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HEADER HYDROLASE 08-DEC-16 5MLY
TITLE CLOSED LOOP CONFORMATION OF PHAZ7 Y105E MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHB DEPOLYMERASE PHAZ7;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: NO ELECTRON DENSITY FOR THE LAST C-TER RESIDUES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PAUCIMONAS LEMOIGNEI;
SOURCE 3 ORGANISM_TAXID: 29443;
SOURCE 4 GENE: PHAZ7;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: WB800
KEYWDS DEPOLYMERASE, CONFORMATIONAL CHANGE, BIOPOLYMER DEGRADATION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KELLICI,T.MAVROMOUSTAKOS,D.JENDROSSEK,A.C.PAPAGEORGIOU
REVDAT 1 10-MAY-17 5MLY 0
JRNL AUTH T.F.KELLICI,T.MAVROMOUSTAKOS,D.JENDROSSEK,A.C.PAPAGEORGIOU
JRNL TITL CRYSTAL STRUCTURE ANALYSIS, COVALENT DOCKING, AND MOLECULAR
JRNL TITL 2 DYNAMICS CALCULATIONS REVEAL A CONFORMATIONAL SWITCH IN
JRNL TITL 3 PHAZ7 PHB DEPOLYMERASE.
JRNL REF PROTEINS 2017
JRNL REFN ESSN 1097-0134
JRNL PMID 28370478
JRNL DOI 10.1002/PROT.25296
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.JENDROSSEK,S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU
REMARK 1 TITL BIOCHEMICAL ANALYSIS AND STRUCTURE DETERMINATION OF
REMARK 1 TITL 2 PAUCIMONAS LEMOIGNEI POLY(3-HYDROXYBUTYRATE) (PHB)
REMARK 1 TITL 3 DEPOLYMERASE PHAZ7 MUTEINS REVEAL THE PHB BINDING SITE AND
REMARK 1 TITL 4 DETAILS OF SUBSTRATE-ENZYME INTERACTIONS.
REMARK 1 REF MOL. MICROBIOL. V. 90 649 2013
REMARK 1 REFN ESSN 1365-2958
REMARK 1 PMID 24007310
REMARK 1 DOI 10.1111/MMI.12391
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.C.PAPAGEORGIOU,S.HERMAWAN,C.B.SINGH,D.JENDROSSEK
REMARK 1 TITL STRUCTURAL BASIS OF POLY(3-HYDROXYBUTYRATE) HYDROLYSIS BY
REMARK 1 TITL 2 PHAZ7 DEPOLYMERASE FROM PAUCIMONAS LEMOIGNEI.
REMARK 1 REF J. MOL. BIOL. V. 382 1184 2008
REMARK 1 REFN ESSN 1089-8638
REMARK 1 PMID 18706425
REMARK 1 DOI 10.1016/J.JMB.2008.07.078
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.030
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 78327
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.130
REMARK 3 R VALUE (WORKING SET) : 0.128
REMARK 3 FREE R VALUE : 0.157
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3909
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 19.4214 - 4.8296 0.90 2630 144 0.1436 0.1435
REMARK 3 2 4.8296 - 3.8431 0.89 2588 143 0.1008 0.1093
REMARK 3 3 3.8431 - 3.3602 0.91 2656 143 0.1127 0.1473
REMARK 3 4 3.3602 - 3.0543 0.94 2759 149 0.1189 0.1441
REMARK 3 5 3.0543 - 2.8361 0.94 2740 135 0.1212 0.1377
REMARK 3 6 2.8361 - 2.6693 0.94 2745 150 0.1182 0.1320
REMARK 3 7 2.6693 - 2.5359 0.95 2740 144 0.1203 0.1604
REMARK 3 8 2.5359 - 2.4257 0.95 2712 139 0.1206 0.1617
REMARK 3 9 2.4257 - 2.3325 0.96 2801 144 0.1186 0.1370
REMARK 3 10 2.3325 - 2.2521 0.95 2774 150 0.1206 0.1655
REMARK 3 11 2.2521 - 2.1818 0.95 2708 135 0.1172 0.1694
REMARK 3 12 2.1818 - 2.1195 0.95 2771 157 0.1207 0.1388
REMARK 3 13 2.1195 - 2.0638 0.95 2740 145 0.1288 0.1598
REMARK 3 14 2.0638 - 2.0135 0.94 2757 142 0.1309 0.1688
REMARK 3 15 2.0135 - 1.9678 0.94 2733 137 0.1342 0.1504
REMARK 3 16 1.9678 - 1.9259 0.94 2715 140 0.1351 0.1820
REMARK 3 17 1.9259 - 1.8874 0.93 2676 144 0.1414 0.1794
REMARK 3 18 1.8874 - 1.8519 0.93 2722 145 0.1466 0.1879
REMARK 3 19 1.8519 - 1.8188 0.92 2664 143 0.1449 0.1814
REMARK 3 20 1.8188 - 1.7880 0.93 2657 134 0.1485 0.1918
REMARK 3 21 1.7880 - 1.7592 0.91 2666 143 0.1500 0.1803
REMARK 3 22 1.7592 - 1.7321 0.91 2619 138 0.1491 0.2222
REMARK 3 23 1.7321 - 1.7067 0.90 2611 134 0.1508 0.2193
REMARK 3 24 1.7067 - 1.6826 0.90 2631 139 0.1574 0.1921
REMARK 3 25 1.6826 - 1.6599 0.89 2554 128 0.1545 0.1918
REMARK 3 26 1.6599 - 1.6384 0.88 2579 128 0.1603 0.1885
REMARK 3 27 1.6384 - 1.6179 0.88 2555 132 0.1716 0.2203
REMARK 3 28 1.6179 - 1.5984 0.67 1915 104 0.1803 0.2129
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 5253
REMARK 3 ANGLE : 0.878 7154
REMARK 3 CHIRALITY : 0.070 751
REMARK 3 PLANARITY : 0.006 928
REMARK 3 DIHEDRAL : 11.908 2996
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5MLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002615.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8123
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78330
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.598
REMARK 200 RESOLUTION RANGE LOW (A) : 19.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03000
REMARK 200 FOR THE DATA SET : 25.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4BRS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M MES, 20% PEG6000, PH
REMARK 280 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 99.88000
REMARK 290 SMTRY3 2 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 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: 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: 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 LEU A 343
REMARK 465 GLU A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 HIS A 348
REMARK 465 HIS A 349
REMARK 465 HIS A 350
REMARK 465 LEU B 343
REMARK 465 GLU B 344
REMARK 465 HIS B 345
REMARK 465 HIS B 346
REMARK 465 HIS B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 349
REMARK 465 HIS B 350
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 499 O HOH B 677 1.57
REMARK 500 O HOH A 478 O HOH A 716 1.65
REMARK 500 O HOH A 404 O HOH A 737 1.65
REMARK 500 O HOH B 804 O HOH B 985 1.66
REMARK 500 O HOH A 808 O HOH A 950 1.69
REMARK 500 O HOH B 405 O HOH B 485 1.69
REMARK 500 O HOH B 431 O HOH B 704 1.70
REMARK 500 O HOH A 689 O HOH A 894 1.71
REMARK 500 O HOH A 930 O HOH B 948 1.78
REMARK 500 O TYR A 204 O HOH A 401 1.80
REMARK 500 O HOH B 1005 O HOH B 1010 1.82
REMARK 500 O HOH A 854 O HOH A 893 1.83
REMARK 500 O HOH A 728 O HOH A 901 1.83
REMARK 500 O HOH A 422 O HOH A 578 1.91
REMARK 500 O HOH A 700 O HOH A 808 1.93
REMARK 500 O HOH A 646 O HOH A 676 1.93
REMARK 500 O HOH A 521 O HOH A 737 1.94
REMARK 500 O HOH A 880 O HOH A 928 1.96
REMARK 500 O HOH B 735 O HOH B 858 1.97
REMARK 500 O HOH A 946 O HOH A 971 1.98
REMARK 500 O HOH A 700 O HOH A 950 2.00
REMARK 500 O HOH A 488 O HOH A 843 2.00
REMARK 500 O HOH A 910 O HOH A 962 2.01
REMARK 500 O HOH B 818 O HOH B 882 2.01
REMARK 500 O HOH B 817 O HOH B 844 2.01
REMARK 500 O HOH B 640 O HOH B 846 2.04
REMARK 500 O HOH B 812 O HOH B 963 2.05
REMARK 500 O HOH A 721 O HOH A 799 2.05
REMARK 500 O HOH B 912 O HOH B 962 2.06
REMARK 500 O HOH A 429 O HOH A 728 2.07
REMARK 500 O HOH B 638 O HOH B 779 2.07
REMARK 500 O HOH A 435 O HOH A 621 2.08
REMARK 500 O HOH A 855 O HOH A 916 2.09
REMARK 500 O HOH B 864 O HOH B 896 2.09
REMARK 500 O HOH A 683 O HOH B 794 2.09
REMARK 500 O HOH A 903 O HOH A 954 2.09
REMARK 500 O HOH B 704 O HOH B 755 2.10
REMARK 500 O HOH B 823 O HOH B 831 2.10
REMARK 500 O HOH A 800 O HOH A 940 2.11
REMARK 500 O HOH A 721 O HOH A 942 2.11
REMARK 500 O HOH B 623 O HOH B 778 2.13
REMARK 500 O HOH B 455 O HOH B 576 2.13
REMARK 500 O HOH A 705 O HOH A 741 2.16
REMARK 500 O HOH A 497 O HOH A 750 2.16
REMARK 500 O HOH A 637 O HOH A 883 2.17
REMARK 500 O HOH A 942 O HOH A 962 2.18
REMARK 500 OE1 GLU B 333 O HOH B 401 2.18
REMARK 500 OG1 THR B 39 O HOH B 402 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 B 858 O HOH B 951 1656 1.60
REMARK 500 O HOH A 842 O HOH A 947 1455 1.76
REMARK 500 O HOH A 878 O HOH B 877 2545 1.77
REMARK 500 O HOH B 615 O HOH B 750 1656 1.88
REMARK 500 O HOH A 566 O HOH A 823 1455 1.90
REMARK 500 O HOH B 874 O HOH B 987 1656 1.90
REMARK 500 O HOH A 872 O HOH B 755 1656 2.03
REMARK 500 O HOH B 735 O HOH B 951 1656 2.09
REMARK 500 O HOH A 415 O HOH B 609 1656 2.09
REMARK 500 O HOH B 618 O HOH B 774 1455 2.12
REMARK 500 O HOH A 581 O HOH A 786 1454 2.14
REMARK 500 O HOH B 629 O HOH B 870 1655 2.15
REMARK 500 O HOH B 839 O HOH B 917 1655 2.17
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 VAL B 206 CG1 - CB - CG2 ANGL. DEV. = 9.7 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 ALA A 23 83.38 -150.39
REMARK 500 SER A 136 -131.73 57.89
REMARK 500 ARG A 156 -62.10 -93.70
REMARK 500 ALA A 177 42.64 -140.07
REMARK 500 ALA A 181 64.46 -150.08
REMARK 500 SER A 186 -159.01 -83.10
REMARK 500 ASN A 210 83.89 -155.38
REMARK 500 ALA A 295 66.94 -104.70
REMARK 500 ALA B 23 87.31 -153.58
REMARK 500 SER B 136 -133.72 56.98
REMARK 500 ARG B 156 -60.33 -96.08
REMARK 500 ALA B 177 41.59 -141.91
REMARK 500 ALA B 181 64.24 -150.57
REMARK 500 SER B 186 -157.37 -83.70
REMARK 500 ASN B 210 80.92 -156.88
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 A 978 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 979 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 980 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH A 981 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A 982 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 983 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A 984 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A 985 DISTANCE = 7.30 ANGSTROMS
REMARK 525 HOH A 986 DISTANCE = 7.98 ANGSTROMS
REMARK 525 HOH A 987 DISTANCE = 7.98 ANGSTROMS
REMARK 525 HOH A 988 DISTANCE = 8.35 ANGSTROMS
REMARK 525 HOH A 989 DISTANCE = 8.69 ANGSTROMS
REMARK 525 HOH B1003 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B1004 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B1005 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B1006 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B1007 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B1008 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B1009 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH B1010 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH B1011 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH B1012 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH B1013 DISTANCE = 8.10 ANGSTROMS
DBREF 5MLY A 1 342 UNP Q939Q9 Q939Q9_PAULE 39 380
DBREF 5MLY B 1 342 UNP Q939Q9 Q939Q9_PAULE 39 380
SEQADV 5MLY GLU A 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQADV 5MLY LEU A 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY GLU A 344 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS A 345 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS A 346 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS A 347 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS A 348 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS A 349 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS A 350 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY GLU B 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQADV 5MLY LEU B 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY GLU B 344 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS B 345 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS B 346 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS B 347 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS B 348 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS B 349 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLY HIS B 350 UNP Q939Q9 EXPRESSION TAG
SEQRES 1 A 350 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 A 350 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 A 350 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 A 350 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 A 350 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 A 350 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 A 350 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 A 350 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 A 350 GLU HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 A 350 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 A 350 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 A 350 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 A 350 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 A 350 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 A 350 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 A 350 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 A 350 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 A 350 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 A 350 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 A 350 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 A 350 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 A 350 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 A 350 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 A 350 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 A 350 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 A 350 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 A 350 LYS ALA ALA TYR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 350 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 B 350 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 B 350 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 B 350 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 B 350 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 B 350 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 B 350 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 B 350 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 B 350 GLU HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 B 350 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 B 350 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 B 350 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 B 350 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 B 350 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 B 350 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 B 350 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 B 350 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 B 350 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 B 350 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 B 350 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 B 350 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 B 350 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 B 350 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 B 350 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 B 350 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 B 350 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 B 350 LYS ALA ALA TYR LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *1202(H2 O)
HELIX 1 AA1 ASN A 52 MET A 58 5 7
HELIX 2 AA2 SER A 72 ARG A 80 1 9
HELIX 3 AA3 SER A 94 GLY A 99 1 6
HELIX 4 AA4 SER A 100 ASN A 104 5 5
HELIX 5 AA5 SER A 107 GLY A 126 1 20
HELIX 6 AA6 SER A 136 ASN A 150 1 15
HELIX 7 AA7 ASN A 151 THR A 153 5 3
HELIX 8 AA8 LEU A 168 TYR A 172 5 5
HELIX 9 AA9 ALA A 181 GLY A 185 5 5
HELIX 10 AB1 SER A 220 ARG A 222 5 3
HELIX 11 AB2 ASP A 223 ARG A 228 1 6
HELIX 12 AB3 ALA A 238 ASP A 242 5 5
HELIX 13 AB4 GLY A 254 ALA A 258 5 5
HELIX 14 AB5 ASP A 286 GLY A 290 5 5
HELIX 15 AB6 PHE A 307 ASN A 312 1 6
HELIX 16 AB7 THR A 313 THR A 323 1 11
HELIX 17 AB8 THR A 326 ALA A 332 5 7
HELIX 18 AB9 ASN B 52 MET B 58 5 7
HELIX 19 AC1 SER B 72 ARG B 80 1 9
HELIX 20 AC2 SER B 94 GLY B 99 1 6
HELIX 21 AC3 SER B 100 ASN B 104 5 5
HELIX 22 AC4 SER B 107 GLY B 126 1 20
HELIX 23 AC5 SER B 136 ASN B 150 1 15
HELIX 24 AC6 ASN B 151 THR B 153 5 3
HELIX 25 AC7 LEU B 168 TYR B 172 5 5
HELIX 26 AC8 ALA B 181 GLY B 185 5 5
HELIX 27 AC9 SER B 220 ARG B 222 5 3
HELIX 28 AD1 ASP B 223 ARG B 228 1 6
HELIX 29 AD2 ALA B 238 ASP B 242 5 5
HELIX 30 AD3 GLY B 254 ALA B 258 5 5
HELIX 31 AD4 ASP B 286 GLY B 290 5 5
HELIX 32 AD5 PHE B 307 ASN B 312 1 6
HELIX 33 AD6 THR B 313 THR B 323 1 11
HELIX 34 AD7 THR B 326 ALA B 332 5 7
SHEET 1 AA1 9 THR A 16 TYR A 18 0
SHEET 2 AA1 9 GLY A 30 GLY A 32 1 O GLY A 30 N GLN A 17
SHEET 3 AA1 9 ILE A 87 VAL A 90 -1 O GLY A 89 N PHE A 31
SHEET 4 AA1 9 VAL A 43 ILE A 46 1 N PHE A 45 O PHE A 88
SHEET 5 AA1 9 VAL A 130 HIS A 135 1 O ASP A 131 N ILE A 44
SHEET 6 AA1 9 VAL A 155 LEU A 161 1 O ILE A 159 N ILE A 132
SHEET 7 AA1 9 SER A 232 SER A 237 1 O TYR A 234 N ASN A 160
SHEET 8 AA1 9 VAL A 268 ASN A 273 1 O ILE A 272 N THR A 235
SHEET 9 AA1 9 ALA A 340 ALA A 341 -1 O ALA A 340 N ASN A 273
SHEET 1 AA2 2 GLY A 201 TYR A 203 0
SHEET 2 AA2 2 VAL A 206 VAL A 208 -1 O VAL A 206 N TYR A 203
SHEET 1 AA3 9 THR B 16 TYR B 18 0
SHEET 2 AA3 9 GLY B 30 GLY B 32 1 O GLY B 30 N GLN B 17
SHEET 3 AA3 9 ILE B 87 VAL B 90 -1 O GLY B 89 N PHE B 31
SHEET 4 AA3 9 VAL B 43 ILE B 46 1 N PHE B 45 O PHE B 88
SHEET 5 AA3 9 VAL B 130 HIS B 135 1 O ASP B 131 N ILE B 44
SHEET 6 AA3 9 VAL B 155 LEU B 161 1 O ILE B 159 N ILE B 132
SHEET 7 AA3 9 SER B 232 SER B 237 1 O TYR B 234 N ASN B 160
SHEET 8 AA3 9 VAL B 268 ASN B 273 1 O ILE B 272 N THR B 235
SHEET 9 AA3 9 ALA B 340 ALA B 341 -1 O ALA B 340 N ASN B 273
SHEET 1 AA4 2 GLY B 201 TYR B 203 0
SHEET 2 AA4 2 VAL B 206 VAL B 208 -1 O VAL B 206 N TYR B 203
SSBOND 1 CYS A 3 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 36 CYS A 85 1555 1555 2.04
SSBOND 3 CYS A 171 CYS A 184 1555 1555 2.03
SSBOND 4 CYS A 246 CYS A 255 1555 1555 2.06
SSBOND 5 CYS A 325 CYS A 330 1555 1555 2.03
SSBOND 6 CYS B 3 CYS B 11 1555 1555 2.04
SSBOND 7 CYS B 36 CYS B 85 1555 1555 2.04
SSBOND 8 CYS B 171 CYS B 184 1555 1555 2.03
SSBOND 9 CYS B 246 CYS B 255 1555 1555 2.06
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.03
CRYST1 41.410 199.760 43.960 90.00 114.17 90.00 P 1 21 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 0.024149 0.000000 0.010838 0.00000
SCALE2 0.000000 0.005006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024934 0.00000
TER 2553 TYR A 342
TER 5105 TYR B 342
MASTER 433 0 0 34 22 0 0 6 6292 2 20 54
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