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HEADER HYDROLASE 15-JUL-16 5GMS
TITLE CRYSTAL STRUCTURE OF THE MUTANT S202W/I203F OF THE ESTERASE E40
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ESTERASE E40;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 5GMS 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. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 67899
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3434
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 42.5708 - 4.9688 0.96 2676 156 0.1933 0.2047
REMARK 3 2 4.9688 - 3.9448 1.00 2660 172 0.1509 0.1553
REMARK 3 3 3.9448 - 3.4464 1.00 2658 144 0.1455 0.1632
REMARK 3 4 3.4464 - 3.1314 1.00 2652 135 0.1589 0.1623
REMARK 3 5 3.1314 - 2.9070 1.00 2639 142 0.1623 0.1996
REMARK 3 6 2.9070 - 2.7356 1.00 2616 137 0.1634 0.1653
REMARK 3 7 2.7356 - 2.5987 1.00 2641 133 0.1576 0.2125
REMARK 3 8 2.5987 - 2.4855 0.99 2611 132 0.1566 0.1644
REMARK 3 9 2.4855 - 2.3899 0.99 2602 129 0.1604 0.1722
REMARK 3 10 2.3899 - 2.3074 0.99 2592 146 0.1551 0.1789
REMARK 3 11 2.3074 - 2.2353 0.99 2589 125 0.1554 0.1790
REMARK 3 12 2.2353 - 2.1714 0.99 2608 143 0.1544 0.1805
REMARK 3 13 2.1714 - 2.1142 0.99 2567 153 0.1571 0.1775
REMARK 3 14 2.1142 - 2.0626 0.99 2563 140 0.1616 0.1835
REMARK 3 15 2.0626 - 2.0157 0.99 2583 123 0.1590 0.2053
REMARK 3 16 2.0157 - 1.9728 0.98 2569 130 0.1582 0.1707
REMARK 3 17 1.9728 - 1.9334 0.97 2528 146 0.1635 0.1624
REMARK 3 18 1.9334 - 1.8969 0.97 2522 142 0.1605 0.1852
REMARK 3 19 1.8969 - 1.8630 0.97 2511 138 0.1639 0.2058
REMARK 3 20 1.8630 - 1.8314 0.97 2521 144 0.1653 0.1975
REMARK 3 21 1.8314 - 1.8019 0.97 2513 132 0.1674 0.1730
REMARK 3 22 1.8019 - 1.7742 0.97 2512 136 0.1821 0.1993
REMARK 3 23 1.7742 - 1.7481 0.96 2512 131 0.1778 0.2054
REMARK 3 24 1.7481 - 1.7235 0.96 2528 119 0.1863 0.2538
REMARK 3 25 1.7235 - 1.7002 0.95 2492 106 0.1898 0.1858
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 : 46.15
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.500
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) : -1.73640
REMARK 3 B22 (A**2) : -3.92010
REMARK 3 B33 (A**2) : 5.65650
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 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 : 0.010 4668
REMARK 3 ANGLE : 1.445 6370
REMARK 3 CHIRALITY : 0.092 706
REMARK 3 PLANARITY : 0.007 838
REMARK 3 DIHEDRAL : 13.876 1722
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): -18.8437 16.5523 18.0881
REMARK 3 T TENSOR
REMARK 3 T11: 0.0879 T22: 0.1278
REMARK 3 T33: 0.1107 T12: 0.0134
REMARK 3 T13: -0.0018 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 0.2861 L22: 0.3218
REMARK 3 L33: 0.3423 L12: 0.0347
REMARK 3 L13: 0.1679 L23: 0.0897
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: -0.0419 S13: 0.0486
REMARK 3 S21: -0.0004 S22: -0.0416 S23: 0.0530
REMARK 3 S31: -0.0269 S32: -0.1138 S33: 0.0548
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 5GMS 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_1300001081.
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 : 69213
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 77.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
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 (%): 46.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE (PH 7.0), 50% (V/V)
REMARK 280 MPD, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 48.03350
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 48.03350
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 45.05400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.42250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.05400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.42250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.03350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.05400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.42250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.03350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.05400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.42250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 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 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 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 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 32 O HOH A 301 1.77
REMARK 500 O HOH A 462 O HOH A 465 1.91
REMARK 500 O HOH A 523 O HOH A 529 1.91
REMARK 500 O HOH B 439 O HOH B 476 1.92
REMARK 500 O HOH A 308 O HOH A 428 1.99
REMARK 500 O HOH B 306 O HOH B 423 2.04
REMARK 500 O HOH A 302 O HOH A 492 2.05
REMARK 500 O HOH A 392 O HOH A 417 2.06
REMARK 500 O HOH B 301 O HOH B 411 2.06
REMARK 500 O HOH A 406 O HOH A 545 2.06
REMARK 500 O HOH A 532 O HOH A 542 2.07
REMARK 500 O HOH A 493 O HOH A 508 2.07
REMARK 500 O HOH B 480 O HOH B 530 2.08
REMARK 500 O HOH A 488 O HOH A 492 2.09
REMARK 500 O HOH A 458 O HOH A 525 2.14
REMARK 500 O HOH A 528 O HOH A 539 2.14
REMARK 500 O HOH B 487 O HOH B 528 2.14
REMARK 500 O HOH B 491 O HOH B 492 2.15
REMARK 500 O HOH B 465 O HOH B 518 2.15
REMARK 500 O HOH A 364 O HOH A 442 2.16
REMARK 500 O HOH B 484 O HOH B 515 2.17
REMARK 500 O HOH A 521 O HOH A 529 2.18
REMARK 500 O HOH B 450 O HOH B 480 2.18
REMARK 500 O HOH B 419 O HOH B 466 2.18
REMARK 500 O HOH A 340 O HOH A 522 2.19
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 520 O HOH A 520 3555 1.80
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU B 74 CA LEU B 74 C 0.206
REMARK 500 THR B 113 CA THR B 113 C 0.195
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 21 CB - CA - C ANGL. DEV. = -25.2 DEGREES
REMARK 500 ARG B 22 N - CA - CB ANGL. DEV. = -26.1 DEGREES
REMARK 500 ASP B 67 CA - C - O ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP B 67 CA - C - O ANGL. DEV. = 14.9 DEGREES
REMARK 500 ASP B 67 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 LEU B 74 C - N - CA ANGL. DEV. = 21.8 DEGREES
REMARK 500 LEU B 74 C - N - CA ANGL. DEV. = 22.8 DEGREES
REMARK 500 THR B 113 C - N - CA ANGL. DEV. = 21.7 DEGREES
REMARK 500 THR B 113 C - N - CA ANGL. DEV. = 20.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 83 -177.69 -179.31
REMARK 500 PHE A 115 136.58 -35.80
REMARK 500 PRO A 116 30.29 -98.48
REMARK 500 SER A 145 -120.62 48.57
REMARK 500 ASP A 266 -2.44 69.82
REMARK 500 ALA B 2 144.22 -177.37
REMARK 500 LYS B 3 42.05 -79.42
REMARK 500 ARG B 22 139.53 -36.88
REMARK 500 SER B 83 -176.70 -178.97
REMARK 500 PHE B 115 137.10 -39.83
REMARK 500 PRO B 116 32.86 -99.33
REMARK 500 SER B 145 -125.22 58.11
REMARK 500 SER B 194 -36.93 -137.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GMR RELATED DB: PDB
DBREF1 5GMS A 1 297 UNP A0A0F6WGE1_9BACT
DBREF2 5GMS A A0A0F6WGE1 1 297
DBREF1 5GMS B 1 297 UNP A0A0F6WGE1_9BACT
DBREF2 5GMS B A0A0F6WGE1 1 297
SEQADV 5GMS HIS A -15 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS A -14 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS A -13 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS A -12 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS A -11 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS A -10 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS SER A -9 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS SER A -8 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS GLY A -7 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS LEU A -6 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS VAL A -5 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS PRO A -4 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS ARG A -3 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS GLY A -2 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS SER A -1 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS A 0 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS TRP A 202 UNP A0A0F6WGE SER 202 ENGINEERED MUTATION
SEQADV 5GMS PHE A 203 UNP A0A0F6WGE ILE 203 ENGINEERED MUTATION
SEQADV 5GMS HIS B -15 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS B -14 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS B -13 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS B -12 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS B -11 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS B -10 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS SER B -9 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS SER B -8 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS GLY B -7 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS LEU B -6 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS VAL B -5 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS PRO B -4 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS ARG B -3 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS GLY B -2 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS SER B -1 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS HIS B 0 UNP A0A0F6WGE EXPRESSION TAG
SEQADV 5GMS TRP B 202 UNP A0A0F6WGE SER 202 ENGINEERED MUTATION
SEQADV 5GMS PHE B 203 UNP A0A0F6WGE ILE 203 ENGINEERED MUTATION
SEQRES 1 A 313 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 313 GLY SER HIS MET ALA LYS SER PRO GLU LEU ASP ARG VAL
SEQRES 3 A 313 ILE GLY MET ILE ARG GLU ARG ALA ALA THR PRO ARG LYS
SEQRES 4 A 313 THR THR ASP ASP ASP ARG ARG LEU TYR GLU THR MET LEU
SEQRES 5 A 313 GLY SER MET PRO LEU ASP ASP ASP ILE GLN THR GLU ARG
SEQRES 6 A 313 LEU GLY VAL ASN GLY VAL PRO ALA GLU TRP ILE TYR ALA
SEQRES 7 A 313 PRO GLY ALA ARG ASP ASP GLN VAL PHE LEU TYR LEU HIS
SEQRES 8 A 313 GLY GLY GLY TYR VAL ILE GLY SER MET ARG THR HIS ARG
SEQRES 9 A 313 VAL MET LEU SER HIS ILE ALA ARG ALA ALA GLY CYS ARG
SEQRES 10 A 313 VAL LEU GLY LEU ASP TYR ARG LEU ALA PRO GLU THR PRO
SEQRES 11 A 313 PHE PRO ALA PRO VAL GLU ASP THR VAL ALA ALA TYR ARG
SEQRES 12 A 313 TRP LEU LEU ALA HIS GLY TYR ASP PRO SER ARG ILE ALA
SEQRES 13 A 313 LEU GLY GLY ASP SER ALA GLY GLY GLY LEU VAL VAL ALA
SEQRES 14 A 313 ALA LEU VAL ALA LEU ARG TYR ILE GLY GLU PRO LEU PRO
SEQRES 15 A 313 ALA ALA GLY VAL CYS LEU SER PRO TRP ILE ASP MET GLU
SEQRES 16 A 313 ALA THR GLY GLU SER PHE THR THR ASN ALA THR MET ASP
SEQRES 17 A 313 PRO SER VAL ASN LYS GLU ARG VAL MET TRP PHE ALA ALA
SEQRES 18 A 313 LEU TYR LEU GLY GLY LYS ASN PRO GLN ALA PRO LEU ALA
SEQRES 19 A 313 SER PRO LEU TYR ALA ASP LEU GLN GLY LEU PRO PRO LEU
SEQRES 20 A 313 LEU VAL GLN VAL GLY GLY ILE GLU THR LEU LEU ASP ASP
SEQRES 21 A 313 ALA ARG ALA LEU THR THR ARG ALA LYS ALA ALA GLY VAL
SEQRES 22 A 313 ASP ALA ASP LEU GLU VAL TRP ASP ASP MET PRO HIS VAL
SEQRES 23 A 313 TRP GLN HIS PHE ALA PRO ILE LEU PRO GLU GLY LYS GLN
SEQRES 24 A 313 ALA ILE ALA ARG ILE GLY GLU PHE LEU ARG LYS GLN ILE
SEQRES 25 A 313 GLY
SEQRES 1 B 313 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 B 313 GLY SER HIS MET ALA LYS SER PRO GLU LEU ASP ARG VAL
SEQRES 3 B 313 ILE GLY MET ILE ARG GLU ARG ALA ALA THR PRO ARG LYS
SEQRES 4 B 313 THR THR ASP ASP ASP ARG ARG LEU TYR GLU THR MET LEU
SEQRES 5 B 313 GLY SER MET PRO LEU ASP ASP ASP ILE GLN THR GLU ARG
SEQRES 6 B 313 LEU GLY VAL ASN GLY VAL PRO ALA GLU TRP ILE TYR ALA
SEQRES 7 B 313 PRO GLY ALA ARG ASP ASP GLN VAL PHE LEU TYR LEU HIS
SEQRES 8 B 313 GLY GLY GLY TYR VAL ILE GLY SER MET ARG THR HIS ARG
SEQRES 9 B 313 VAL MET LEU SER HIS ILE ALA ARG ALA ALA GLY CYS ARG
SEQRES 10 B 313 VAL LEU GLY LEU ASP TYR ARG LEU ALA PRO GLU THR PRO
SEQRES 11 B 313 PHE PRO ALA PRO VAL GLU ASP THR VAL ALA ALA TYR ARG
SEQRES 12 B 313 TRP LEU LEU ALA HIS GLY TYR ASP PRO SER ARG ILE ALA
SEQRES 13 B 313 LEU GLY GLY ASP SER ALA GLY GLY GLY LEU VAL VAL ALA
SEQRES 14 B 313 ALA LEU VAL ALA LEU ARG TYR ILE GLY GLU PRO LEU PRO
SEQRES 15 B 313 ALA ALA GLY VAL CYS LEU SER PRO TRP ILE ASP MET GLU
SEQRES 16 B 313 ALA THR GLY GLU SER PHE THR THR ASN ALA THR MET ASP
SEQRES 17 B 313 PRO SER VAL ASN LYS GLU ARG VAL MET TRP PHE ALA ALA
SEQRES 18 B 313 LEU TYR LEU GLY GLY LYS ASN PRO GLN ALA PRO LEU ALA
SEQRES 19 B 313 SER PRO LEU TYR ALA ASP LEU GLN GLY LEU PRO PRO LEU
SEQRES 20 B 313 LEU VAL GLN VAL GLY GLY ILE GLU THR LEU LEU ASP ASP
SEQRES 21 B 313 ALA ARG ALA LEU THR THR ARG ALA LYS ALA ALA GLY VAL
SEQRES 22 B 313 ASP ALA ASP LEU GLU VAL TRP ASP ASP MET PRO HIS VAL
SEQRES 23 B 313 TRP GLN HIS PHE ALA PRO ILE LEU PRO GLU GLY LYS GLN
SEQRES 24 B 313 ALA ILE ALA ARG ILE GLY GLU PHE LEU ARG LYS GLN ILE
SEQRES 25 B 313 GLY
FORMUL 3 HOH *482(H2 O)
HELIX 1 AA1 SER A 4 ALA A 18 1 15
HELIX 2 AA2 THR A 24 GLY A 37 1 14
HELIX 3 AA3 SER A 83 GLY A 99 1 17
HELIX 4 AA4 PRO A 116 HIS A 132 1 17
HELIX 5 AA5 ASP A 135 SER A 137 5 3
HELIX 6 AA6 SER A 145 ILE A 161 1 17
HELIX 7 AA7 GLU A 183 ASN A 188 1 6
HELIX 8 AA8 ASN A 196 GLY A 209 1 14
HELIX 9 AA9 SER A 219 ALA A 223 5 5
HELIX 10 AB1 LEU A 241 ALA A 255 1 15
HELIX 11 AB2 VAL A 270 ILE A 277 5 8
HELIX 12 AB3 LEU A 278 GLY A 297 1 20
HELIX 13 AB4 SER B 4 THR B 20 1 17
HELIX 14 AB5 THR B 24 GLY B 37 1 14
HELIX 15 AB6 SER B 83 GLY B 99 1 17
HELIX 16 AB7 PRO B 116 HIS B 132 1 17
HELIX 17 AB8 ASP B 135 SER B 137 5 3
HELIX 18 AB9 SER B 145 ILE B 161 1 17
HELIX 19 AC1 GLU B 183 ASN B 188 1 6
HELIX 20 AC2 ASN B 196 GLY B 209 1 14
HELIX 21 AC3 SER B 219 ALA B 223 5 5
HELIX 22 AC4 LEU B 241 ALA B 255 1 15
HELIX 23 AC5 VAL B 270 ILE B 277 5 8
HELIX 24 AC6 LEU B 278 GLY B 297 1 20
SHEET 1 AA1 8 GLN A 46 VAL A 52 0
SHEET 2 AA1 8 VAL A 55 TYR A 61 -1 O TYR A 61 N GLN A 46
SHEET 3 AA1 8 CYS A 100 LEU A 105 -1 O GLY A 104 N GLU A 58
SHEET 4 AA1 8 ARG A 66 LEU A 74 1 N PHE A 71 O LEU A 103
SHEET 5 AA1 8 ILE A 139 ASP A 144 1 O GLY A 142 N LEU A 74
SHEET 6 AA1 8 ALA A 168 LEU A 172 1 O LEU A 172 N GLY A 143
SHEET 7 AA1 8 LEU A 231 GLY A 236 1 O LEU A 232 N CYS A 171
SHEET 8 AA1 8 ALA A 259 TRP A 264 1 O GLU A 262 N VAL A 233
SHEET 1 AA2 8 GLN B 46 VAL B 52 0
SHEET 2 AA2 8 VAL B 55 TYR B 61 -1 O TYR B 61 N GLN B 46
SHEET 3 AA2 8 CYS B 100 LEU B 105 -1 O GLY B 104 N GLU B 58
SHEET 4 AA2 8 ARG B 66 LEU B 74 1 N PHE B 71 O ARG B 101
SHEET 5 AA2 8 ILE B 139 ASP B 144 1 O ALA B 140 N LEU B 72
SHEET 6 AA2 8 ALA B 168 LEU B 172 1 O LEU B 172 N GLY B 143
SHEET 7 AA2 8 LEU B 231 GLY B 236 1 O LEU B 232 N CYS B 171
SHEET 8 AA2 8 ALA B 259 TRP B 264 1 O TRP B 264 N VAL B 235
CISPEP 1 ALA A 110 PRO A 111 0 3.37
CISPEP 2 PHE A 115 PRO A 116 0 3.65
CISPEP 3 ALA B 110 PRO B 111 0 5.25
CISPEP 4 PHE B 115 PRO B 116 0 4.24
CRYST1 90.108 144.845 96.067 90.00 90.00 90.00 C 2 2 21 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 0.011098 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006904 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010409 0.00000
TER 2274 GLY A 297
TER 4556 GLY B 297
MASTER 421 0 0 24 16 0 0 6 5016 2 0 50
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