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HEADER HYDROLASE 15-JUL-16 5GMR
TITLE CRYSTAL STRUCTURE OF THE MUTANT M3+S202W/I203F OF THE ESTERASE E40
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: C, A, B, D;
COMPND 4 SYNONYM: ESTERASE E40;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-Z.ZHANG,P.-Y.LI
REVDAT 1 19-JUL-17 5GMR 0
JRNL AUTH Y.-Z.ZHANG,P.-Y.LI
JRNL TITL IMPROVING THE SALT-TOLERANCE OF AN ESTERASE BY INTRODUCING
JRNL TITL 2 HYDROPHOBIC INTERACTIONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.6
REMARK 3 NUMBER OF REFLECTIONS : 109130
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5350
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.0168 - 5.5727 0.98 3820 213 0.1514 0.1682
REMARK 3 2 5.5727 - 4.4251 0.97 3757 207 0.1395 0.1540
REMARK 3 3 4.4251 - 3.8662 0.97 3777 190 0.1400 0.1634
REMARK 3 4 3.8662 - 3.5130 0.97 3816 194 0.1524 0.1868
REMARK 3 5 3.5130 - 3.2613 0.98 3814 196 0.1658 0.1955
REMARK 3 6 3.2613 - 3.0691 0.97 3766 193 0.1673 0.2070
REMARK 3 7 3.0691 - 2.9154 0.96 3794 177 0.1682 0.2095
REMARK 3 8 2.9154 - 2.7886 0.96 3737 183 0.1709 0.2028
REMARK 3 9 2.7886 - 2.6812 0.95 3705 205 0.1612 0.2165
REMARK 3 10 2.6812 - 2.5887 0.95 3683 207 0.1708 0.2040
REMARK 3 11 2.5887 - 2.5078 0.94 3665 177 0.1605 0.2037
REMARK 3 12 2.5078 - 2.4361 0.94 3668 189 0.1644 0.1973
REMARK 3 13 2.4361 - 2.3720 0.93 3670 166 0.1555 0.1971
REMARK 3 14 2.3720 - 2.3141 0.93 3658 182 0.1571 0.2266
REMARK 3 15 2.3141 - 2.2615 0.91 3557 174 0.1611 0.1976
REMARK 3 16 2.2615 - 2.2134 0.92 3601 159 0.1615 0.2088
REMARK 3 17 2.2134 - 2.1691 0.90 3510 192 0.1586 0.2102
REMARK 3 18 2.1691 - 2.1282 0.89 3472 187 0.1746 0.2304
REMARK 3 19 2.1282 - 2.0902 0.88 3412 178 0.1868 0.2286
REMARK 3 20 2.0902 - 2.0548 0.87 3405 188 0.1787 0.2461
REMARK 3 21 2.0548 - 2.0216 0.86 3388 176 0.2039 0.2317
REMARK 3 22 2.0216 - 1.9905 0.85 3272 183 0.1973 0.2667
REMARK 3 23 1.9905 - 1.9612 0.82 3243 175 0.2046 0.2419
REMARK 3 24 1.9612 - 1.9336 0.82 3167 167 0.2038 0.2385
REMARK 3 25 1.9336 - 1.9075 0.80 3101 163 0.2197 0.2820
REMARK 3 26 1.9075 - 1.8827 0.79 3108 171 0.2225 0.2654
REMARK 3 27 1.8827 - 1.8592 0.78 2969 142 0.2381 0.2787
REMARK 3 28 1.8592 - 1.8368 0.75 3019 155 0.2508 0.3215
REMARK 3 29 1.8368 - 1.8154 0.74 2852 146 0.2572 0.3053
REMARK 3 30 1.8154 - 1.7950 0.61 2374 115 0.2557 0.2924
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 45.53
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.78590
REMARK 3 B22 (A**2) : 6.30240
REMARK 3 B33 (A**2) : -7.08830
REMARK 3 B12 (A**2) : 12.06680
REMARK 3 B13 (A**2) : 1.98100
REMARK 3 B23 (A**2) : 10.52260
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 9340
REMARK 3 ANGLE : 0.999 12738
REMARK 3 CHIRALITY : 0.067 1402
REMARK 3 PLANARITY : 0.005 1674
REMARK 3 DIHEDRAL : 11.849 3422
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0197 -53.5512 -25.7925
REMARK 3 T TENSOR
REMARK 3 T11: 0.1562 T22: 0.1572
REMARK 3 T33: 0.1606 T12: -0.0047
REMARK 3 T13: -0.0030 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.0123 L22: 0.0201
REMARK 3 L33: 0.0239 L12: -0.0073
REMARK 3 L13: -0.0317 L23: 0.0037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: 0.0037 S13: -0.0076
REMARK 3 S21: 0.0010 S22: -0.0008 S23: 0.0017
REMARK 3 S31: -0.0017 S32: -0.0028 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5GMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1300001080.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-14
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 : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118334
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.6130
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELXDE
REMARK 200 STARTING MODEL: 4XVC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SUCCINIC ACID (PH 6.5), 15% (W/V)
REMARK 280 PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
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 O HOH B 322 O HOH B 565 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 PRO C 21 102.37 -59.15
REMARK 500 SER C 147 -119.15 47.37
REMARK 500 ASP C 268 -0.30 68.38
REMARK 500 SER A 85 -177.00 -174.52
REMARK 500 SER A 147 -119.56 52.39
REMARK 500 SER B 85 -176.81 -176.93
REMARK 500 SER B 147 -124.55 53.26
REMARK 500 SER D 85 -173.37 -172.31
REMARK 500 SER D 147 -122.30 54.61
REMARK 500 ASP D 268 -3.88 70.29
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 C 628 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 644 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 645 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 646 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A 647 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 648 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH D 607 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH D 608 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH D 609 DISTANCE = 6.67 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GMS RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES ARG22-LYS23-THR24 OF E40 (UNIPROTKB - A0A0F6WGE1
REMARK 999 (A0A0F6WGE1_9BACT)) WERE REPLACED BY RESIDUES TYR22-LYS23-HIS24-
REMARK 999 LEU25-SER26 TO GENERATE THE MUTANT M3.
DBREF1 5GMR C 1 299 UNP A0A0F6WGE1_9BACT
DBREF2 5GMR C A0A0F6WGE1 1 297
DBREF1 5GMR A 1 299 UNP A0A0F6WGE1_9BACT
DBREF2 5GMR A A0A0F6WGE1 1 297
DBREF1 5GMR B 1 299 UNP A0A0F6WGE1_9BACT
DBREF2 5GMR B A0A0F6WGE1 1 297
DBREF1 5GMR D 1 299 UNP A0A0F6WGE1_9BACT
DBREF2 5GMR D A0A0F6WGE1 1 297
SEQADV 5GMR HIS C -15 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS C -14 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS C -13 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS C -12 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS C -11 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS C -10 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER C -9 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER C -8 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY C -7 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR LEU C -6 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR VAL C -5 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR PRO C -4 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR ARG C -3 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY C -2 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER C -1 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS C 0 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR TYR C 22 UNP A0A0F6WGE ARG 22 SEE SEQUENCE DETAILS
SEQADV 5GMR HIS C 24 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR LEU C 25 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR SER C 26 UNP A0A0F6WGE THR 24 SEE SEQUENCE DETAILS
SEQADV 5GMR TRP C 204 UNP A0A0F6WGE SER 202 ENGINEERED MUTATION
SEQADV 5GMR PHE C 205 UNP A0A0F6WGE ILE 203 ENGINEERED MUTATION
SEQADV 5GMR HIS A -15 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS A -14 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS A -13 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS A -12 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS A -11 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS A -10 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER A -9 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER A -8 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY A -7 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR LEU A -6 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR VAL A -5 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR PRO A -4 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR ARG A -3 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY A -2 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER A -1 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS A 0 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR TYR A 22 UNP A0A0F6WGE ARG 22 SEE SEQUENCE DETAILS
SEQADV 5GMR HIS A 24 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR LEU A 25 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR SER A 26 UNP A0A0F6WGE THR 24 SEE SEQUENCE DETAILS
SEQADV 5GMR TRP A 204 UNP A0A0F6WGE SER 202 ENGINEERED MUTATION
SEQADV 5GMR PHE A 205 UNP A0A0F6WGE ILE 203 ENGINEERED MUTATION
SEQADV 5GMR HIS B -15 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS B -14 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS B -13 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS B -12 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS B -11 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS B -10 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER B -9 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER B -8 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY B -7 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR LEU B -6 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR VAL B -5 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR PRO B -4 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR ARG B -3 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY B -2 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER B -1 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS B 0 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR TYR B 22 UNP A0A0F6WGE ARG 22 SEE SEQUENCE DETAILS
SEQADV 5GMR HIS B 24 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR LEU B 25 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR SER B 26 UNP A0A0F6WGE THR 24 SEE SEQUENCE DETAILS
SEQADV 5GMR TRP B 204 UNP A0A0F6WGE SER 202 ENGINEERED MUTATION
SEQADV 5GMR PHE B 205 UNP A0A0F6WGE ILE 203 ENGINEERED MUTATION
SEQADV 5GMR HIS D -15 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS D -14 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS D -13 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS D -12 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS D -11 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS D -10 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER D -9 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER D -8 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY D -7 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR LEU D -6 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR VAL D -5 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR PRO D -4 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR ARG D -3 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR GLY D -2 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR SER D -1 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR HIS D 0 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMR TYR D 22 UNP A0A0F6WGE ARG 22 SEE SEQUENCE DETAILS
SEQADV 5GMR HIS D 24 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR LEU D 25 UNP A0A0F6WGE SEE SEQUENCE DETAILS
SEQADV 5GMR SER D 26 UNP A0A0F6WGE THR 24 SEE SEQUENCE DETAILS
SEQADV 5GMR TRP D 204 UNP A0A0F6WGE SER 202 ENGINEERED MUTATION
SEQADV 5GMR PHE D 205 UNP A0A0F6WGE ILE 203 ENGINEERED MUTATION
SEQRES 1 C 315 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 C 315 GLY SER HIS MET ALA LYS SER PRO GLU LEU ASP ARG VAL
SEQRES 3 C 315 ILE GLY MET ILE ARG GLU ARG ALA ALA THR PRO TYR LYS
SEQRES 4 C 315 HIS LEU SER THR ASP ASP ASP ARG ARG LEU TYR GLU THR
SEQRES 5 C 315 MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE GLN THR
SEQRES 6 C 315 GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU TRP ILE
SEQRES 7 C 315 TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE LEU TYR
SEQRES 8 C 315 LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET ARG THR
SEQRES 9 C 315 HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA ALA GLY
SEQRES 10 C 315 CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA PRO GLU
SEQRES 11 C 315 THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL ALA ALA
SEQRES 12 C 315 TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO SER ARG
SEQRES 13 C 315 ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY LEU VAL
SEQRES 14 C 315 VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY GLU PRO
SEQRES 15 C 315 LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP ILE ASP
SEQRES 16 C 315 MET GLU ALA THR GLY GLU SER PHE THR THR ASN ALA THR
SEQRES 17 C 315 MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET TRP PHE
SEQRES 18 C 315 ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN ALA PRO
SEQRES 19 C 315 LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY LEU PRO
SEQRES 20 C 315 PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR LEU LEU
SEQRES 21 C 315 ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS ALA ALA
SEQRES 22 C 315 GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP MET PRO
SEQRES 23 C 315 HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO GLU GLY
SEQRES 24 C 315 LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU ARG LYS
SEQRES 25 C 315 GLN ILE GLY
SEQRES 1 A 315 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 315 GLY SER HIS MET ALA LYS SER PRO GLU LEU ASP ARG VAL
SEQRES 3 A 315 ILE GLY MET ILE ARG GLU ARG ALA ALA THR PRO TYR LYS
SEQRES 4 A 315 HIS LEU SER THR ASP ASP ASP ARG ARG LEU TYR GLU THR
SEQRES 5 A 315 MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE GLN THR
SEQRES 6 A 315 GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU TRP ILE
SEQRES 7 A 315 TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE LEU TYR
SEQRES 8 A 315 LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET ARG THR
SEQRES 9 A 315 HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA ALA GLY
SEQRES 10 A 315 CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA PRO GLU
SEQRES 11 A 315 THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL ALA ALA
SEQRES 12 A 315 TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO SER ARG
SEQRES 13 A 315 ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY LEU VAL
SEQRES 14 A 315 VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY GLU PRO
SEQRES 15 A 315 LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP ILE ASP
SEQRES 16 A 315 MET GLU ALA THR GLY GLU SER PHE THR THR ASN ALA THR
SEQRES 17 A 315 MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET TRP PHE
SEQRES 18 A 315 ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN ALA PRO
SEQRES 19 A 315 LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY LEU PRO
SEQRES 20 A 315 PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR LEU LEU
SEQRES 21 A 315 ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS ALA ALA
SEQRES 22 A 315 GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP MET PRO
SEQRES 23 A 315 HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO GLU GLY
SEQRES 24 A 315 LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU ARG LYS
SEQRES 25 A 315 GLN ILE GLY
SEQRES 1 B 315 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 B 315 GLY SER HIS MET ALA LYS SER PRO GLU LEU ASP ARG VAL
SEQRES 3 B 315 ILE GLY MET ILE ARG GLU ARG ALA ALA THR PRO TYR LYS
SEQRES 4 B 315 HIS LEU SER THR ASP ASP ASP ARG ARG LEU TYR GLU THR
SEQRES 5 B 315 MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE GLN THR
SEQRES 6 B 315 GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU TRP ILE
SEQRES 7 B 315 TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE LEU TYR
SEQRES 8 B 315 LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET ARG THR
SEQRES 9 B 315 HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA ALA GLY
SEQRES 10 B 315 CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA PRO GLU
SEQRES 11 B 315 THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL ALA ALA
SEQRES 12 B 315 TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO SER ARG
SEQRES 13 B 315 ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY LEU VAL
SEQRES 14 B 315 VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY GLU PRO
SEQRES 15 B 315 LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP ILE ASP
SEQRES 16 B 315 MET GLU ALA THR GLY GLU SER PHE THR THR ASN ALA THR
SEQRES 17 B 315 MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET TRP PHE
SEQRES 18 B 315 ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN ALA PRO
SEQRES 19 B 315 LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY LEU PRO
SEQRES 20 B 315 PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR LEU LEU
SEQRES 21 B 315 ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS ALA ALA
SEQRES 22 B 315 GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP MET PRO
SEQRES 23 B 315 HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO GLU GLY
SEQRES 24 B 315 LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU ARG LYS
SEQRES 25 B 315 GLN ILE GLY
SEQRES 1 D 315 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 D 315 GLY SER HIS MET ALA LYS SER PRO GLU LEU ASP ARG VAL
SEQRES 3 D 315 ILE GLY MET ILE ARG GLU ARG ALA ALA THR PRO TYR LYS
SEQRES 4 D 315 HIS LEU SER THR ASP ASP ASP ARG ARG LEU TYR GLU THR
SEQRES 5 D 315 MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE GLN THR
SEQRES 6 D 315 GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU TRP ILE
SEQRES 7 D 315 TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE LEU TYR
SEQRES 8 D 315 LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET ARG THR
SEQRES 9 D 315 HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA ALA GLY
SEQRES 10 D 315 CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA PRO GLU
SEQRES 11 D 315 THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL ALA ALA
SEQRES 12 D 315 TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO SER ARG
SEQRES 13 D 315 ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY LEU VAL
SEQRES 14 D 315 VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY GLU PRO
SEQRES 15 D 315 LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP ILE ASP
SEQRES 16 D 315 MET GLU ALA THR GLY GLU SER PHE THR THR ASN ALA THR
SEQRES 17 D 315 MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET TRP PHE
SEQRES 18 D 315 ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN ALA PRO
SEQRES 19 D 315 LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY LEU PRO
SEQRES 20 D 315 PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR LEU LEU
SEQRES 21 D 315 ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS ALA ALA
SEQRES 22 D 315 GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP MET PRO
SEQRES 23 D 315 HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO GLU GLY
SEQRES 24 D 315 LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU ARG LYS
SEQRES 25 D 315 GLN ILE GLY
FORMUL 5 HOH *1325(H2 O)
HELIX 1 AA1 SER C 4 THR C 20 1 17
HELIX 2 AA2 PRO C 21 LEU C 25 5 5
HELIX 3 AA3 SER C 26 GLY C 39 1 14
HELIX 4 AA4 SER C 85 GLY C 101 1 17
HELIX 5 AA5 PRO C 118 HIS C 134 1 17
HELIX 6 AA6 ASP C 137 SER C 139 5 3
HELIX 7 AA7 SER C 147 ILE C 163 1 17
HELIX 8 AA8 GLU C 185 ASN C 190 1 6
HELIX 9 AA9 ASN C 198 GLY C 211 1 14
HELIX 10 AB1 SER C 221 ALA C 225 5 5
HELIX 11 AB2 LEU C 243 ALA C 257 1 15
HELIX 12 AB3 VAL C 272 ALA C 277 5 6
HELIX 13 AB4 LEU C 280 GLY C 299 1 20
HELIX 14 AB5 SER A 4 THR A 20 1 17
HELIX 15 AB6 SER A 26 GLY A 39 1 14
HELIX 16 AB7 SER A 85 GLY A 101 1 17
HELIX 17 AB8 PRO A 118 HIS A 134 1 17
HELIX 18 AB9 ASP A 137 SER A 139 5 3
HELIX 19 AC1 SER A 147 ILE A 163 1 17
HELIX 20 AC2 GLU A 185 ASN A 190 1 6
HELIX 21 AC3 ASN A 198 GLY A 211 1 14
HELIX 22 AC4 SER A 221 ALA A 225 5 5
HELIX 23 AC5 LEU A 243 ALA A 257 1 15
HELIX 24 AC6 VAL A 272 ALA A 277 5 6
HELIX 25 AC7 LEU A 280 GLY A 299 1 20
HELIX 26 AC8 SER B 4 THR B 20 1 17
HELIX 27 AC9 PRO B 21 LEU B 25 5 5
HELIX 28 AD1 SER B 26 GLY B 39 1 14
HELIX 29 AD2 SER B 85 GLY B 101 1 17
HELIX 30 AD3 PRO B 118 HIS B 134 1 17
HELIX 31 AD4 ASP B 137 SER B 139 5 3
HELIX 32 AD5 SER B 147 ILE B 163 1 17
HELIX 33 AD6 GLU B 185 ASN B 190 1 6
HELIX 34 AD7 ASN B 198 GLY B 211 1 14
HELIX 35 AD8 SER B 221 ALA B 225 5 5
HELIX 36 AD9 LEU B 243 ALA B 257 1 15
HELIX 37 AE1 VAL B 272 ALA B 277 5 6
HELIX 38 AE2 LEU B 280 GLY B 299 1 20
HELIX 39 AE3 SER D 4 THR D 20 1 17
HELIX 40 AE4 SER D 26 GLY D 39 1 14
HELIX 41 AE5 SER D 85 GLY D 101 1 17
HELIX 42 AE6 PRO D 118 HIS D 134 1 17
HELIX 43 AE7 ASP D 137 SER D 139 5 3
HELIX 44 AE8 SER D 147 ILE D 163 1 17
HELIX 45 AE9 GLU D 185 ASN D 190 1 6
HELIX 46 AF1 ASN D 198 GLY D 211 1 14
HELIX 47 AF2 SER D 221 ALA D 225 5 5
HELIX 48 AF3 LEU D 243 ALA D 257 1 15
HELIX 49 AF4 VAL D 272 ALA D 277 5 6
HELIX 50 AF5 LEU D 280 GLY D 299 1 20
SHEET 1 AA1 8 GLN C 48 VAL C 54 0
SHEET 2 AA1 8 VAL C 57 TYR C 63 -1 O TYR C 63 N GLN C 48
SHEET 3 AA1 8 CYS C 102 LEU C 107 -1 O GLY C 106 N GLU C 60
SHEET 4 AA1 8 ARG C 68 LEU C 76 1 N TYR C 75 O LEU C 105
SHEET 5 AA1 8 ILE C 141 ASP C 146 1 O GLY C 144 N LEU C 76
SHEET 6 AA1 8 ALA C 170 LEU C 174 1 O LEU C 174 N GLY C 145
SHEET 7 AA1 8 LEU C 233 GLY C 238 1 O LEU C 234 N CYS C 173
SHEET 8 AA1 8 ALA C 261 TRP C 266 1 O GLU C 264 N VAL C 235
SHEET 1 AA2 8 GLN A 48 VAL A 54 0
SHEET 2 AA2 8 VAL A 57 TYR A 63 -1 O VAL A 57 N VAL A 54
SHEET 3 AA2 8 CYS A 102 LEU A 107 -1 O VAL A 104 N ILE A 62
SHEET 4 AA2 8 ARG A 68 LEU A 76 1 N TYR A 75 O LEU A 105
SHEET 5 AA2 8 ILE A 141 ASP A 146 1 O GLY A 144 N LEU A 76
SHEET 6 AA2 8 ALA A 170 LEU A 174 1 O LEU A 174 N GLY A 145
SHEET 7 AA2 8 LEU A 233 GLY A 238 1 O LEU A 234 N CYS A 173
SHEET 8 AA2 8 ALA A 261 TRP A 266 1 O GLU A 264 N VAL A 235
SHEET 1 AA3 8 GLN B 48 VAL B 54 0
SHEET 2 AA3 8 VAL B 57 TYR B 63 -1 O TYR B 63 N GLN B 48
SHEET 3 AA3 8 CYS B 102 LEU B 107 -1 O GLY B 106 N GLU B 60
SHEET 4 AA3 8 ARG B 68 LEU B 76 1 N TYR B 75 O LEU B 105
SHEET 5 AA3 8 ILE B 141 ASP B 146 1 O GLY B 144 N LEU B 76
SHEET 6 AA3 8 ALA B 170 LEU B 174 1 O LEU B 174 N GLY B 145
SHEET 7 AA3 8 LEU B 233 GLY B 238 1 O LEU B 234 N CYS B 173
SHEET 8 AA3 8 ALA B 261 TRP B 266 1 O GLU B 264 N VAL B 235
SHEET 1 AA4 8 GLN D 48 VAL D 54 0
SHEET 2 AA4 8 VAL D 57 TYR D 63 -1 O TYR D 63 N GLN D 48
SHEET 3 AA4 8 ARG D 103 LEU D 107 -1 O GLY D 106 N GLU D 60
SHEET 4 AA4 8 VAL D 72 LEU D 76 1 N TYR D 75 O LEU D 105
SHEET 5 AA4 8 ILE D 141 ASP D 146 1 O ALA D 142 N LEU D 74
SHEET 6 AA4 8 ALA D 170 LEU D 174 1 O LEU D 174 N GLY D 145
SHEET 7 AA4 8 LEU D 233 GLY D 238 1 O LEU D 234 N CYS D 173
SHEET 8 AA4 8 ALA D 261 TRP D 266 1 O GLU D 264 N VAL D 235
CISPEP 1 ALA C 112 PRO C 113 0 5.32
CISPEP 2 PHE C 117 PRO C 118 0 3.77
CISPEP 3 ALA A 112 PRO A 113 0 5.12
CISPEP 4 PHE A 117 PRO A 118 0 6.64
CISPEP 5 ALA B 112 PRO B 113 0 2.06
CISPEP 6 PHE B 117 PRO B 118 0 3.01
CISPEP 7 ALA D 112 PRO D 113 0 4.03
CISPEP 8 PHE D 117 PRO D 118 0 5.52
CRYST1 63.133 73.679 85.553 67.54 68.32 76.86 P 1 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 0.015840 -0.003696 -0.005380 0.00000
SCALE2 0.000000 0.013937 -0.004862 0.00000
SCALE3 0.000000 0.000000 0.013322 0.00000
TER 2273 GLY C 299
TER 4568 GLY A 299
TER 6841 GLY B 299
TER 9114 GLY D 299
MASTER 393 0 0 50 32 0 0 610413 4 0 100
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