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HEADER UNKNOWN FUNCTION 26-JUN-02 1M33
TITLE CRYSTAL STRUCTURE OF BIOH AT 1.7 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIOH PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: BIOH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ALPHA-BETTA-ALPHA SANDWICH
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SANISHVILI,A.SAVCHENKO,T.SKARINA,A.EDWARDS,A.JOACHIMIAK,
AUTHOR 2 A.YAKUNIN
REVDAT 1 21-JAN-03 1M33 0
JRNL AUTH R.SANISHVILI,A.SAVCHENKO,T.SKARINA,A.EDWARDS,
JRNL AUTH 2 A.JOACHIMIAK,A.YAKUNIN
JRNL TITL 1.7 A CRYSTAL STRUCTURE OF BIOH PROTEIN LEADS TO
JRNL TITL 2 DISCOVERY OF ITS FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.05
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 74.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 27141
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1422
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3631
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 175
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2419
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.30000
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): 0.099
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.933
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2327 ; 0.022 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2174 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3158 ; 1.941 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5079 ; 2.329 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 276 ; 6.629 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 455 ;19.565 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.143 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2551 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 468 ; 0.009 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 539 ; 0.286 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2506 ; 0.268 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1273 ; 0.098 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 144 ; 0.196 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 17 ; 0.300 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 59 ; 0.293 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.142 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 1373 ; 1.107 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2248 ; 1.791 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 954 ; 2.650 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 910 ; 3.961 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 109
REMARK 3 RESIDUE RANGE : A 188 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9707 10.8230 14.3217
REMARK 3 T TENSOR
REMARK 3 T11: 0.0210 T22: 0.0190
REMARK 3 T33: 0.0393 T12: 0.0147
REMARK 3 T13: 0.0092 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.5960 L22: 2.1184
REMARK 3 L33: 1.7319 L12: -0.2217
REMARK 3 L13: 0.2992 L23: -0.0851
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: 0.0109 S13: 0.0518
REMARK 3 S21: 0.0451 S22: -0.0312 S23: 0.0583
REMARK 3 S31: -0.0046 S32: -0.0260 S33: 0.0133
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 110 A 187
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4722 2.5709 11.6658
REMARK 3 T TENSOR
REMARK 3 T11: 0.1338 T22: 0.1620
REMARK 3 T33: 0.1404 T12: 0.0224
REMARK 3 T13: -0.0063 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.9386 L22: 1.3232
REMARK 3 L33: 1.1053 L12: -0.4449
REMARK 3 L13: -0.1438 L23: -0.4501
REMARK 3 S TENSOR
REMARK 3 S11: 0.0483 S12: 0.2257 S13: -0.0386
REMARK 3 S21: -0.1064 S22: -0.0571 S23: -0.3146
REMARK 3 S31: 0.0521 S32: 0.3817 S33: 0.0088
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 999
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4028 9.3391 13.2230
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.1592
REMARK 3 T33: 0.1408 T12: 0.0069
REMARK 3 T13: -0.0114 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 1.6269 L22: 1.8027
REMARK 3 L33: 1.4051 L12: -0.3573
REMARK 3 L13: 0.0707 L23: -0.1525
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.0193 S13: 0.0915
REMARK 3 S21: 0.0099 S22: -0.0147 S23: -0.0578
REMARK 3 S31: -0.0585 S32: 0.0426 S33: -0.0086
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1M33 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-2002.
REMARK 100 THE RCSB ID CODE IS RCSB016536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979464, 0.953732, 1.03321
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSING SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : SAGITALLY FOCUSING
REMARK 200 MONOCHROMATOR, VERTICALLY
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DTCOLLECT, DTDISPLAY
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33538
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.59500
REMARK 200 FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M TRI NA CITRATE, 0.1M TRIS, 15%
REMARK 280 ETHYLENE GLYCOL, PH 8.8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 -Y,X,3/4+Z
REMARK 290 4555 Y,-X,1/4+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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 24.62800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.94200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.31400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 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 MSE A 1
REMARK 465 ASN A 2
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 GLU A 116 CG CD OE1 OE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 ASP A 123 OD1 OD2
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
REMARK 500 NE2 GLN A 137 CE MSE A 170 2.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ILE A 4 CG2 ILE A 4 CB -0.137
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 82 -118.33 62.09
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 191 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH 218 DISTANCE = 6.70 ANGSTROMS
DBREF 1M33 A 1 256 SWS P13001 BIOH_ECOLI 1 256
SEQADV 1M33 MSE A 1 SWS P13001 MET 1 MODIFIED RESIDUE
SEQADV 1M33 MSE A 64 SWS P13001 MET 64 MODIFIED RESIDUE
SEQADV 1M33 ARG A 100 SWS P13001 GLN 100 CONFLICT
SEQADV 1M33 GLN A 136 SWS P13001 PHE 136 CONFLICT
SEQADV 1M33 TRP A 143 SWS P13001 PHE 143 CONFLICT
SEQADV 1M33 MSE A 149 SWS P13001 MET 149 MODIFIED RESIDUE
SEQADV 1M33 ARG A 162 SWS P13001 LYS 162 CONFLICT
SEQADV 1M33 MSE A 170 SWS P13001 MET 170 MODIFIED RESIDUE
SEQADV 1M33 MSE A 197 SWS P13001 MET 197 MODIFIED RESIDUE
SEQADV 1M33 MSE A 217 SWS P13001 MET 217 MODIFIED RESIDUE
SEQADV 1M33 GLY A 257 SWS P13001 INSERTION
SEQADV 1M33 SER A 258 SWS P13001 INSERTION
SEQRES 1 A 258 MSE ASN ASN ILE TRP TRP GLN THR LYS GLY GLN GLY ASN
SEQRES 2 A 258 VAL HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 A 258 GLU VAL TRP ARG CYS ILE ASP GLU GLU LEU SER SER HIS
SEQRES 4 A 258 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY PHE GLY ARG
SEQRES 5 A 258 SER ARG GLY PHE GLY ALA LEU SER LEU ALA ASP MSE ALA
SEQRES 6 A 258 GLU ALA VAL LEU GLN GLN ALA PRO ASP LYS ALA ILE TRP
SEQRES 7 A 258 LEU GLY TRP SER LEU GLY GLY LEU VAL ALA SER GLN ILE
SEQRES 8 A 258 ALA LEU THR HIS PRO GLU ARG VAL ARG ALA LEU VAL THR
SEQRES 9 A 258 VAL ALA SER SER PRO CYS PHE SER ALA ARG ASP GLU TRP
SEQRES 10 A 258 PRO GLY ILE LYS PRO ASP VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 A 258 GLN LEU SER ASP ASP GLN GLN ARG THR VAL GLU ARG PHE
SEQRES 12 A 258 LEU ALA LEU GLN THR MSE GLY THR GLU THR ALA ARG GLN
SEQRES 13 A 258 ASP ALA ARG ALA LEU LYS LYS THR VAL LEU ALA LEU PRO
SEQRES 14 A 258 MSE PRO GLU VAL ASP VAL LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 A 258 LEU LYS THR VAL ASP LEU ARG GLN PRO LEU GLN ASN VAL
SEQRES 16 A 258 SER MSE PRO PHE LEU ARG LEU TYR GLY TYR LEU ASP GLY
SEQRES 17 A 258 LEU VAL PRO ARG LYS VAL VAL PRO MSE LEU ASP LYS LEU
SEQRES 18 A 258 TRP PRO HIS SER GLU SER TYR ILE PHE ALA LYS ALA ALA
SEQRES 19 A 258 HIS ALA PRO PHE ILE SER HIS PRO ALA GLU PHE CYS HIS
SEQRES 20 A 258 LEU LEU VAL ALA LEU LYS GLN ARG VAL GLY SER
MODRES 1M33 MSE A 64 MET SELENOMETHIONINE
MODRES 1M33 MSE A 149 MET SELENOMETHIONINE
MODRES 1M33 MSE A 170 MET SELENOMETHIONINE
MODRES 1M33 MSE A 197 MET SELENOMETHIONINE
MODRES 1M33 MSE A 217 MET SELENOMETHIONINE
HET MSE A 64 8
HET MSE A 149 12
HET MSE A 170 12
HET MSE A 197 11
HET MSE A 217 12
HET 3OH A 300 12
HET EGL 301 4
HET EGL 302 8
HETNAM MSE SELENOMETHIONINE
HETNAM 3OH 3-HYDROXY-PROPANOIC ACID
HETNAM EGL ETHYLENE GLYCOL
FORMUL 1 MSE 5(C5 H11 N1 O2 SE1)
FORMUL 2 3OH C3 H6 O3
FORMUL 3 EGL 2(C2 H6 O2)
FORMUL 5 HOH *238(H2 O1)
HELIX 1 1 ASN A 25 CYS A 31 5 7
HELIX 2 2 ILE A 32 SER A 38 1 7
HELIX 3 3 SER A 60 GLN A 70 1 11
HELIX 4 4 SER A 82 HIS A 95 1 14
HELIX 5 5 LYS A 121 ARG A 142 1 22
HELIX 6 6 LEU A 144 THR A 148 5 5
HELIX 7 7 THR A 153 LEU A 161 1 9
HELIX 8 8 LYS A 163 VAL A 165 5 3
HELIX 9 9 GLU A 172 VAL A 186 1 15
HELIX 10 10 GLN A 190 VAL A 195 5 6
HELIX 11 11 LYS A 213 TRP A 222 1 10
HELIX 12 12 ALA A 236 HIS A 241 1 6
HELIX 13 13 HIS A 241 GLN A 254 1 14
SHEET 1 A 7 TRP A 6 LYS A 9 0
SHEET 2 A 7 THR A 41 VAL A 45 -1 O LEU A 44 N GLN A 7
SHEET 3 A 7 HIS A 15 LEU A 19 1 N LEU A 18 O HIS A 43
SHEET 4 A 7 ALA A 76 TRP A 81 1 O TRP A 81 N LEU A 19
SHEET 5 A 7 VAL A 99 VAL A 105 1 O VAL A 103 N TRP A 78
SHEET 6 A 7 PHE A 199 GLY A 204 1 O LEU A 202 N THR A 104
SHEET 7 A 7 GLU A 226 PHE A 230 1 O PHE A 230 N TYR A 203
LINK OG SER A 82 C3 A3OH A 300
LINK OG SER A 82 C3 B3OH A 300
CRYST1 75.210 75.210 49.256 90.00 90.00 90.00 P 43 1
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 0.013296 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020302 0.00000
TER 2257 SER A 258
MASTER 340 0 8 13 7 0 0 6 2532 1 79 20
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