| content |
HEADER HYDROLASE 26-JUN-13 4BVL
TITLE STRUCTURE OF 202-208 DELETION MUTANT OF PHAZ7 PHB DEPOLYMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHB DEPOLYMERASE PHAZ7;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 39-380;
COMPND 5 EC: 3.1.1.75;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PAUCIMONAS LEMOIGNEI;
SOURCE 3 ORGANISM_TAXID: 29443;
SOURCE 4 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: WB800
KEYWDS HYDROLASE, CATALYTIC TRIAD, BIOPOLYMER BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU,D.JENDROSSEK
REVDAT 1 18-SEP-13 4BVL 0
JRNL AUTH D.JENDROSSEK,S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU
JRNL TITL BIOCHEMICAL ANALYSIS AND STRUCTURE DETERMINATION OF
JRNL TITL 2 PAUCIMONAS LEMOIGNEI POLY(3-HYDROXYBUTYRATE) (PHB)
JRNL TITL 3 DEPOLYMERASE PHAZ7 MUTEINS REVEAL THE PHB BINDING SITE AND
JRNL TITL 4 DETAILS OF SUBSTRATE-ENZYME INTERACTIONS.
JRNL REF MOL.MICROBIOL. 2013
JRNL REFN ESSN 1365-2958
JRNL PMID 24007310
JRNL DOI 10.1111/MMI.12391
REMARK 1
REMARK 1 REFERENCE 1
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 ISSN 0022-2836
REMARK 1 PMID 18706425
REMARK 1 DOI 10.1016/J.JMB.2008.07.078
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.002
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.558
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.99
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.70
REMARK 3 NUMBER OF REFLECTIONS : 74248
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1190
REMARK 3 R VALUE (WORKING SET) : 0.1152
REMARK 3 FREE R VALUE : 0.1908
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3711
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 19.5590 - 5.9524 0.95 2649 140 0.1582 0.2042
REMARK 3 2 5.9524 - 4.7468 0.98 2687 140 0.1128 0.1350
REMARK 3 3 4.7468 - 4.1533 0.99 2645 140 0.0940 0.1582
REMARK 3 4 4.1533 - 3.7766 0.99 2661 140 0.1004 0.1475
REMARK 3 5 3.7766 - 3.5075 0.99 2650 139 0.1105 0.1815
REMARK 3 6 3.5075 - 3.3018 1.00 2648 140 0.1171 0.2072
REMARK 3 7 3.3018 - 3.1371 1.00 2643 139 0.1226 0.2151
REMARK 3 8 3.1371 - 3.0011 1.00 2638 139 0.1183 0.1601
REMARK 3 9 3.0011 - 2.8859 1.00 2637 138 0.1181 0.1990
REMARK 3 10 2.8859 - 2.7866 1.00 2635 138 0.1190 0.1975
REMARK 3 11 2.7866 - 2.6997 1.00 2628 139 0.1138 0.1831
REMARK 3 12 2.6997 - 2.6227 1.00 2653 139 0.1127 0.1956
REMARK 3 13 2.6227 - 2.5538 1.00 2629 139 0.1106 0.1947
REMARK 3 14 2.5538 - 2.4917 1.00 2654 139 0.1140 0.2218
REMARK 3 15 2.4917 - 2.4351 1.00 2628 139 0.1142 0.1897
REMARK 3 16 2.4351 - 2.3834 1.00 2604 137 0.1052 0.1907
REMARK 3 17 2.3834 - 2.3358 1.00 2619 137 0.1042 0.2120
REMARK 3 18 2.3358 - 2.2918 1.00 2659 140 0.1047 0.1832
REMARK 3 19 2.2918 - 2.2509 1.00 2603 137 0.1085 0.2205
REMARK 3 20 2.2509 - 2.2128 1.00 2621 138 0.1113 0.1770
REMARK 3 21 2.2128 - 2.1772 1.00 2612 138 0.1114 0.2198
REMARK 3 22 2.1772 - 2.1437 1.00 2628 138 0.1182 0.2036
REMARK 3 23 2.1437 - 2.1122 1.00 2605 137 0.1165 0.1971
REMARK 3 24 2.1122 - 2.0825 1.00 2633 139 0.1218 0.2064
REMARK 3 25 2.0825 - 2.0544 1.00 2619 138 0.1236 0.2204
REMARK 3 26 2.0544 - 2.0277 1.00 2601 136 0.1327 0.2560
REMARK 3 27 2.0277 - 2.0024 0.78 2048 108 0.1684 0.2382
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.17
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.7
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 : 0.013 10237
REMARK 3 ANGLE : 1.319 13883
REMARK 3 CHIRALITY : 0.076 1470
REMARK 3 PLANARITY : 0.007 1814
REMARK 3 DIHEDRAL : 12.544 3487
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 4BVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-13.
REMARK 100 THE PDBE ID CODE IS EBI-57482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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 (SX-165)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74317
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 19.60
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 5.2
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.2
REMARK 200 R MERGE FOR SHELL (I) : 0.33
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4BRS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOUR DIFFUSION.
REMARK 280 PROTEIN CONCENTRATION 10 MG/ML. 0.1 M NAOAC (PH 5.0), 0.2
REMARK 280 M LICL, 15% W/V PEG6000
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 86.18350
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 86.18350
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 46.61950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.41450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.61950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.41450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 86.18350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.61950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.41450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 86.18350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.61950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.41450
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, 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: 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 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: 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: 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 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 A2205 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C2176 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D2417 LIES ON A SPECIAL POSITION.
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 PRO C 69 O HOH C 2159 2.18
REMARK 500 OG SER D 136 O HOH D 2108 2.20
REMARK 500 O ALA D 179 O HOH D 2280 2.09
REMARK 500 O HOH A 2099 O HOH A 2100 2.12
REMARK 500 O HOH A 2111 O HOH A 2210 2.13
REMARK 500 O HOH A 2126 O HOH A 2297 2.10
REMARK 500 O HOH A 2138 O HOH A 2303 2.19
REMARK 500 O HOH A 2141 O HOH D 2397 2.09
REMARK 500 O HOH A 2425 O HOH A 2475 2.17
REMARK 500 O HOH A 2491 O HOH A 2492 2.20
REMARK 500 O HOH B 2028 O HOH B 2036 2.20
REMARK 500 O HOH B 2040 O HOH B 2080 2.18
REMARK 500 O HOH B 2042 O HOH B 2082 2.08
REMARK 500 O HOH B 2053 O HOH B 2054 2.17
REMARK 500 O HOH B 2445 O HOH B 2447 2.16
REMARK 500 O HOH C 2067 O HOH C 2068 2.15
REMARK 500 O HOH C 2086 O HOH C 2087 2.13
REMARK 500 O HOH C 2132 O HOH C 2274 2.20
REMARK 500 O HOH C 2163 O HOH C 2164 2.15
REMARK 500 O HOH C 2276 O HOH C 2429 2.15
REMARK 500 O HOH C 2282 O HOH C 2283 2.17
REMARK 500 O HOH C 2312 O HOH C 2315 2.14
REMARK 500 O HOH C 2335 O HOH C 2340 2.14
REMARK 500 O HOH D 2022 O HOH D 2074 2.19
REMARK 500 O HOH D 2069 O HOH D 2136 2.11
REMARK 500 O HOH D 2135 O HOH D 2271 2.17
REMARK 500 O HOH D 2197 O HOH D 2370 2.18
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 ND2 ASN D 62 O HOH B 2264 5445 2.09
REMARK 500 O HOH A 2067 O HOH D 2067 8445 2.19
REMARK 500 O HOH C 2063 O HOH A 2127 8545 2.06
REMARK 500 O HOH D 2008 O HOH D 2008 4545 2.19
REMARK 500 O HOH D 2287 O HOH A 2289 5545 2.18
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 85.42 -150.97
REMARK 500 SER A 136 -130.82 55.90
REMARK 500 ALA A 181 72.58 -150.46
REMARK 500 GLU A 200 -138.33 56.84
REMARK 500 ARG A 228 66.30 -103.33
REMARK 500 PHE A 251 38.11 -141.23
REMARK 500 PHE B 9 -6.84 78.95
REMARK 500 SER B 136 -132.72 60.32
REMARK 500 ARG B 156 -65.06 -93.48
REMARK 500 ALA B 181 66.14 -154.57
REMARK 500 SER B 186 -156.22 -87.34
REMARK 500 GLU B 200 -143.12 56.97
REMARK 500 ARG B 228 72.52 -101.81
REMARK 500 SER C 55 -6.65 -59.39
REMARK 500 SER C 136 -132.72 56.19
REMARK 500 ARG C 156 -63.32 -94.41
REMARK 500 ALA C 181 59.32 -151.80
REMARK 500 SER C 186 -155.88 -83.49
REMARK 500 GLU C 200 -132.73 57.58
REMARK 500 ALA D 23 86.21 -152.02
REMARK 500 TYR D 66 -38.31 -135.66
REMARK 500 SER D 136 -136.53 57.19
REMARK 500 ARG D 156 -61.38 -91.94
REMARK 500 ALA D 181 67.54 -155.11
REMARK 500 SER D 186 -148.44 -92.41
REMARK 500 GLU D 200 -140.27 57.52
REMARK 500 ARG D 228 72.26 -109.17
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 A2044 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH A2234 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A2494 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH B2247 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH C2025 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C2066 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH C2213 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH C2447 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH D2137 DISTANCE = 7.30 ANGSTROMS
REMARK 525 HOH D2139 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH D2413 DISTANCE = 8.09 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BTV RELATED DB: PDB
REMARK 900 STRUCTURE OF PHAZ7 PHB DEPOLYMERASE IN COMPLEX WITH
REMARK 900 3HB TRIMER
REMARK 900 RELATED ID: 4BVJ RELATED DB: PDB
REMARK 900 STRUCTURE OF Y105A MUTANT OF PHAZ7 PHB DEPOLYMERASE
REMARK 900 RELATED ID: 4BVK RELATED DB: PDB
REMARK 900 STRUCTURE OF Y190E MUTANT OF PHAZ7 PHB DEPOLYMERASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 202-208 HAVE BEEN DELETED
DBREF 4BVL A 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BVL B 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BVL C 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 4BVL D 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
SEQADV 4BVL A UNP Q939Q9 TRP 240 DELETION
SEQADV 4BVL A UNP Q939Q9 TYR 241 DELETION
SEQADV 4BVL A UNP Q939Q9 TYR 242 DELETION
SEQADV 4BVL A UNP Q939Q9 GLY 243 DELETION
SEQADV 4BVL A UNP Q939Q9 VAL 244 DELETION
SEQADV 4BVL A UNP Q939Q9 TRP 245 DELETION
SEQADV 4BVL A UNP Q939Q9 VAL 246 DELETION
SEQADV 4BVL B UNP Q939Q9 TRP 240 DELETION
SEQADV 4BVL B UNP Q939Q9 TYR 241 DELETION
SEQADV 4BVL B UNP Q939Q9 TYR 242 DELETION
SEQADV 4BVL B UNP Q939Q9 GLY 243 DELETION
SEQADV 4BVL B UNP Q939Q9 VAL 244 DELETION
SEQADV 4BVL B UNP Q939Q9 TRP 245 DELETION
SEQADV 4BVL B UNP Q939Q9 VAL 246 DELETION
SEQADV 4BVL C UNP Q939Q9 TRP 240 DELETION
SEQADV 4BVL C UNP Q939Q9 TYR 241 DELETION
SEQADV 4BVL C UNP Q939Q9 TYR 242 DELETION
SEQADV 4BVL C UNP Q939Q9 GLY 243 DELETION
SEQADV 4BVL C UNP Q939Q9 VAL 244 DELETION
SEQADV 4BVL C UNP Q939Q9 TRP 245 DELETION
SEQADV 4BVL C UNP Q939Q9 VAL 246 DELETION
SEQADV 4BVL D UNP Q939Q9 TRP 240 DELETION
SEQADV 4BVL D UNP Q939Q9 TYR 241 DELETION
SEQADV 4BVL D UNP Q939Q9 TYR 242 DELETION
SEQADV 4BVL D UNP Q939Q9 GLY 243 DELETION
SEQADV 4BVL D UNP Q939Q9 VAL 244 DELETION
SEQADV 4BVL D UNP Q939Q9 TRP 245 DELETION
SEQADV 4BVL D UNP Q939Q9 VAL 246 DELETION
SEQRES 1 A 335 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 A 335 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 A 335 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 A 335 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 A 335 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 A 335 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 A 335 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 A 335 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 A 335 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 A 335 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 A 335 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 A 335 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 A 335 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 A 335 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 A 335 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 A 335 GLY PHE PHE PRO GLU GLY SER ASN PRO TRP THR GLY SER
SEQRES 17 A 335 GLY SER THR ASN SER MET ARG ASP MET PRO ALA LYS ARG
SEQRES 18 A 335 THR ALA VAL SER PHE TYR THR LEU SER ALA GLY PHE LYS
SEQRES 19 A 335 ASP GLN VAL GLY CYS ALA THR ALA SER PHE TRP ALA GLY
SEQRES 20 A 335 CYS ASP SER ALA ALA LYS PHE ALA SER THR THR SER ASN
SEQRES 21 A 335 VAL LYS ALA GLN ILE ASN VAL GLY ALA GLY SER ASN ALA
SEQRES 22 A 335 THR GLN ALA ASP TYR ASP TRP ALA ASP GLY MET PRO TYR
SEQRES 23 A 335 ASN ALA GLY GLY GLY ASP THR THR ASN GLY VAL GLY HIS
SEQRES 24 A 335 PHE ARG THR LYS THR ASN THR GLY ALA ILE ILE GLN ARG
SEQRES 25 A 335 MET LEU LEU THR THR CYS THR GLY LEU ASP CYS ALA ALA
SEQRES 26 A 335 GLU TYR THR THR GLY PRO LYS ALA ALA TYR
SEQRES 1 B 335 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 B 335 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 B 335 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 B 335 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 B 335 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 B 335 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 B 335 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 B 335 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 B 335 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 B 335 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 B 335 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 B 335 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 B 335 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 B 335 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 B 335 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 B 335 GLY PHE PHE PRO GLU GLY SER ASN PRO TRP THR GLY SER
SEQRES 17 B 335 GLY SER THR ASN SER MET ARG ASP MET PRO ALA LYS ARG
SEQRES 18 B 335 THR ALA VAL SER PHE TYR THR LEU SER ALA GLY PHE LYS
SEQRES 19 B 335 ASP GLN VAL GLY CYS ALA THR ALA SER PHE TRP ALA GLY
SEQRES 20 B 335 CYS ASP SER ALA ALA LYS PHE ALA SER THR THR SER ASN
SEQRES 21 B 335 VAL LYS ALA GLN ILE ASN VAL GLY ALA GLY SER ASN ALA
SEQRES 22 B 335 THR GLN ALA ASP TYR ASP TRP ALA ASP GLY MET PRO TYR
SEQRES 23 B 335 ASN ALA GLY GLY GLY ASP THR THR ASN GLY VAL GLY HIS
SEQRES 24 B 335 PHE ARG THR LYS THR ASN THR GLY ALA ILE ILE GLN ARG
SEQRES 25 B 335 MET LEU LEU THR THR CYS THR GLY LEU ASP CYS ALA ALA
SEQRES 26 B 335 GLU TYR THR THR GLY PRO LYS ALA ALA TYR
SEQRES 1 C 335 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 C 335 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 C 335 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 C 335 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 C 335 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 C 335 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 C 335 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 C 335 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 C 335 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 C 335 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 C 335 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 C 335 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 C 335 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 C 335 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 C 335 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 C 335 GLY PHE PHE PRO GLU GLY SER ASN PRO TRP THR GLY SER
SEQRES 17 C 335 GLY SER THR ASN SER MET ARG ASP MET PRO ALA LYS ARG
SEQRES 18 C 335 THR ALA VAL SER PHE TYR THR LEU SER ALA GLY PHE LYS
SEQRES 19 C 335 ASP GLN VAL GLY CYS ALA THR ALA SER PHE TRP ALA GLY
SEQRES 20 C 335 CYS ASP SER ALA ALA LYS PHE ALA SER THR THR SER ASN
SEQRES 21 C 335 VAL LYS ALA GLN ILE ASN VAL GLY ALA GLY SER ASN ALA
SEQRES 22 C 335 THR GLN ALA ASP TYR ASP TRP ALA ASP GLY MET PRO TYR
SEQRES 23 C 335 ASN ALA GLY GLY GLY ASP THR THR ASN GLY VAL GLY HIS
SEQRES 24 C 335 PHE ARG THR LYS THR ASN THR GLY ALA ILE ILE GLN ARG
SEQRES 25 C 335 MET LEU LEU THR THR CYS THR GLY LEU ASP CYS ALA ALA
SEQRES 26 C 335 GLU TYR THR THR GLY PRO LYS ALA ALA TYR
SEQRES 1 D 335 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 D 335 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 D 335 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 D 335 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 D 335 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 D 335 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 D 335 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 D 335 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 D 335 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 D 335 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 D 335 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 D 335 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 D 335 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 D 335 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 D 335 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 D 335 GLY PHE PHE PRO GLU GLY SER ASN PRO TRP THR GLY SER
SEQRES 17 D 335 GLY SER THR ASN SER MET ARG ASP MET PRO ALA LYS ARG
SEQRES 18 D 335 THR ALA VAL SER PHE TYR THR LEU SER ALA GLY PHE LYS
SEQRES 19 D 335 ASP GLN VAL GLY CYS ALA THR ALA SER PHE TRP ALA GLY
SEQRES 20 D 335 CYS ASP SER ALA ALA LYS PHE ALA SER THR THR SER ASN
SEQRES 21 D 335 VAL LYS ALA GLN ILE ASN VAL GLY ALA GLY SER ASN ALA
SEQRES 22 D 335 THR GLN ALA ASP TYR ASP TRP ALA ASP GLY MET PRO TYR
SEQRES 23 D 335 ASN ALA GLY GLY GLY ASP THR THR ASN GLY VAL GLY HIS
SEQRES 24 D 335 PHE ARG THR LYS THR ASN THR GLY ALA ILE ILE GLN ARG
SEQRES 25 D 335 MET LEU LEU THR THR CYS THR GLY LEU ASP CYS ALA ALA
SEQRES 26 D 335 GLU TYR THR THR GLY PRO LYS ALA ALA TYR
FORMUL 5 HOH *1803(H2 O)
HELIX 1 1 ASN A 52 MET A 58 5 7
HELIX 2 2 SER A 72 ARG A 80 1 9
HELIX 3 3 SER A 94 SER A 100 1 7
HELIX 4 4 ALA A 101 ASN A 104 5 4
HELIX 5 5 SER A 107 GLY A 126 1 20
HELIX 6 6 SER A 136 ASN A 150 1 15
HELIX 7 7 ASN A 151 THR A 153 5 3
HELIX 8 8 SER A 170 GLY A 175 1 6
HELIX 9 9 ALA A 181 GLY A 185 5 5
HELIX 10 10 SER A 220 ARG A 222 5 3
HELIX 11 11 ASP A 223 ARG A 228 1 6
HELIX 12 12 ALA A 238 LYS A 241 5 4
HELIX 13 13 ASP A 242 ALA A 247 1 6
HELIX 14 14 GLY A 254 ALA A 258 5 5
HELIX 15 15 ASP A 286 GLY A 290 5 5
HELIX 16 16 PHE A 307 ASN A 312 1 6
HELIX 17 17 THR A 313 THR A 323 1 11
HELIX 18 18 THR A 326 ALA A 332 5 7
HELIX 19 19 ASN B 52 MET B 58 5 7
HELIX 20 20 SER B 72 ARG B 80 1 9
HELIX 21 21 SER B 94 SER B 100 1 7
HELIX 22 22 ALA B 101 ASN B 104 5 4
HELIX 23 23 SER B 107 GLY B 126 1 20
HELIX 24 24 SER B 136 ASN B 150 1 15
HELIX 25 25 ASN B 151 THR B 153 5 3
HELIX 26 26 SER B 170 GLY B 175 1 6
HELIX 27 27 ALA B 181 GLY B 185 5 5
HELIX 28 28 SER B 220 ARG B 222 5 3
HELIX 29 29 ASP B 223 ARG B 228 1 6
HELIX 30 30 ALA B 238 ASP B 242 5 5
HELIX 31 31 GLY B 254 ALA B 258 5 5
HELIX 32 32 ASP B 286 GLY B 290 5 5
HELIX 33 33 PHE B 307 ASN B 312 1 6
HELIX 34 34 THR B 313 THR B 323 1 11
HELIX 35 35 THR B 326 ALA B 332 5 7
HELIX 36 36 ASN C 52 MET C 58 5 7
HELIX 37 37 SER C 72 ARG C 80 1 9
HELIX 38 38 SER C 94 SER C 100 1 7
HELIX 39 39 ALA C 101 ASN C 104 5 4
HELIX 40 40 SER C 107 GLY C 126 1 20
HELIX 41 41 SER C 136 ASN C 150 1 15
HELIX 42 42 ASN C 151 THR C 153 5 3
HELIX 43 43 SER C 170 GLY C 175 1 6
HELIX 44 44 ALA C 181 GLY C 185 5 5
HELIX 45 45 SER C 220 ARG C 222 5 3
HELIX 46 46 ASP C 223 ARG C 228 1 6
HELIX 47 47 ALA C 238 ASP C 242 5 5
HELIX 48 48 GLY C 254 ALA C 258 5 5
HELIX 49 49 ASP C 286 GLY C 290 5 5
HELIX 50 50 PHE C 307 ASN C 312 1 6
HELIX 51 51 THR C 313 THR C 323 1 11
HELIX 52 52 THR C 326 ALA C 332 5 7
HELIX 53 53 ASN D 52 MET D 58 5 7
HELIX 54 54 SER D 72 ARG D 80 1 9
HELIX 55 55 SER D 94 SER D 100 1 7
HELIX 56 56 ALA D 101 ASN D 104 5 4
HELIX 57 57 SER D 107 GLY D 126 1 20
HELIX 58 58 SER D 136 ASN D 150 1 15
HELIX 59 59 ASN D 151 THR D 153 5 3
HELIX 60 60 SER D 170 GLY D 175 1 6
HELIX 61 61 ALA D 181 GLY D 185 5 5
HELIX 62 62 SER D 220 ARG D 222 5 3
HELIX 63 63 ASP D 223 ARG D 228 1 6
HELIX 64 64 ALA D 238 ASP D 242 5 5
HELIX 65 65 GLY D 254 ALA D 258 5 5
HELIX 66 66 ASP D 286 GLY D 290 5 5
HELIX 67 67 PHE D 307 ASN D 312 1 6
HELIX 68 68 THR D 313 THR D 323 1 11
HELIX 69 69 THR D 326 ALA D 332 5 7
SHEET 1 AA 9 THR A 16 TYR A 18 0
SHEET 2 AA 9 GLY A 30 GLY A 32 1 O GLY A 30 N GLN A 17
SHEET 3 AA 9 ILE A 87 VAL A 90 -1 O GLY A 89 N PHE A 31
SHEET 4 AA 9 VAL A 43 ILE A 46 1 O VAL A 43 N PHE A 88
SHEET 5 AA 9 VAL A 130 HIS A 135 1 O ASP A 131 N ILE A 44
SHEET 6 AA 9 VAL A 155 LEU A 161 1 N ARG A 156 O VAL A 130
SHEET 7 AA 9 SER A 232 SER A 237 1 O SER A 232 N PHE A 158
SHEET 8 AA 9 VAL A 268 ASN A 273 1 N LYS A 269 O PHE A 233
SHEET 9 AA 9 ALA A 340 ALA A 341 -1 O ALA A 340 N ASN A 273
SHEET 1 BA 2 ASN B 6 SER B 7 0
SHEET 2 BA 2 VAL B 10 CYS B 11 -1 O VAL B 10 N SER B 7
SHEET 1 BB 9 THR B 16 TYR B 18 0
SHEET 2 BB 9 GLY B 30 GLY B 32 1 O GLY B 30 N GLN B 17
SHEET 3 BB 9 ILE B 87 VAL B 90 -1 O GLY B 89 N PHE B 31
SHEET 4 BB 9 VAL B 43 ILE B 46 1 O VAL B 43 N PHE B 88
SHEET 5 BB 9 VAL B 130 HIS B 135 1 O ASP B 131 N ILE B 44
SHEET 6 BB 9 VAL B 155 LEU B 161 1 N ARG B 156 O VAL B 130
SHEET 7 BB 9 SER B 232 SER B 237 1 O SER B 232 N PHE B 158
SHEET 8 BB 9 VAL B 268 ASN B 273 1 N LYS B 269 O PHE B 233
SHEET 9 BB 9 ALA B 340 ALA B 341 -1 O ALA B 340 N ASN B 273
SHEET 1 CA 9 THR C 16 TYR C 18 0
SHEET 2 CA 9 GLY C 30 GLY C 32 1 O GLY C 30 N GLN C 17
SHEET 3 CA 9 ILE C 87 VAL C 90 -1 O GLY C 89 N PHE C 31
SHEET 4 CA 9 VAL C 43 ILE C 46 1 O VAL C 43 N PHE C 88
SHEET 5 CA 9 VAL C 130 HIS C 135 1 O ASP C 131 N ILE C 44
SHEET 6 CA 9 VAL C 155 LEU C 161 1 N ARG C 156 O VAL C 130
SHEET 7 CA 9 SER C 232 SER C 237 1 O SER C 232 N PHE C 158
SHEET 8 CA 9 VAL C 268 ASN C 273 1 N LYS C 269 O PHE C 233
SHEET 9 CA 9 ALA C 340 ALA C 341 -1 O ALA C 340 N ASN C 273
SHEET 1 DA 9 THR D 16 TYR D 18 0
SHEET 2 DA 9 GLY D 30 GLY D 32 1 O GLY D 30 N GLN D 17
SHEET 3 DA 9 ILE D 87 VAL D 90 -1 O GLY D 89 N PHE D 31
SHEET 4 DA 9 VAL D 43 ILE D 46 1 O VAL D 43 N PHE D 88
SHEET 5 DA 9 VAL D 130 HIS D 135 1 O ASP D 131 N ILE D 44
SHEET 6 DA 9 VAL D 155 LEU D 161 1 N ARG D 156 O VAL D 130
SHEET 7 DA 9 SER D 232 SER D 237 1 O SER D 232 N PHE D 158
SHEET 8 DA 9 VAL D 268 ASN D 273 1 N LYS D 269 O PHE D 233
SHEET 9 DA 9 ALA D 340 ALA D 341 -1 O ALA D 340 N ASN D 273
SSBOND 1 CYS A 3 CYS A 11 1555 1555 2.03
SSBOND 2 CYS A 36 CYS A 85 1555 1555 2.02
SSBOND 3 CYS A 171 CYS A 184 1555 1555 2.02
SSBOND 4 CYS A 246 CYS A 255 1555 1555 2.04
SSBOND 5 CYS A 325 CYS A 330 1555 1555 2.04
SSBOND 6 CYS B 3 CYS B 11 1555 1555 2.03
SSBOND 7 CYS B 36 CYS B 85 1555 1555 2.05
SSBOND 8 CYS B 171 CYS B 184 1555 1555 2.06
SSBOND 9 CYS B 246 CYS B 255 1555 1555 2.08
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.05
SSBOND 11 CYS C 3 CYS C 11 1555 1555 2.03
SSBOND 12 CYS C 36 CYS C 85 1555 1555 2.04
SSBOND 13 CYS C 171 CYS C 184 1555 1555 2.07
SSBOND 14 CYS C 246 CYS C 255 1555 1555 2.04
SSBOND 15 CYS C 325 CYS C 330 1555 1555 2.05
SSBOND 16 CYS D 3 CYS D 11 1555 1555 2.04
SSBOND 17 CYS D 36 CYS D 85 1555 1555 2.04
SSBOND 18 CYS D 171 CYS D 184 1555 1555 2.04
SSBOND 19 CYS D 246 CYS D 255 1555 1555 2.08
SSBOND 20 CYS D 325 CYS D 330 1555 1555 2.06
CRYST1 93.239 138.829 172.367 90.00 90.00 90.00 C 2 2 21 32
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 0.010725 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007203 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005802 0.00000
TER 2491 TYR A 342
TER 4979 TYR B 342
TER 7465 TYR C 342
TER 9959 TYR D 342
MASTER 416 0 0 69 38 0 0 611758 4 45 104
END |