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HEADER HYDROLASE 13-FEB-13 4J7A
TITLE CRYSTAL STRUCTURE OF EST25 - A BACTERIAL HOMOLOG OF HORMONE-SENSITIVE
TITLE 2 LIPASE FROM A METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS ALPHA/BETA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.NGO,B.H.RYU,H.S.JU,E.J.JANG,K.S.PARK,S.B.JOO,K.K.KIM,D.H.KIM
REVDAT 1 15-JAN-14 4J7A 0
JRNL AUTH T.D.NGO,B.H.RYU,H.JU,E.JANG,K.PARK,K.K.KIM,D.H.KIM
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSES OF A BACTERIAL HOMOLOGUE
JRNL TITL 2 OF HORMONE-SENSITIVE LIPASE FROM A METAGENOMIC LIBRARY
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 1726 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 23999296
JRNL DOI 10.1107/S0907444913013425
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1063)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 285892
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 14491
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 28.5600 - 4.6298 0.88 8375 482 0.1861 0.2019
REMARK 3 2 4.6298 - 3.6773 0.93 8746 473 0.1429 0.1494
REMARK 3 3 3.6773 - 3.2132 0.98 9223 504 0.1383 0.1478
REMARK 3 4 3.2132 - 2.9197 0.99 9364 471 0.1554 0.1794
REMARK 3 5 2.9197 - 2.7106 0.99 9398 452 0.1561 0.1645
REMARK 3 6 2.7106 - 2.5509 0.99 9306 471 0.1507 0.1822
REMARK 3 7 2.5509 - 2.4232 0.99 9308 517 0.1467 0.1878
REMARK 3 8 2.4232 - 2.3178 0.99 9282 506 0.1375 0.1582
REMARK 3 9 2.3178 - 2.2286 0.99 9251 504 0.1340 0.1634
REMARK 3 10 2.2286 - 2.1517 0.98 9206 480 0.1307 0.1646
REMARK 3 11 2.1517 - 2.0845 0.98 9224 463 0.1273 0.1538
REMARK 3 12 2.0845 - 2.0249 0.98 9197 452 0.1299 0.1606
REMARK 3 13 2.0249 - 1.9716 0.98 9196 496 0.1362 0.1693
REMARK 3 14 1.9716 - 1.9235 0.98 9131 465 0.1343 0.1691
REMARK 3 15 1.9235 - 1.8798 0.97 9097 510 0.1324 0.1700
REMARK 3 16 1.8798 - 1.8398 0.97 9059 513 0.1268 0.1608
REMARK 3 17 1.8398 - 1.8030 0.97 9085 502 0.1288 0.1597
REMARK 3 18 1.8030 - 1.7690 0.97 9035 477 0.1360 0.1955
REMARK 3 19 1.7690 - 1.7374 0.97 9068 495 0.1368 0.1774
REMARK 3 20 1.7374 - 1.7079 0.96 9029 486 0.1249 0.1611
REMARK 3 21 1.7079 - 1.6804 0.96 9055 453 0.1238 0.1630
REMARK 3 22 1.6804 - 1.6545 0.96 8979 503 0.1256 0.1655
REMARK 3 23 1.6545 - 1.6302 0.96 8981 498 0.1270 0.1722
REMARK 3 24 1.6302 - 1.6073 0.96 8931 503 0.1255 0.1642
REMARK 3 25 1.6073 - 1.5855 0.96 8965 457 0.1250 0.1605
REMARK 3 26 1.5855 - 1.5649 0.95 8812 509 0.1288 0.1677
REMARK 3 27 1.5649 - 1.5454 0.96 8945 467 0.1389 0.1791
REMARK 3 28 1.5454 - 1.5268 0.95 8836 500 0.1447 0.2033
REMARK 3 29 1.5268 - 1.5090 0.95 8854 479 0.1640 0.2228
REMARK 3 30 1.5090 - 1.4920 0.90 8463 403 0.1711 0.2223
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.900
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) : 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 : 0.006 10812
REMARK 3 ANGLE : 1.177 14760
REMARK 3 CHIRALITY : 0.078 1652
REMARK 3 PLANARITY : 0.006 1956
REMARK 3 DIHEDRAL : 12.701 3860
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 4J7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 203
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97888, 0.97917, 0.96395,
REMARK 200 1.00000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 285917
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 50.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.31600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M SODIUM MALONATE PH 7.0,
REMARK 280 MICROBATCH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 98.87900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.60650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 98.87900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.60650
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 674 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 697 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 LEU A 6
REMARK 465 ASN A 7
REMARK 465 MET B -11
REMARK 465 ARG B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASN B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 LEU B 6
REMARK 465 ASN B 7
REMARK 465 MET C -11
REMARK 465 ARG C -10
REMARK 465 GLY C -9
REMARK 465 SER C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ASN C 3
REMARK 465 ALA C 4
REMARK 465 THR C 5
REMARK 465 LEU C 6
REMARK 465 ASN C 7
REMARK 465 MET D -11
REMARK 465 ARG D -10
REMARK 465 GLY D -9
REMARK 465 SER D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 ASN D 3
REMARK 465 ALA D 4
REMARK 465 THR D 5
REMARK 465 LEU D 6
REMARK 465 ASN D 7
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 441 O HOH B 483 2.03
REMARK 500 O HOH A 525 O HOH B 610 2.09
REMARK 500 OD2 ASP C 56 O HOH C 833 2.09
REMARK 500 OD2 ASP A 86 O HOH A 726 2.09
REMARK 500 O HOH D 862 O HOH D 882 2.09
REMARK 500 O HOH B 607 O HOH B 813 2.10
REMARK 500 O HOH D 768 O HOH D 922 2.12
REMARK 500 OE2 GLU D 243 O HOH D 854 2.14
REMARK 500 OE1 GLU D 53 O HOH D 678 2.15
REMARK 500 OE1 GLU A 243 O HOH A 699 2.16
REMARK 500 O HOH C 440 O HOH C 728 2.16
REMARK 500 O GLY D 79 O HOH D 787 2.16
REMARK 500 O HOH B 653 O HOH B 789 2.17
REMARK 500 O HOH B 531 O HOH B 564 2.17
REMARK 500 O HOH B 823 O HOH B 892 2.18
REMARK 500 O HOH B 798 O HOH B 815 2.18
REMARK 500 OE1 GLU C 272 O HOH C 583 2.18
REMARK 500 O HOH A 893 O HOH A 936 2.18
REMARK 500 O HOH C 542 O HOH C 551 2.18
REMARK 500 O HOH C 476 O HOH C 728 2.18
REMARK 500 O HOH A 901 O HOH A 950 2.19
REMARK 500 OD1 ASP A 353 O HOH A 504 2.19
REMARK 500 O HOH D 575 O HOH D 706 2.19
REMARK 500 NZ LYS C 93 O HOH C 815 2.19
REMARK 500 O HOH B 813 O HOH B 892 2.19
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 LEU A 195 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 LEU B 195 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 GLY C 76 N - CA - C ANGL. DEV. = 16.0 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 GLN A 78 42.65 -81.72
REMARK 500 LEU A 131 156.37 79.64
REMARK 500 SER A 193 -94.74 -89.70
REMARK 500 SER A 201 -120.88 63.66
REMARK 500 CYS A 230 59.24 26.33
REMARK 500 PHE A 254 -60.74 67.90
REMARK 500 LEU A 302 40.96 -102.77
REMARK 500 ALA A 334 16.61 59.81
REMARK 500 SER A 338 -35.29 -138.80
REMARK 500 GLN B 78 43.84 -79.10
REMARK 500 LEU B 131 156.03 80.06
REMARK 500 SER B 193 -96.62 -88.91
REMARK 500 SER B 201 -121.28 64.16
REMARK 500 CYS B 230 58.81 25.82
REMARK 500 PHE B 254 -61.05 72.50
REMARK 500 SER B 338 -34.61 -137.99
REMARK 500 LEU C 131 156.25 80.57
REMARK 500 SER C 193 -97.03 -89.69
REMARK 500 SER C 201 -119.71 63.16
REMARK 500 CYS C 230 59.07 26.30
REMARK 500 PHE C 254 -55.29 71.80
REMARK 500 LEU C 302 40.54 -102.65
REMARK 500 ALA C 334 16.55 59.75
REMARK 500 SER C 338 -33.27 -138.90
REMARK 500 GLN D 78 49.19 -76.87
REMARK 500 LEU D 131 155.91 80.67
REMARK 500 SER D 193 -95.65 -90.27
REMARK 500 SER D 201 -118.67 63.71
REMARK 500 CYS D 230 59.48 26.55
REMARK 500 PHE D 254 -57.01 72.81
REMARK 500 LEU D 302 42.07 -103.50
REMARK 500 ALA D 334 17.26 59.81
REMARK 500 SER D 338 -34.84 -138.67
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 C 739 DISTANCE = 6.34 ANGSTROMS
DBREF 4J7A A 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
DBREF 4J7A B 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
DBREF 4J7A C 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
DBREF 4J7A D 1 362 UNP Q4TZQ3 Q4TZQ3_9BACT 1 362
SEQADV 4J7A MET A -11 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A ARG A -10 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY A -9 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER A -8 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS A -7 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS A -6 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS A -5 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS A -4 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS A -3 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS A -2 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY A -1 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER A 0 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A MET B -11 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A ARG B -10 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY B -9 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER B -8 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS B -7 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS B -6 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS B -5 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS B -4 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS B -3 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS B -2 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY B -1 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER B 0 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A MET C -11 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A ARG C -10 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY C -9 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER C -8 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS C -7 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS C -6 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS C -5 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS C -4 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS C -3 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS C -2 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY C -1 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER C 0 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A MET D -11 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A ARG D -10 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY D -9 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER D -8 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS D -7 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS D -6 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS D -5 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS D -4 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS D -3 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A HIS D -2 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A GLY D -1 UNP Q4TZQ3 EXPRESSION TAG
SEQADV 4J7A SER D 0 UNP Q4TZQ3 EXPRESSION TAG
SEQRES 1 A 374 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 A 374 SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU GLY
SEQRES 3 A 374 ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR ASP
SEQRES 4 A 374 PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU ALA
SEQRES 5 A 374 ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER GLU
SEQRES 6 A 374 VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU GLN
SEQRES 7 A 374 ALA TRP GLN THR LEU PHE ALA MET LEU GLY SER GLN GLY
SEQRES 8 A 374 GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR ILE
SEQRES 9 A 374 LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE HIS
SEQRES 10 A 374 SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU PRO
SEQRES 11 A 374 CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE LEU
SEQRES 12 A 374 THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER GLU
SEQRES 13 A 374 LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU PHE
SEQRES 14 A 374 ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE PRO
SEQRES 15 A 374 ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP VAL
SEQRES 16 A 374 ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU ILE
SEQRES 17 A 374 MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU ALA
SEQRES 18 A 374 THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU GLU
SEQRES 19 A 374 ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER GLY
SEQRES 20 A 374 LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU LEU
SEQRES 21 A 374 GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET GLY
SEQRES 22 A 374 ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN ALA
SEQRES 23 A 374 SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU GLU
SEQRES 24 A 374 ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL ASN
SEQRES 25 A 374 GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS TYR
SEQRES 26 A 374 ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY ARG
SEQRES 27 A 374 THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER PHE
SEQRES 28 A 374 VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL ARG
SEQRES 29 A 374 ASP ILE SER ALA PHE ALA TYR SER ARG ALA
SEQRES 1 B 374 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 B 374 SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU GLY
SEQRES 3 B 374 ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR ASP
SEQRES 4 B 374 PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU ALA
SEQRES 5 B 374 ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER GLU
SEQRES 6 B 374 VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU GLN
SEQRES 7 B 374 ALA TRP GLN THR LEU PHE ALA MET LEU GLY SER GLN GLY
SEQRES 8 B 374 GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR ILE
SEQRES 9 B 374 LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE HIS
SEQRES 10 B 374 SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU PRO
SEQRES 11 B 374 CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE LEU
SEQRES 12 B 374 THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER GLU
SEQRES 13 B 374 LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU PHE
SEQRES 14 B 374 ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE PRO
SEQRES 15 B 374 ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP VAL
SEQRES 16 B 374 ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU ILE
SEQRES 17 B 374 MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU ALA
SEQRES 18 B 374 THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU GLU
SEQRES 19 B 374 ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER GLY
SEQRES 20 B 374 LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU LEU
SEQRES 21 B 374 GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET GLY
SEQRES 22 B 374 ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN ALA
SEQRES 23 B 374 SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU GLU
SEQRES 24 B 374 ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL ASN
SEQRES 25 B 374 GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS TYR
SEQRES 26 B 374 ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY ARG
SEQRES 27 B 374 THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER PHE
SEQRES 28 B 374 VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL ARG
SEQRES 29 B 374 ASP ILE SER ALA PHE ALA TYR SER ARG ALA
SEQRES 1 C 374 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 C 374 SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU GLY
SEQRES 3 C 374 ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR ASP
SEQRES 4 C 374 PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU ALA
SEQRES 5 C 374 ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER GLU
SEQRES 6 C 374 VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU GLN
SEQRES 7 C 374 ALA TRP GLN THR LEU PHE ALA MET LEU GLY SER GLN GLY
SEQRES 8 C 374 GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR ILE
SEQRES 9 C 374 LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE HIS
SEQRES 10 C 374 SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU PRO
SEQRES 11 C 374 CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE LEU
SEQRES 12 C 374 THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER GLU
SEQRES 13 C 374 LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU PHE
SEQRES 14 C 374 ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE PRO
SEQRES 15 C 374 ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP VAL
SEQRES 16 C 374 ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU ILE
SEQRES 17 C 374 MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU ALA
SEQRES 18 C 374 THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU GLU
SEQRES 19 C 374 ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER GLY
SEQRES 20 C 374 LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU LEU
SEQRES 21 C 374 GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET GLY
SEQRES 22 C 374 ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN ALA
SEQRES 23 C 374 SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU GLU
SEQRES 24 C 374 ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL ASN
SEQRES 25 C 374 GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS TYR
SEQRES 26 C 374 ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY ARG
SEQRES 27 C 374 THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER PHE
SEQRES 28 C 374 VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL ARG
SEQRES 29 C 374 ASP ILE SER ALA PHE ALA TYR SER ARG ALA
SEQRES 1 D 374 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 D 374 SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU GLY
SEQRES 3 D 374 ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR ASP
SEQRES 4 D 374 PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU ALA
SEQRES 5 D 374 ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER GLU
SEQRES 6 D 374 VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU GLN
SEQRES 7 D 374 ALA TRP GLN THR LEU PHE ALA MET LEU GLY SER GLN GLY
SEQRES 8 D 374 GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR ILE
SEQRES 9 D 374 LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE HIS
SEQRES 10 D 374 SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU PRO
SEQRES 11 D 374 CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE LEU
SEQRES 12 D 374 THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER GLU
SEQRES 13 D 374 LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU PHE
SEQRES 14 D 374 ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE PRO
SEQRES 15 D 374 ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP VAL
SEQRES 16 D 374 ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU ILE
SEQRES 17 D 374 MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU ALA
SEQRES 18 D 374 THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU GLU
SEQRES 19 D 374 ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER GLY
SEQRES 20 D 374 LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU LEU
SEQRES 21 D 374 GLU ASN ASP ALA TYR PHE LEU ASP MET LYS THR MET GLY
SEQRES 22 D 374 ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN ALA
SEQRES 23 D 374 SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU GLU
SEQRES 24 D 374 ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL ASN
SEQRES 25 D 374 GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS TYR
SEQRES 26 D 374 ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY ARG
SEQRES 27 D 374 THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER PHE
SEQRES 28 D 374 VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL ARG
SEQRES 29 D 374 ASP ILE SER ALA PHE ALA TYR SER ARG ALA
FORMUL 5 HOH *2111(H2 O)
HELIX 1 1 PRO A 10 ASP A 15 1 6
HELIX 2 2 ASP A 27 LEU A 37 1 11
HELIX 3 3 GLU A 53 SER A 77 1 25
HELIX 4 4 ASP A 135 THR A 148 1 14
HELIX 5 5 ALA A 161 GLY A 165 5 5
HELIX 6 6 PRO A 170 SER A 185 1 16
HELIX 7 7 ASN A 186 GLY A 191 1 6
HELIX 8 8 SER A 201 GLU A 217 1 17
HELIX 9 9 TRP A 219 ILE A 223 5 5
HELIX 10 10 PRO A 245 ASN A 250 1 6
HELIX 11 11 ASP A 256 ASP A 268 1 13
HELIX 12 12 TRP A 280 ALA A 284 5 5
HELIX 13 13 SER A 285 ALA A 290 1 6
HELIX 14 14 LEU A 305 ALA A 319 1 15
HELIX 15 15 ALA A 334 SER A 338 5 5
HELIX 16 16 ILE A 343 ALA A 362 1 20
HELIX 17 17 PRO B 10 ASP B 15 1 6
HELIX 18 18 ASP B 27 LEU B 37 1 11
HELIX 19 19 GLU B 53 SER B 77 1 25
HELIX 20 20 ASP B 135 THR B 148 1 14
HELIX 21 21 ALA B 161 GLY B 165 5 5
HELIX 22 22 PRO B 170 SER B 185 1 16
HELIX 23 23 ASN B 186 GLY B 191 1 6
HELIX 24 24 SER B 201 GLY B 218 1 18
HELIX 25 25 TRP B 219 ILE B 223 5 5
HELIX 26 26 PRO B 245 ASN B 250 1 6
HELIX 27 27 ASP B 256 ASP B 268 1 13
HELIX 28 28 TRP B 280 ALA B 284 5 5
HELIX 29 29 SER B 285 ALA B 290 1 6
HELIX 30 30 LEU B 305 ALA B 319 1 15
HELIX 31 31 ALA B 334 SER B 338 5 5
HELIX 32 32 ILE B 343 ALA B 362 1 20
HELIX 33 33 PRO C 10 ASP C 15 1 6
HELIX 34 34 ASP C 27 GLY C 38 1 12
HELIX 35 35 GLU C 53 SER C 77 1 25
HELIX 36 36 ASP C 135 THR C 148 1 14
HELIX 37 37 ALA C 161 GLY C 165 5 5
HELIX 38 38 PRO C 170 SER C 185 1 16
HELIX 39 39 ASN C 186 GLY C 191 1 6
HELIX 40 40 SER C 201 GLY C 218 1 18
HELIX 41 41 TRP C 219 ILE C 223 5 5
HELIX 42 42 PRO C 245 ASN C 250 1 6
HELIX 43 43 ASP C 256 ASP C 268 1 13
HELIX 44 44 TRP C 280 ALA C 284 5 5
HELIX 45 45 SER C 285 ALA C 290 1 6
HELIX 46 46 LEU C 305 ALA C 319 1 15
HELIX 47 47 ALA C 334 SER C 338 5 5
HELIX 48 48 ILE C 343 ALA C 362 1 20
HELIX 49 49 PRO D 10 ASP D 15 1 6
HELIX 50 50 ASP D 27 GLY D 38 1 12
HELIX 51 51 GLU D 53 SER D 77 1 25
HELIX 52 52 ASP D 135 THR D 148 1 14
HELIX 53 53 ALA D 161 GLY D 165 5 5
HELIX 54 54 PRO D 170 SER D 185 1 16
HELIX 55 55 ASN D 186 GLY D 191 1 6
HELIX 56 56 SER D 201 GLY D 218 1 18
HELIX 57 57 TRP D 219 ILE D 223 5 5
HELIX 58 58 PRO D 245 ASN D 250 1 6
HELIX 59 59 ASP D 256 ASP D 268 1 13
HELIX 60 60 TRP D 280 ALA D 284 5 5
HELIX 61 61 SER D 285 ALA D 290 1 6
HELIX 62 62 LEU D 305 ALA D 319 1 15
HELIX 63 63 ALA D 334 SER D 338 5 5
HELIX 64 64 ILE D 343 ALA D 362 1 20
SHEET 1 A16 VAL A 85 LYS A 93 0
SHEET 2 A16 GLU A 99 PRO A 107 -1 O ILE A 104 N ARG A 88
SHEET 3 A16 VAL A 151 GLU A 156 -1 O GLY A 154 N TYR A 103
SHEET 4 A16 LEU A 117 THR A 123 1 N VAL A 120 O VAL A 153
SHEET 5 A16 ILE A 192 GLU A 200 1 O ILE A 196 N VAL A 121
SHEET 6 A16 GLY A 225 GLN A 229 1 O TYR A 227 N MET A 197
SHEET 7 A16 HIS A 295 ASN A 300 1 O VAL A 296 N ALA A 228
SHEET 8 A16 THR A 323 VAL A 328 1 O VAL A 328 N VAL A 299
SHEET 9 A16 THR D 323 VAL D 328 -1 O THR D 327 N THR A 327
SHEET 10 A16 HIS D 295 ASN D 300 1 N VAL D 299 O VAL D 328
SHEET 11 A16 GLY D 225 GLN D 229 1 N ALA D 228 O VAL D 296
SHEET 12 A16 ILE D 192 GLU D 200 1 N GLY D 199 O GLN D 229
SHEET 13 A16 LEU D 117 HIS D 122 1 N VAL D 121 O ILE D 196
SHEET 14 A16 VAL D 151 GLU D 156 1 O VAL D 153 N VAL D 120
SHEET 15 A16 GLU D 99 PRO D 107 -1 N TYR D 103 O GLY D 154
SHEET 16 A16 VAL D 85 LYS D 93 -1 N ARG D 88 O ILE D 104
SHEET 1 B16 VAL B 85 LYS B 93 0
SHEET 2 B16 GLU B 99 PRO B 107 -1 O ILE B 104 N ARG B 88
SHEET 3 B16 VAL B 151 GLU B 156 -1 O GLY B 154 N TYR B 103
SHEET 4 B16 LEU B 117 HIS B 122 1 N VAL B 120 O VAL B 153
SHEET 5 B16 ILE B 192 GLU B 200 1 O ILE B 196 N VAL B 121
SHEET 6 B16 GLY B 225 GLN B 229 1 O GLN B 229 N GLY B 199
SHEET 7 B16 HIS B 295 ASN B 300 1 O VAL B 296 N ALA B 228
SHEET 8 B16 THR B 323 VAL B 328 1 O VAL B 328 N VAL B 299
SHEET 9 B16 THR C 323 VAL C 328 -1 O THR C 327 N THR B 327
SHEET 10 B16 HIS C 295 ASN C 300 1 N VAL C 299 O VAL C 328
SHEET 11 B16 GLY C 225 GLN C 229 1 N ALA C 228 O VAL C 296
SHEET 12 B16 ILE C 192 GLU C 200 1 N MET C 197 O TYR C 227
SHEET 13 B16 LEU C 117 HIS C 122 1 N VAL C 121 O ILE C 196
SHEET 14 B16 VAL C 151 GLU C 156 1 O VAL C 153 N VAL C 120
SHEET 15 B16 GLU C 99 PRO C 107 -1 N TYR C 103 O GLY C 154
SHEET 16 B16 VAL C 85 LYS C 93 -1 N ASP C 86 O SER C 106
CISPEP 1 GLY A 165 ASN A 166 0 -1.58
CISPEP 2 PHE A 169 PRO A 170 0 7.05
CISPEP 3 GLY B 165 ASN B 166 0 -0.64
CISPEP 4 PHE B 169 PRO B 170 0 7.91
CISPEP 5 GLY C 165 ASN C 166 0 -1.16
CISPEP 6 PHE C 169 PRO C 170 0 7.40
CISPEP 7 GLY D 165 ASN D 166 0 -1.22
CISPEP 8 PHE D 169 PRO D 170 0 7.38
CRYST1 197.758 95.213 99.418 90.00 97.05 90.00 C 1 2 1 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 0.005057 0.000000 0.000625 0.00000
SCALE2 0.000000 0.010503 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010135 0.00000
TER 2641 ALA A 362
TER 5282 ALA B 362
TER 7923 ALA C 362
TER 10564 ALA D 362
MASTER 445 0 0 64 32 0 0 612671 4 0 116
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