| content |
HEADER HYDROLASE 08-DEC-16 5MLX
TITLE OPEN 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 OTHER_DETAILS: NO ELECTRON DENSITY FOR THE LAST C-TERMINAL 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 5MLX 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) : 23.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 76716
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.127
REMARK 3 R VALUE (WORKING SET) : 0.126
REMARK 3 FREE R VALUE : 0.152
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3836
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 23.0845 - 4.7767 0.81 2489 131 0.1544 0.1508
REMARK 3 2 4.7767 - 3.7969 0.83 2531 133 0.1180 0.1274
REMARK 3 3 3.7969 - 3.3185 0.85 2601 137 0.1227 0.1314
REMARK 3 4 3.3185 - 3.0158 0.86 2613 137 0.1237 0.1668
REMARK 3 5 3.0158 - 2.8000 0.86 2616 138 0.1236 0.1699
REMARK 3 6 2.8000 - 2.6352 0.87 2648 139 0.1215 0.1296
REMARK 3 7 2.6352 - 2.5034 0.88 2690 142 0.1139 0.1564
REMARK 3 8 2.5034 - 2.3945 0.88 2671 141 0.1157 0.1259
REMARK 3 9 2.3945 - 2.3024 0.88 2667 140 0.1196 0.1392
REMARK 3 10 2.3024 - 2.2231 0.89 2706 143 0.1154 0.1361
REMARK 3 11 2.2231 - 2.1536 0.90 2772 145 0.1186 0.1664
REMARK 3 12 2.1536 - 2.0921 0.90 2724 144 0.1188 0.1528
REMARK 3 13 2.0921 - 2.0370 0.90 2704 142 0.1205 0.1549
REMARK 3 14 2.0370 - 1.9874 0.91 2796 147 0.1224 0.1550
REMARK 3 15 1.9874 - 1.9422 0.91 2703 142 0.1233 0.1476
REMARK 3 16 1.9422 - 1.9009 0.92 2835 150 0.1264 0.1628
REMARK 3 17 1.9009 - 1.8629 0.91 2725 143 0.1289 0.1488
REMARK 3 18 1.8629 - 1.8277 0.92 2837 149 0.1323 0.1745
REMARK 3 19 1.8277 - 1.7951 0.92 2702 143 0.1352 0.1683
REMARK 3 20 1.7951 - 1.7647 0.92 2842 149 0.1316 0.1747
REMARK 3 21 1.7647 - 1.7362 0.92 2777 146 0.1348 0.1714
REMARK 3 22 1.7362 - 1.7095 0.92 2795 148 0.1320 0.1684
REMARK 3 23 1.7095 - 1.6844 0.93 2864 150 0.1333 0.1569
REMARK 3 24 1.6844 - 1.6607 0.93 2766 146 0.1348 0.1857
REMARK 3 25 1.6607 - 1.6383 0.92 2809 148 0.1410 0.1754
REMARK 3 26 1.6383 - 1.6170 0.93 2828 148 0.1477 0.1759
REMARK 3 27 1.6170 - 1.5968 0.72 2169 115 0.1608 0.1844
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.40
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 5189
REMARK 3 ANGLE : 0.882 7072
REMARK 3 CHIRALITY : 0.140 749
REMARK 3 PLANARITY : 0.006 915
REMARK 3 DIHEDRAL : 12.303 2981
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 5MLX 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_1200002622.
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 : 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
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 : 77568
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 23.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 FOR THE DATA SET : 18.6000
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) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.13000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.100
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 (%): 45.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4CL, O.1 M SODIUM ACETATE, 20%
REMARK 280 PEG6000, PH 5.0, 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 99.75000
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 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 GLN B 282
REMARK 465 ALA B 283
REMARK 465 ASP B 284
REMARK 465 TYR B 285
REMARK 465 ASP B 286
REMARK 465 TRP B 287
REMARK 465 ALA B 288
REMARK 465 ASP B 289
REMARK 465 GLY B 290
REMARK 465 MET B 291
REMARK 465 PRO B 292
REMARK 465 TYR B 293
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR B 281 OG1 CG2
REMARK 470 ASN B 294 CG OD1 ND2
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 819 O HOH B 981 1.67
REMARK 500 O HOH A 1268 O HOH A 1346 1.82
REMARK 500 O HOH A 1003 O HOH A 1161 1.84
REMARK 500 O HOH A 1245 O HOH A 1288 1.84
REMARK 500 O HOH B 810 O HOH B 853 1.85
REMARK 500 O HOH B 505 O HOH B 764 1.91
REMARK 500 O HOH B 719 O HOH B 866 1.91
REMARK 500 O HOH B 748 O HOH B 854 1.94
REMARK 500 O HOH A 1021 O HOH A 1240 1.94
REMARK 500 O HOH B 871 O HOH B 967 1.94
REMARK 500 O HOH A 881 O HOH A 1171 1.97
REMARK 500 O HOH B 760 O HOH B 909 1.98
REMARK 500 O HOH A 1338 O HOH A 1389 2.00
REMARK 500 O HOH B 925 O HOH B 1018 2.00
REMARK 500 O HOH B 883 O HOH B 985 2.02
REMARK 500 O HOH B 885 O HOH B 1028 2.02
REMARK 500 O HOH A 1199 O HOH A 1213 2.03
REMARK 500 O HOH B 877 O HOH B 901 2.04
REMARK 500 O HOH B 861 O HOH B 864 2.04
REMARK 500 O HOH A 1102 O HOH A 1173 2.04
REMARK 500 O HOH B 693 O HOH B 941 2.06
REMARK 500 O HOH A 1015 O HOH A 1309 2.06
REMARK 500 O HOH A 984 O HOH A 1201 2.06
REMARK 500 O HOH B 872 O HOH B 901 2.07
REMARK 500 O HOH B 528 O HOH B 937 2.08
REMARK 500 O HOH A 1302 O HOH A 1340 2.08
REMARK 500 O HOH B 684 O HOH B 835 2.09
REMARK 500 ND2 ASN B 279 O HOH B 501 2.10
REMARK 500 O HOH A 1010 O HOH A 1136 2.10
REMARK 500 O HOH A 1043 O HOH A 1215 2.10
REMARK 500 O HOH A 804 O HOH A 980 2.10
REMARK 500 OE1 GLU A 333 O HOH A 801 2.11
REMARK 500 O HOH B 609 O HOH B 885 2.11
REMARK 500 O HOH A 872 O HOH A 1013 2.13
REMARK 500 O HOH A 888 O HOH A 1365 2.13
REMARK 500 O HOH A 837 O HOH A 892 2.14
REMARK 500 O HOH A 1281 O HOH A 1292 2.15
REMARK 500 O HOH B 658 O HOH B 725 2.16
REMARK 500 O HOH B 613 O HOH B 803 2.17
REMARK 500 O HOH B 590 O HOH B 722 2.17
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 821 O HOH A 918 1455 1.58
REMARK 500 O HOH A 844 O HOH B 522 2545 1.81
REMARK 500 O HOH B 898 O HOH B 951 1454 1.84
REMARK 500 O HOH A 823 O HOH B 512 1656 1.89
REMARK 500 O HOH A 1164 O HOH A 1172 1455 2.02
REMARK 500 O HOH B 764 O HOH B 915 1655 2.04
REMARK 500 O HOH A 984 O HOH A 1242 1454 2.06
REMARK 500 O HOH B 1016 O HOH B 1026 1554 2.12
REMARK 500 O HOH B 636 O HOH B 835 1655 2.12
REMARK 500 O HOH B 1024 O HOH B 1037 1655 2.16
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 274 CG1 - CB - CG2 ANGL. DEV. = 12.8 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 PHE A 9 -36.28 -134.25
REMARK 500 ALA A 23 88.38 -150.94
REMARK 500 SER A 136 -124.60 51.07
REMARK 500 ARG A 156 -62.28 -91.76
REMARK 500 ALA A 181 59.49 -154.10
REMARK 500 SER A 186 -157.76 -85.00
REMARK 500 ASN A 210 82.52 -154.16
REMARK 500 ALA B 23 84.73 -153.52
REMARK 500 SER B 136 -125.86 49.41
REMARK 500 ARG B 156 -62.19 -95.38
REMARK 500 ALA B 181 60.23 -155.06
REMARK 500 ASN B 210 83.14 -153.66
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 A1387 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A1388 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A1389 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A1390 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A1391 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A1392 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A1393 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A1394 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A1395 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A1396 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A1397 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH B1033 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B1034 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B1035 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1036 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH B1037 DISTANCE = 7.62 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 703 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 41 OG1
REMARK 620 2 HOH A1130 O 129.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 704 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 921 O
REMARK 620 2 HOH A 968 O 127.3
REMARK 620 3 HOH A1076 O 144.6 81.8
REMARK 620 4 HOH A1374 O 86.8 91.8 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 686 O
REMARK 620 2 HOH B 826 O 44.3
REMARK 620 3 HOH B 834 O 80.6 124.9
REMARK 620 4 HOH B 844 O 130.4 131.7 79.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402
DBREF 5MLX A 1 342 UNP Q939Q9 Q939Q9_PAULE 39 380
DBREF 5MLX B 1 342 UNP Q939Q9 Q939Q9_PAULE 39 380
SEQADV 5MLX GLU A 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQADV 5MLX LEU A 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX GLU A 344 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS A 345 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS A 346 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS A 347 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS A 348 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS A 349 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS A 350 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX GLU B 105 UNP Q939Q9 TYR 143 ENGINEERED MUTATION
SEQADV 5MLX LEU B 343 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX GLU B 344 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS B 345 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS B 346 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS B 347 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS B 348 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX HIS B 349 UNP Q939Q9 EXPRESSION TAG
SEQADV 5MLX 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
HET CL A 701 1
HET CL A 702 1
HET NA A 703 1
HET NA A 704 1
HET NA A 705 1
HET NA B 401 1
HET NA B 402 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 NA 5(NA 1+)
FORMUL 10 HOH *1134(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 SER A 170 GLY A 175 1 6
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 ALA A 247 PHE A 251 5 5
HELIX 14 AB5 GLY A 254 ALA A 258 5 5
HELIX 15 AB6 THR A 281 ALA A 288 1 8
HELIX 16 AB7 GLY A 296 THR A 301 5 6
HELIX 17 AB8 PHE A 307 ASN A 312 1 6
HELIX 18 AB9 THR A 313 THR A 323 1 11
HELIX 19 AC1 THR A 326 ALA A 332 5 7
HELIX 20 AC2 ASN B 52 MET B 58 5 7
HELIX 21 AC3 SER B 72 ARG B 80 1 9
HELIX 22 AC4 SER B 94 GLY B 99 1 6
HELIX 23 AC5 SER B 100 ASN B 104 5 5
HELIX 24 AC6 SER B 107 GLY B 126 1 20
HELIX 25 AC7 SER B 136 ASN B 150 1 15
HELIX 26 AC8 ASN B 151 THR B 153 5 3
HELIX 27 AC9 SER B 170 GLY B 175 1 6
HELIX 28 AD1 ALA B 181 GLY B 185 5 5
HELIX 29 AD2 SER B 220 ARG B 222 5 3
HELIX 30 AD3 ASP B 223 ARG B 228 1 6
HELIX 31 AD4 ALA B 238 ASP B 242 5 5
HELIX 32 AD5 ALA B 247 PHE B 251 5 5
HELIX 33 AD6 GLY B 254 ALA B 258 5 5
HELIX 34 AD7 PHE B 307 ASN B 312 1 6
HELIX 35 AD8 THR B 313 THR B 323 1 11
HELIX 36 AD9 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 208 N GLY B 201
SSBOND 1 CYS A 3 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 36 CYS A 85 1555 1555 2.05
SSBOND 3 CYS A 171 CYS A 184 1555 1555 2.04
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 2.06
SSBOND 7 CYS B 36 CYS B 85 1555 1555 2.04
SSBOND 8 CYS B 171 CYS B 184 1555 1555 2.05
SSBOND 9 CYS B 246 CYS B 255 1555 1555 2.05
SSBOND 10 CYS B 325 CYS B 330 1555 1555 2.03
LINK OG1 THR A 41 NA NA A 703 1555 1555 3.05
LINK NA NA A 703 O HOH A1130 1555 1555 2.03
LINK NA NA A 704 O HOH A 921 1555 1555 2.75
LINK NA NA A 704 O HOH A 968 1555 1555 2.67
LINK NA NA A 704 O HOH A1076 1555 1555 2.78
LINK NA NA A 704 O HOH A1374 1555 1555 3.02
LINK NA NA B 401 O HOH B 932 1555 1555 3.10
LINK NA NA B 402 O HOH B 686 1555 1555 2.95
LINK NA NA B 402 O HOH B 826 1555 1555 2.96
LINK NA NA B 402 O HOH B 834 1555 1555 3.09
LINK NA NA B 402 O HOH B 844 1555 1556 2.93
SITE 1 AC1 4 ALA A 23 PRO A 24 GLY A 25 HOH A1310
SITE 1 AC2 5 GLN A 15 SER A 95 THR A 326 LEU A 328
SITE 2 AC2 5 ASP A 329
SITE 1 AC3 3 THR A 41 GLN A 129 HOH A1130
SITE 1 AC4 5 PHE A 197 HOH A 921 HOH A 968 HOH A1076
SITE 2 AC4 5 HOH A1374
SITE 1 AC5 2 ASN A 83 ASP A 84
SITE 1 AC6 3 ALA B 23 PRO B 24 GLY B 25
SITE 1 AC7 7 THR B 326 LEU B 328 ASP B 329 HOH B 686
SITE 2 AC7 7 HOH B 826 HOH B 834 HOH B 844
CRYST1 41.300 199.500 44.400 90.00 114.20 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 0.024213 0.000000 0.010882 0.00000
SCALE2 0.000000 0.005013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024692 0.00000
TER 2581 LEU A 343
TER 5042 TYR B 342
MASTER 488 0 7 36 22 0 10 6 6134 2 34 54
END |