| content |
HEADER HYDROLASE 17-DEC-21 7QJM
TITLE CRYSTAL STRUCTURE OF AN ALPHA/BETA-HYDROLASE ENZYME FROM CHLOROFLEXUS
TITLE 2 SP. MS-G (202)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA-HYDROLASE (202);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLOROFLEXUS SP. MS-G;
SOURCE 3 ORGANISM_TAXID: 1521187;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC DEGRADATION, PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,R.GRAHAM,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 28-DEC-22 7QJM 0
JRNL AUTH E.ERICKSON,J.E.GADO,L.AVILAN,F.BRATTI,R.K.BRIZENDINE,
JRNL AUTH 2 P.A.COX,R.GILL,R.GRAHAM,D.J.KIM,G.KONIG,W.E.MICHENER,
JRNL AUTH 3 S.POUDEL,K.J.RAMIREZ,T.J.SHAKESPEARE,M.ZAHN,E.S.BOYD,
JRNL AUTH 4 C.M.PAYNE,J.L.DUBOIS,A.R.PICKFORD,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL SOURCING THERMOTOLERANT POLY(ETHYLENE TEREPHTHALATE)
JRNL TITL 2 HYDROLASE SCAFFOLDS FROM NATURAL DIVERSITY
JRNL REF NAT COMMUN V. 13 7850 2022
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-022-35237-X
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 49979
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2537
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3833
REMARK 3 BIN FREE R VALUE : 0.3464
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 50
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4629
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.58380
REMARK 3 B22 (A**2) : 0.50050
REMARK 3 B33 (A**2) : -4.08420
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.320
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.182
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.162
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.185
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.165
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4736 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6452 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1611 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 802 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4736 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 604 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3802 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.16
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.54
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1544 -33.7073 17.6131
REMARK 3 T TENSOR
REMARK 3 T11: 0.0344 T22: 0.0154
REMARK 3 T33: -0.0567 T12: -0.0184
REMARK 3 T13: -0.1298 T23: 0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 2.9144 L22: 0.7022
REMARK 3 L33: 2.6189 L12: 0.5012
REMARK 3 L13: 1.0858 L23: 0.9359
REMARK 3 S TENSOR
REMARK 3 S11: -0.1655 S12: -0.0756 S13: 0.0122
REMARK 3 S21: -0.0756 S22: 0.109 S23: 0.223
REMARK 3 S31: 0.0122 S32: 0.223 S33: 0.0564
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6795 -18.5367 30.8241
REMARK 3 T TENSOR
REMARK 3 T11: -0.0752 T22: 0.1161
REMARK 3 T33: 0.2169 T12: -0.0207
REMARK 3 T13: -0.0899 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 2.387 L22: 2.9126
REMARK 3 L33: 2.9522 L12: 0.9996
REMARK 3 L13: -0.1658 L23: 2.0696
REMARK 3 S TENSOR
REMARK 3 S11: -0.1563 S12: -0.3097 S13: -0.1802
REMARK 3 S21: -0.3097 S22: -0.2441 S23: -0.7702
REMARK 3 S31: -0.1802 S32: -0.7702 S33: 0.4004
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7QJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1292118047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-20
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 : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49979
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 50.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 3.18100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 7D78
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % PEG 3350, 0.1 M SUCCINIC ACID,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.34000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.45500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 84.99500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.34000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.45500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.99500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.34000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 62.45500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.99500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.34000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 62.45500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 84.99500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 407 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 VAL A 2
REMARK 465 ASP A 3
REMARK 465 ILE A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 ASN A 7
REMARK 465 GLY A 8
REMARK 465 MET A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 THR A 12
REMARK 465 ALA A 13
REMARK 465 PRO A 14
REMARK 465 THR A 15
REMARK 465 ASP A 16
REMARK 465 GLU A 17
REMARK 465 ARG A 18
REMARK 465 ILE A 19
REMARK 465 VAL A 20
REMARK 465 ASP A 21
REMARK 465 LYS A 22
REMARK 465 PRO A 23
REMARK 465 LEU A 24
REMARK 465 PRO A 25
REMARK 465 GLN A 26
REMARK 465 PRO A 27
REMARK 465 GLN A 28
REMARK 465 ILE A 29
REMARK 465 ARG A 30
REMARK 465 SER A 31
REMARK 465 GLY A 32
REMARK 465 ASN A 33
REMARK 465 VAL A 34
REMARK 465 ARG A 35
REMARK 465 ALA A 36
REMARK 465 MET A 37
REMARK 465 PRO A 38
REMARK 465 ALA A 39
REMARK 465 ALA A 40
REMARK 465 ARG A 41
REMARK 465 LYS A 42
REMARK 465 LEU A 43
REMARK 465 ALA A 44
REMARK 465 GLN A 45
REMARK 465 GLU A 46
REMARK 465 HIS A 47
REMARK 465 GLY A 48
REMARK 465 ILE A 49
REMARK 465 ASP A 50
REMARK 465 LEU A 51
REMARK 465 SER A 52
REMARK 465 THR A 53
REMARK 465 LEU A 54
REMARK 465 THR A 55
REMARK 465 GLY A 56
REMARK 465 SER A 57
REMARK 465 GLY A 58
REMARK 465 PRO A 59
REMARK 465 GLY A 60
REMARK 465 GLY A 61
REMARK 465 VAL A 62
REMARK 465 ILE A 63
REMARK 465 VAL A 64
REMARK 465 LYS A 65
REMARK 465 GLU A 66
REMARK 465 ASP A 67
REMARK 465 VAL A 68
REMARK 465 GLU A 69
REMARK 465 ARG A 70
REMARK 465 ALA A 71
REMARK 465 ILE A 72
REMARK 465 THR A 73
REMARK 465 ALA A 74
REMARK 465 ARG A 75
REMARK 465 ALA A 76
REMARK 465 ALA A 378
REMARK 465 ASP A 379
REMARK 465 ASN A 380
REMARK 465 LEU A 381
REMARK 465 GLU A 382
REMARK 465 HIS A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 ASP B 3
REMARK 465 ILE B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 ASN B 7
REMARK 465 GLY B 8
REMARK 465 MET B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 THR B 12
REMARK 465 ALA B 13
REMARK 465 PRO B 14
REMARK 465 THR B 15
REMARK 465 ASP B 16
REMARK 465 GLU B 17
REMARK 465 ARG B 18
REMARK 465 ILE B 19
REMARK 465 VAL B 20
REMARK 465 ASP B 21
REMARK 465 LYS B 22
REMARK 465 PRO B 23
REMARK 465 LEU B 24
REMARK 465 PRO B 25
REMARK 465 GLN B 26
REMARK 465 PRO B 27
REMARK 465 GLN B 28
REMARK 465 ILE B 29
REMARK 465 ARG B 30
REMARK 465 SER B 31
REMARK 465 GLY B 32
REMARK 465 ASN B 33
REMARK 465 VAL B 34
REMARK 465 ARG B 35
REMARK 465 ALA B 36
REMARK 465 MET B 37
REMARK 465 PRO B 38
REMARK 465 ALA B 39
REMARK 465 ALA B 40
REMARK 465 ARG B 41
REMARK 465 LYS B 42
REMARK 465 LEU B 43
REMARK 465 ALA B 44
REMARK 465 GLN B 45
REMARK 465 GLU B 46
REMARK 465 HIS B 47
REMARK 465 GLY B 48
REMARK 465 ILE B 49
REMARK 465 ASP B 50
REMARK 465 LEU B 51
REMARK 465 SER B 52
REMARK 465 THR B 53
REMARK 465 LEU B 54
REMARK 465 THR B 55
REMARK 465 GLY B 56
REMARK 465 SER B 57
REMARK 465 GLY B 58
REMARK 465 PRO B 59
REMARK 465 GLY B 60
REMARK 465 GLY B 61
REMARK 465 VAL B 62
REMARK 465 ILE B 63
REMARK 465 VAL B 64
REMARK 465 LYS B 65
REMARK 465 GLU B 66
REMARK 465 ASP B 67
REMARK 465 VAL B 68
REMARK 465 GLU B 69
REMARK 465 ARG B 70
REMARK 465 ALA B 71
REMARK 465 ILE B 72
REMARK 465 THR B 73
REMARK 465 ALA B 74
REMARK 465 ARG B 75
REMARK 465 ALA B 76
REMARK 465 VAL B 77
REMARK 465 PRO B 78
REMARK 465 VAL B 79
REMARK 465 SER B 377
REMARK 465 ALA B 378
REMARK 465 ASP B 379
REMARK 465 ASN B 380
REMARK 465 LEU B 381
REMARK 465 GLU B 382
REMARK 465 HIS B 383
REMARK 465 HIS B 384
REMARK 465 HIS B 385
REMARK 465 HIS B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
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 TYR A 119 107.77 -47.37
REMARK 500 VAL A 126 -51.08 71.90
REMARK 500 SER A 192 -113.29 56.88
REMARK 500 PHE A 279 74.51 -115.59
REMARK 500 ALA A 307 -121.85 41.17
REMARK 500 HIS B 103 40.20 37.69
REMARK 500 TYR B 119 108.81 -49.84
REMARK 500 VAL B 126 -51.21 74.47
REMARK 500 SER B 192 -111.90 57.01
REMARK 500 ALA B 307 -121.79 41.94
REMARK 500 SER B 337 -10.07 70.19
REMARK 500 SER B 347 -138.95 -87.94
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7QJM A 1 388 PDB 7QJM 7QJM 1 388
DBREF 7QJM B 1 388 PDB 7QJM 7QJM 1 388
SEQRES 1 A 388 MET VAL ASP ILE THR GLY ASN GLY MET ALA ALA THR ALA
SEQRES 2 A 388 PRO THR ASP GLU ARG ILE VAL ASP LYS PRO LEU PRO GLN
SEQRES 3 A 388 PRO GLN ILE ARG SER GLY ASN VAL ARG ALA MET PRO ALA
SEQRES 4 A 388 ALA ARG LYS LEU ALA GLN GLU HIS GLY ILE ASP LEU SER
SEQRES 5 A 388 THR LEU THR GLY SER GLY PRO GLY GLY VAL ILE VAL LYS
SEQRES 6 A 388 GLU ASP VAL GLU ARG ALA ILE THR ALA ARG ALA VAL PRO
SEQRES 7 A 388 VAL SER PRO LEU GLN ARG VAL ASN PHE TYR SER ALA GLY
SEQRES 8 A 388 TYR ARG LEU ASP GLY LEU LEU TYR THR PRO ARG HIS LEU
SEQRES 9 A 388 PRO ALA GLY GLU ARG ARG PRO GLY VAL VAL LEU LEU VAL
SEQRES 10 A 388 GLY TYR THR TYR LEU LYS THR MET VAL MET PRO ASP ILE
SEQRES 11 A 388 ALA LYS VAL LEU ASN ALA ALA GLY TYR VAL ALA LEU VAL
SEQRES 12 A 388 PHE ASP TYR ARG GLY PHE GLY GLU SER GLU GLY PRO ARG
SEQRES 13 A 388 GLY ARG LEU ILE PRO LEU GLU GLN VAL ALA ASP ALA ARG
SEQRES 14 A 388 ALA ALA LEU THR PHE LEU ALA GLU GLN SER MET VAL ASP
SEQRES 15 A 388 PRO ASP ARG LEU ALA VAL ILE GLY ILE SER LEU GLY GLY
SEQRES 16 A 388 ALA HIS ALA ILE THR THR ALA ALA LEU ASP GLN ARG VAL
SEQRES 17 A 388 ARG ALA VAL VAL ALA LEU GLU PRO PRO GLY HIS GLY ALA
SEQRES 18 A 388 ARG TRP LEU ARG SER LEU ARG ARG HIS TRP GLU TRP ARG
SEQRES 19 A 388 GLN PHE LEU SER ARG LEU ALA GLU ASP ARG ARG GLN ARG
SEQRES 20 A 388 VAL LEU SER GLY GLY SER THR MET VAL ASP PRO LEU GLU
SEQRES 21 A 388 ILE VAL LEU PRO ASP PRO GLU SER GLN ALA PHE LEU ASP
SEQRES 22 A 388 GLN VAL ALA ALA GLU PHE PRO GLN MET LYS VAL THR LEU
SEQRES 23 A 388 PRO LEU GLU SER ALA GLU ALA LEU ILE GLU TYR VAL SER
SEQRES 24 A 388 GLU ASP LEU ALA GLY ARG ILE ALA PRO ARG PRO LEU LEU
SEQRES 25 A 388 ILE ILE HIS SER ASP ALA ASP GLN LEU VAL PRO VAL ALA
SEQRES 26 A 388 GLU ALA GLN ALA ILE ALA GLU ARG ALA GLY SER SER ALA
SEQRES 27 A 388 GLN LEU GLU ILE ILE PRO GLY MET SER HIS PHE ASN TRP
SEQRES 28 A 388 VAL MET PRO GLY SER PRO GLY PHE THR ARG VAL THR ASP
SEQRES 29 A 388 SER ILE VAL LYS PHE LEU ARG ASN THR LEU PRO VAL SER
SEQRES 30 A 388 ALA ASP ASN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 388 MET VAL ASP ILE THR GLY ASN GLY MET ALA ALA THR ALA
SEQRES 2 B 388 PRO THR ASP GLU ARG ILE VAL ASP LYS PRO LEU PRO GLN
SEQRES 3 B 388 PRO GLN ILE ARG SER GLY ASN VAL ARG ALA MET PRO ALA
SEQRES 4 B 388 ALA ARG LYS LEU ALA GLN GLU HIS GLY ILE ASP LEU SER
SEQRES 5 B 388 THR LEU THR GLY SER GLY PRO GLY GLY VAL ILE VAL LYS
SEQRES 6 B 388 GLU ASP VAL GLU ARG ALA ILE THR ALA ARG ALA VAL PRO
SEQRES 7 B 388 VAL SER PRO LEU GLN ARG VAL ASN PHE TYR SER ALA GLY
SEQRES 8 B 388 TYR ARG LEU ASP GLY LEU LEU TYR THR PRO ARG HIS LEU
SEQRES 9 B 388 PRO ALA GLY GLU ARG ARG PRO GLY VAL VAL LEU LEU VAL
SEQRES 10 B 388 GLY TYR THR TYR LEU LYS THR MET VAL MET PRO ASP ILE
SEQRES 11 B 388 ALA LYS VAL LEU ASN ALA ALA GLY TYR VAL ALA LEU VAL
SEQRES 12 B 388 PHE ASP TYR ARG GLY PHE GLY GLU SER GLU GLY PRO ARG
SEQRES 13 B 388 GLY ARG LEU ILE PRO LEU GLU GLN VAL ALA ASP ALA ARG
SEQRES 14 B 388 ALA ALA LEU THR PHE LEU ALA GLU GLN SER MET VAL ASP
SEQRES 15 B 388 PRO ASP ARG LEU ALA VAL ILE GLY ILE SER LEU GLY GLY
SEQRES 16 B 388 ALA HIS ALA ILE THR THR ALA ALA LEU ASP GLN ARG VAL
SEQRES 17 B 388 ARG ALA VAL VAL ALA LEU GLU PRO PRO GLY HIS GLY ALA
SEQRES 18 B 388 ARG TRP LEU ARG SER LEU ARG ARG HIS TRP GLU TRP ARG
SEQRES 19 B 388 GLN PHE LEU SER ARG LEU ALA GLU ASP ARG ARG GLN ARG
SEQRES 20 B 388 VAL LEU SER GLY GLY SER THR MET VAL ASP PRO LEU GLU
SEQRES 21 B 388 ILE VAL LEU PRO ASP PRO GLU SER GLN ALA PHE LEU ASP
SEQRES 22 B 388 GLN VAL ALA ALA GLU PHE PRO GLN MET LYS VAL THR LEU
SEQRES 23 B 388 PRO LEU GLU SER ALA GLU ALA LEU ILE GLU TYR VAL SER
SEQRES 24 B 388 GLU ASP LEU ALA GLY ARG ILE ALA PRO ARG PRO LEU LEU
SEQRES 25 B 388 ILE ILE HIS SER ASP ALA ASP GLN LEU VAL PRO VAL ALA
SEQRES 26 B 388 GLU ALA GLN ALA ILE ALA GLU ARG ALA GLY SER SER ALA
SEQRES 27 B 388 GLN LEU GLU ILE ILE PRO GLY MET SER HIS PHE ASN TRP
SEQRES 28 B 388 VAL MET PRO GLY SER PRO GLY PHE THR ARG VAL THR ASP
SEQRES 29 B 388 SER ILE VAL LYS PHE LEU ARG ASN THR LEU PRO VAL SER
SEQRES 30 B 388 ALA ASP ASN LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *139(H2 O)
HELIX 1 AA1 VAL A 126 ALA A 137 1 12
HELIX 2 AA2 ILE A 160 GLU A 177 1 18
HELIX 3 AA3 SER A 192 ASP A 205 1 14
HELIX 4 AA4 HIS A 219 LEU A 227 1 9
HELIX 5 AA5 ARG A 229 GLY A 251 1 23
HELIX 6 AA6 ASP A 257 ILE A 261 5 5
HELIX 7 AA7 ASP A 265 PHE A 279 1 15
HELIX 8 AA8 PRO A 280 LYS A 283 5 4
HELIX 9 AA9 LEU A 288 GLU A 296 1 9
HELIX 10 AB1 SER A 299 GLY A 304 1 6
HELIX 11 AB2 ARG A 305 ALA A 307 5 3
HELIX 12 AB3 PRO A 323 GLY A 335 1 13
HELIX 13 AB4 SER A 356 ASN A 372 1 17
HELIX 14 AB5 VAL B 126 ALA B 137 1 12
HELIX 15 AB6 ILE B 160 GLU B 177 1 18
HELIX 16 AB7 SER B 192 ASP B 205 1 14
HELIX 17 AB8 HIS B 219 LEU B 227 1 9
HELIX 18 AB9 ARG B 229 GLY B 251 1 23
HELIX 19 AC1 ASP B 257 ILE B 261 5 5
HELIX 20 AC2 ASP B 265 PHE B 279 1 15
HELIX 21 AC3 PRO B 280 LYS B 283 5 4
HELIX 22 AC4 LEU B 288 GLU B 296 1 9
HELIX 23 AC5 SER B 299 GLY B 304 1 6
HELIX 24 AC6 ARG B 305 ALA B 307 5 3
HELIX 25 AC7 PRO B 323 ALA B 334 1 12
HELIX 26 AC8 SER B 356 ASN B 372 1 17
SHEET 1 AA1 8 LEU A 82 SER A 89 0
SHEET 2 AA1 8 TYR A 92 TYR A 99 -1 O LEU A 94 N PHE A 87
SHEET 3 AA1 8 VAL A 140 PHE A 144 -1 O ALA A 141 N TYR A 99
SHEET 4 AA1 8 ARG A 110 LEU A 116 1 N LEU A 115 O LEU A 142
SHEET 5 AA1 8 VAL A 181 ILE A 191 1 O ILE A 189 N LEU A 116
SHEET 6 AA1 8 VAL A 208 LEU A 214 1 O ARG A 209 N LEU A 186
SHEET 7 AA1 8 LEU A 311 HIS A 315 1 O LEU A 312 N ALA A 213
SHEET 8 AA1 8 ALA A 338 ILE A 342 1 O GLU A 341 N ILE A 313
SHEET 1 AA2 2 MET A 255 VAL A 256 0
SHEET 2 AA2 2 LEU A 286 PRO A 287 -1 O LEU A 286 N VAL A 256
SHEET 1 AA3 8 LEU B 82 SER B 89 0
SHEET 2 AA3 8 TYR B 92 TYR B 99 -1 O LEU B 94 N PHE B 87
SHEET 3 AA3 8 VAL B 140 PHE B 144 -1 O ALA B 141 N TYR B 99
SHEET 4 AA3 8 ARG B 110 LEU B 116 1 N LEU B 115 O LEU B 142
SHEET 5 AA3 8 VAL B 181 ILE B 191 1 O ILE B 189 N LEU B 116
SHEET 6 AA3 8 VAL B 208 LEU B 214 1 O ARG B 209 N LEU B 186
SHEET 7 AA3 8 LEU B 311 HIS B 315 1 O LEU B 312 N ALA B 213
SHEET 8 AA3 8 ALA B 338 ILE B 342 1 O GLU B 341 N ILE B 313
SHEET 1 AA4 2 MET B 255 VAL B 256 0
SHEET 2 AA4 2 LEU B 286 PRO B 287 -1 O LEU B 286 N VAL B 256
CRYST1 90.680 124.910 169.990 90.00 90.00 90.00 I 2 2 2 16
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 0.011028 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005883 0.00000
TER 2329 SER A 377
TER 4631 VAL B 376
MASTER 488 0 0 26 20 0 0 6 4768 2 0 60
END |