 72.950 100.530 108.880 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 0.013708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009184 0.00000
TER 5581 GLU A 677
MASTER 314 0 1 19 40 0 0 6 6166 1 14 53
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