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HEADER HYDROLASE 04-JAN-16 5HC2
TITLE STRUCTURE OF ESTERASE EST22 MUTANT-S188A WITH P-NITROPHENOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOLYTIC ENZYME;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, EST22, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LI,J.HUANG
REVDAT 1 18-JAN-17 5HC2 0
JRNL AUTH J.HUANG,Y.Y.HUO,R.JI,S.KUANG,C.JI,X.W.XU,J.LI
JRNL TITL STRUCTURAL INSIGHTS OF A HORMONE SENSITIVE LIPASE HOMOLOGUE
JRNL TITL 2 EST22.
JRNL REF SCI REP V. 6 28550 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27328716
JRNL DOI 10.1038/SREP28550
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2155
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 103555
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 5141
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 46.3447 - 6.1656 0.98 3474 196 0.1523 0.1484
REMARK 3 2 6.1656 - 4.8955 1.00 3386 186 0.1481 0.1579
REMARK 3 3 4.8955 - 4.2772 1.00 3371 157 0.1243 0.1350
REMARK 3 4 4.2772 - 3.8863 1.00 3326 177 0.1222 0.1491
REMARK 3 5 3.8863 - 3.6079 1.00 3352 185 0.1384 0.1613
REMARK 3 6 3.6079 - 3.3953 1.00 3309 160 0.1484 0.1789
REMARK 3 7 3.3953 - 3.2253 1.00 3304 178 0.1561 0.1937
REMARK 3 8 3.2253 - 3.0849 1.00 3330 158 0.1633 0.2110
REMARK 3 9 3.0849 - 2.9662 1.00 3301 175 0.1601 0.1963
REMARK 3 10 2.9662 - 2.8638 1.00 3274 191 0.1660 0.2052
REMARK 3 11 2.8638 - 2.7743 1.00 3274 180 0.1667 0.1997
REMARK 3 12 2.7743 - 2.6950 1.00 3288 177 0.1664 0.2053
REMARK 3 13 2.6950 - 2.6241 1.00 3256 180 0.1634 0.2070
REMARK 3 14 2.6241 - 2.5600 1.00 3273 171 0.1655 0.2285
REMARK 3 15 2.5600 - 2.5018 1.00 3290 165 0.1650 0.2023
REMARK 3 16 2.5018 - 2.4486 1.00 3267 173 0.1674 0.2233
REMARK 3 17 2.4486 - 2.3996 1.00 3261 181 0.1567 0.1935
REMARK 3 18 2.3996 - 2.3543 1.00 3305 163 0.1601 0.1901
REMARK 3 19 2.3543 - 2.3123 1.00 3258 154 0.1549 0.2240
REMARK 3 20 2.3123 - 2.2731 1.00 3302 156 0.1567 0.2044
REMARK 3 21 2.2731 - 2.2364 1.00 3263 176 0.1608 0.1986
REMARK 3 22 2.2364 - 2.2020 1.00 3245 160 0.1617 0.1996
REMARK 3 23 2.2020 - 2.1697 1.00 3273 177 0.1611 0.2230
REMARK 3 24 2.1697 - 2.1391 1.00 3268 156 0.1541 0.1880
REMARK 3 25 2.1391 - 2.1102 1.00 3258 167 0.1605 0.2037
REMARK 3 26 2.1102 - 2.0828 1.00 3264 182 0.1673 0.2203
REMARK 3 27 2.0828 - 2.0567 1.00 3248 177 0.1759 0.2305
REMARK 3 28 2.0567 - 2.0320 1.00 3276 151 0.1780 0.2281
REMARK 3 29 2.0320 - 2.0083 1.00 3253 164 0.1848 0.2363
REMARK 3 30 2.0083 - 1.9858 0.89 2865 168 0.1819 0.2366
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.190
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 10756
REMARK 3 ANGLE : 0.812 14657
REMARK 3 CHIRALITY : 0.052 1589
REMARK 3 PLANARITY : 0.005 1981
REMARK 3 DIHEDRAL : 14.029 6463
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 5HC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103730
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SODIUM CITRATE, 0.1M IMIDAZOLE, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 40.82300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.13350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.96700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.13350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.82300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.96700
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: 3790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 3500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
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 ASN B 3 CG OD1 ND2
REMARK 470 THR C 2 OG1 CG2
REMARK 470 THR D 2 OG1 CG2
REMARK 470 ASP D 23 CG OD1 OD2
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 D 718 O HOH D 754 1.80
REMARK 500 O HOH B 650 O HOH B 685 1.82
REMARK 500 O HOH D 704 O HOH D 748 1.86
REMARK 500 O HOH C 696 O HOH C 737 1.92
REMARK 500 OE1 GLU A 270 O HOH A 501 1.92
REMARK 500 O HOH C 683 O HOH C 729 1.93
REMARK 500 OE1 GLU B 234 O HOH B 501 1.93
REMARK 500 OE1 GLU B 34 O HOH B 502 1.93
REMARK 500 O HOH C 590 O HOH C 722 1.96
REMARK 500 O HOH A 697 O HOH A 707 1.97
REMARK 500 O HOH B 718 O HOH C 727 1.97
REMARK 500 O HOH C 579 O HOH D 675 2.02
REMARK 500 O HOH B 627 O HOH B 758 2.03
REMARK 500 O HOH C 622 O HOH C 712 2.03
REMARK 500 O HOH B 673 O HOH B 738 2.07
REMARK 500 O HOH A 694 O HOH B 566 2.09
REMARK 500 O HOH C 690 O HOH C 707 2.09
REMARK 500 O HOH C 615 O HOH C 727 2.10
REMARK 500 O HOH B 609 O HOH B 703 2.10
REMARK 500 O HOH A 607 O HOH A 720 2.10
REMARK 500 O HOH D 665 O HOH D 720 2.12
REMARK 500 O HOH C 532 O HOH C 711 2.14
REMARK 500 OG1 THR D 96 O HOH D 501 2.15
REMARK 500 OE2 GLU D 62 O HOH D 502 2.15
REMARK 500 O HOH C 702 O HOH C 735 2.15
REMARK 500 NH2 ARG D 121 O HOH D 503 2.18
REMARK 500 O HOH D 502 O HOH D 503 2.19
REMARK 500 OE1 GLU D 227 O HOH D 504 2.19
REMARK 500 O HOH D 552 O HOH D 713 2.19
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 LEU A 113 176.62 76.47
REMARK 500 LEU A 143 -56.76 -137.53
REMARK 500 SER A 146 -148.97 -94.35
REMARK 500 ALA A 188 -124.33 60.78
REMARK 500 CYS A 217 58.18 22.16
REMARK 500 LEU A 239 -59.00 69.68
REMARK 500 PHE A 322 72.35 -114.20
REMARK 500 LEU B 24 -86.92 -73.29
REMARK 500 LEU B 113 176.70 75.66
REMARK 500 LEU B 143 -50.40 -129.80
REMARK 500 SER B 146 -150.71 -88.92
REMARK 500 ALA B 188 -126.10 64.03
REMARK 500 CYS B 217 61.13 20.25
REMARK 500 LEU B 239 -60.63 70.53
REMARK 500 PHE B 322 68.85 -115.71
REMARK 500 ASP C 23 15.88 138.39
REMARK 500 LEU C 24 -82.11 -63.03
REMARK 500 LEU C 113 175.12 81.50
REMARK 500 LEU C 143 -57.65 -131.86
REMARK 500 SER C 146 -147.76 -89.83
REMARK 500 ALA C 188 -126.59 61.99
REMARK 500 CYS C 217 61.23 22.26
REMARK 500 LEU C 239 -59.40 66.94
REMARK 500 PHE C 322 66.05 -119.72
REMARK 500 LEU D 113 176.46 76.93
REMARK 500 LEU D 143 -59.07 -134.28
REMARK 500 SER D 146 -147.50 -85.53
REMARK 500 ALA D 188 -122.63 60.69
REMARK 500 CYS D 217 60.96 21.74
REMARK 500 LEU D 239 -62.43 66.97
REMARK 500 SER D 306 108.06 -57.73
REMARK 500 PHE D 322 69.55 -116.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD D 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HC0 RELATED DB: PDB
REMARK 900 RELATED ID: 5HC3 RELATED DB: PDB
REMARK 900 RELATED ID: 5HC4 RELATED DB: PDB
REMARK 900 RELATED ID: 5HC5 RELATED DB: PDB
DBREF 5HC2 A 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC2 B 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC2 C 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC2 D 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
SEQADV 5HC2 MET A -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY A -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER A -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER A -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER A -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER A -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY A -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 LEU A -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 VAL A -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 PRO A -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ARG A -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY A -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER A -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS A 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ALA A 188 UNP H6BDX1 SER 188 ENGINEERED MUTATION
SEQADV 5HC2 MET B -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY B -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER B -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER B -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER B -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER B -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY B -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 LEU B -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 VAL B -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 PRO B -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ARG B -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY B -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER B -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS B 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ALA B 188 UNP H6BDX1 SER 188 ENGINEERED MUTATION
SEQADV 5HC2 MET C -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY C -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER C -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER C -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER C -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER C -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY C -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 LEU C -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 VAL C -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 PRO C -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ARG C -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY C -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER C -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS C 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ALA C 188 UNP H6BDX1 SER 188 ENGINEERED MUTATION
SEQADV 5HC2 MET D -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY D -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER D -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER D -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER D -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER D -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY D -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 LEU D -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 VAL D -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 PRO D -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ARG D -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 GLY D -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 SER D -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 HIS D 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC2 ALA D 188 UNP H6BDX1 SER 188 ENGINEERED MUTATION
SEQRES 1 A 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 A 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 A 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 A 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 A 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 A 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 A 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 A 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 A 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 A 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 A 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 A 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 A 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 A 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 A 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 A 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 A 365 ALA GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 A 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 A 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 A 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 A 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 A 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 A 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 A 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 A 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 A 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 A 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 A 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 A 365 GLY
SEQRES 1 B 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 B 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 B 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 B 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 B 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 B 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 B 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 B 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 B 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 B 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 B 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 B 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 B 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 B 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 B 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 B 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 B 365 ALA GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 B 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 B 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 B 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 B 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 B 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 B 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 B 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 B 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 B 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 B 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 B 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 B 365 GLY
SEQRES 1 C 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 C 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 C 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 C 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 C 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 C 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 C 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 C 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 C 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 C 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 C 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 C 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 C 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 C 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 C 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 C 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 C 365 ALA GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 C 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 C 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 C 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 C 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 C 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 C 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 C 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 C 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 C 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 C 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 C 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 C 365 GLY
SEQRES 1 D 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 D 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 D 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 D 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 D 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 D 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 D 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 D 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 D 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 D 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 D 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 D 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 D 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 D 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 D 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 D 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 D 365 ALA GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 D 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 D 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 D 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 D 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 D 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 D 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 D 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 D 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 D 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 D 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 D 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 D 365 GLY
HET NPO A 401 15
HET IMD A 402 10
HET IMD A 403 10
HET NPO B 401 15
HET IMD B 402 10
HET NPO C 401 15
HET IMD C 402 10
HET NPO D 401 15
HET IMD D 402 10
HETNAM NPO P-NITROPHENOL
HETNAM IMD IMIDAZOLE
FORMUL 5 NPO 4(C6 H5 N O3)
FORMUL 6 IMD 5(C3 H5 N2 1+)
FORMUL 14 HOH *1020(H2 O)
HELIX 1 AA1 ASP A 12 ALA A 17 1 6
HELIX 2 AA2 SER A 32 SER A 41 1 10
HELIX 3 AA3 SER A 42 CYS A 59 1 18
HELIX 4 AA4 TYR A 117 SER A 129 1 13
HELIX 5 AA5 PRO A 155 HIS A 171 1 17
HELIX 6 AA6 HIS A 171 GLY A 176 1 6
HELIX 7 AA7 ALA A 188 GLU A 204 1 17
HELIX 8 AA8 SER A 206 ILE A 210 5 5
HELIX 9 AA9 PRO A 230 ASN A 235 1 6
HELIX 10 AB1 ASN A 245 MET A 258 1 14
HELIX 11 AB2 TRP A 264 ALA A 268 5 5
HELIX 12 AB3 THR A 269 SER A 274 1 6
HELIX 13 AB4 LEU A 289 GLY A 304 1 16
HELIX 14 AB5 GLY A 318 PHE A 322 5 5
HELIX 15 AB6 CYS A 326 GLY A 343 1 18
HELIX 16 AB7 LYS B 4 ASP B 8 1 5
HELIX 17 AB8 ASP B 12 SER B 20 1 9
HELIX 18 AB9 SER B 32 SER B 41 1 10
HELIX 19 AC1 SER B 42 ALA B 58 1 17
HELIX 20 AC2 TYR B 117 SER B 129 1 13
HELIX 21 AC3 PRO B 155 HIS B 171 1 17
HELIX 22 AC4 HIS B 171 GLY B 176 1 6
HELIX 23 AC5 ALA B 188 GLU B 204 1 17
HELIX 24 AC6 SER B 206 ILE B 210 5 5
HELIX 25 AC7 PRO B 230 ASN B 235 1 6
HELIX 26 AC8 ASN B 245 MET B 258 1 14
HELIX 27 AC9 TRP B 264 ALA B 268 5 5
HELIX 28 AD1 THR B 269 SER B 274 1 6
HELIX 29 AD2 LEU B 289 ALA B 303 1 15
HELIX 30 AD3 GLY B 318 PHE B 322 5 5
HELIX 31 AD4 CYS B 326 GLY B 343 1 18
HELIX 32 AD5 ASN C 3 ASP C 8 1 6
HELIX 33 AD6 ASP C 12 SER C 20 1 9
HELIX 34 AD7 SER C 32 SER C 41 1 10
HELIX 35 AD8 SER C 42 ALA C 58 1 17
HELIX 36 AD9 TYR C 117 SER C 129 1 13
HELIX 37 AE1 PRO C 155 HIS C 171 1 17
HELIX 38 AE2 HIS C 171 GLY C 176 1 6
HELIX 39 AE3 ALA C 188 GLU C 204 1 17
HELIX 40 AE4 SER C 206 ILE C 210 5 5
HELIX 41 AE5 SER C 229 ASN C 235 1 7
HELIX 42 AE6 ASN C 245 MET C 258 1 14
HELIX 43 AE7 TRP C 264 ALA C 268 5 5
HELIX 44 AE8 THR C 269 SER C 274 1 6
HELIX 45 AE9 LEU C 289 ALA C 303 1 15
HELIX 46 AF1 GLY C 318 PHE C 322 5 5
HELIX 47 AF2 CYS C 326 GLY C 343 1 18
HELIX 48 AF3 ASN D 3 ASP D 8 1 6
HELIX 49 AF4 ASP D 12 SER D 20 1 9
HELIX 50 AF5 SER D 32 SER D 41 1 10
HELIX 51 AF6 SER D 42 CYS D 59 1 18
HELIX 52 AF7 TYR D 117 SER D 129 1 13
HELIX 53 AF8 PRO D 155 HIS D 171 1 17
HELIX 54 AF9 HIS D 171 GLY D 176 1 6
HELIX 55 AG1 ALA D 188 GLU D 204 1 17
HELIX 56 AG2 SER D 206 ILE D 210 5 5
HELIX 57 AG3 PRO D 230 ASN D 235 1 6
HELIX 58 AG4 ASN D 245 MET D 258 1 14
HELIX 59 AG5 TRP D 264 ALA D 268 5 5
HELIX 60 AG6 THR D 269 SER D 274 1 6
HELIX 61 AG7 LEU D 289 GLY D 304 1 16
HELIX 62 AG8 GLY D 318 PHE D 322 5 5
HELIX 63 AG9 CYS D 326 GLY D 343 1 18
SHEET 1 AA116 LEU A 70 THR A 78 0
SHEET 2 AA116 ILE A 85 PRO A 93 -1 O TYR A 90 N GLU A 73
SHEET 3 AA116 ALA A 133 GLU A 138 -1 O GLU A 138 N LYS A 87
SHEET 4 AA116 LEU A 99 ILE A 105 1 N VAL A 102 O ALA A 133
SHEET 5 AA116 ILE A 177 GLU A 187 1 O ILE A 183 N TYR A 103
SHEET 6 AA116 GLY A 212 LEU A 216 1 O LEU A 216 N GLY A 186
SHEET 7 AA116 THR A 279 ASN A 284 1 O PHE A 280 N LEU A 213
SHEET 8 AA116 ALA A 307 VAL A 312 1 O VAL A 312 N VAL A 283
SHEET 9 AA116 ALA B 307 VAL B 312 -1 O GLN B 311 N GLN A 311
SHEET 10 AA116 THR B 279 ASN B 284 1 N VAL B 283 O VAL B 312
SHEET 11 AA116 GLY B 212 LEU B 216 1 N ALA B 215 O PHE B 280
SHEET 12 AA116 ILE B 177 GLU B 187 1 N GLY B 186 O LEU B 216
SHEET 13 AA116 LEU B 99 ILE B 105 1 N TYR B 103 O ILE B 183
SHEET 14 AA116 ALA B 133 GLU B 138 1 O ALA B 133 N VAL B 102
SHEET 15 AA116 ILE B 85 PRO B 93 -1 N ILE B 91 O VAL B 134
SHEET 16 AA116 LEU B 70 THR B 78 -1 N GLU B 73 O TYR B 90
SHEET 1 AA216 LEU C 70 THR C 78 0
SHEET 2 AA216 ILE C 85 PRO C 93 -1 O TYR C 90 N GLU C 73
SHEET 3 AA216 ALA C 133 GLU C 138 -1 O MET C 136 N GLN C 89
SHEET 4 AA216 LEU C 99 ILE C 105 1 N VAL C 102 O ALA C 133
SHEET 5 AA216 ILE C 177 GLU C 187 1 O ILE C 183 N TYR C 103
SHEET 6 AA216 GLY C 212 LEU C 216 1 O LEU C 216 N GLY C 186
SHEET 7 AA216 THR C 279 ASN C 284 1 O PHE C 280 N LEU C 213
SHEET 8 AA216 ALA C 307 VAL C 312 1 O VAL C 312 N VAL C 283
SHEET 9 AA216 ALA D 307 VAL D 312 -1 O GLN D 311 N GLN C 311
SHEET 10 AA216 THR D 279 ASN D 284 1 N VAL D 283 O VAL D 312
SHEET 11 AA216 GLY D 212 LEU D 216 1 N LEU D 213 O PHE D 280
SHEET 12 AA216 ILE D 177 GLU D 187 1 N GLY D 186 O LEU D 216
SHEET 13 AA216 LEU D 99 ILE D 105 1 N TYR D 103 O ILE D 183
SHEET 14 AA216 ALA D 133 GLU D 138 1 O ALA D 133 N VAL D 102
SHEET 15 AA216 ILE D 85 PRO D 93 -1 N LYS D 87 O GLU D 138
SHEET 16 AA216 LEU D 70 THR D 78 -1 N GLU D 73 O TYR D 90
SHEET 1 AA3 2 ASP D 23 LEU D 24 0
SHEET 2 AA3 2 LEU D 239 LEU D 240 1 O LEU D 239 N LEU D 24
CISPEP 1 GLY A 25 GLY A 26 0 0.92
CISPEP 2 GLU A 80 PRO A 81 0 6.21
CISPEP 3 TYR A 154 PRO A 155 0 2.65
CISPEP 4 TRP A 224 PRO A 225 0 0.94
CISPEP 5 GLU B 80 PRO B 81 0 7.75
CISPEP 6 TYR B 154 PRO B 155 0 5.84
CISPEP 7 TRP B 224 PRO B 225 0 -2.44
CISPEP 8 MET C 22 ASP C 23 0 -5.81
CISPEP 9 LEU C 24 GLY C 25 0 6.33
CISPEP 10 GLU C 80 PRO C 81 0 8.11
CISPEP 11 TYR C 154 PRO C 155 0 5.02
CISPEP 12 TRP C 224 PRO C 225 0 -3.22
CISPEP 13 GLY D 25 GLY D 26 0 10.85
CISPEP 14 GLU D 80 PRO D 81 0 6.93
CISPEP 15 TYR D 154 PRO D 155 0 4.62
CISPEP 16 TRP D 224 PRO D 225 0 -1.41
SITE 1 AC1 10 LEU A 24 GLY A 107 GLY A 108 GLY A 109
SITE 2 AC1 10 ALA A 188 GLY A 189 TYR A 219 LEU A 240
SITE 3 AC1 10 LEU A 242 IMD A 402
SITE 1 AC2 7 LEU A 113 TYR A 120 GLU A 187 ALA A 188
SITE 2 AC2 7 HIS A 317 NPO A 401 IMD A 403
SITE 1 AC3 3 MET A 22 LEU A 24 IMD A 402
SITE 1 AC4 9 GLY B 25 GLY B 108 GLY B 109 ALA B 188
SITE 2 AC4 9 GLY B 189 TYR B 219 LEU B 240 LEU B 242
SITE 3 AC4 9 IMD B 402
SITE 1 AC5 7 LEU B 24 LEU B 113 TYR B 120 ALA B 188
SITE 2 AC5 7 HIS B 317 ILE B 321 NPO B 401
SITE 1 AC6 9 GLY C 25 GLY C 108 GLY C 109 ALA C 188
SITE 2 AC6 9 GLY C 189 TYR C 219 LEU C 240 LEU C 242
SITE 3 AC6 9 IMD C 402
SITE 1 AC7 8 LEU C 113 TYR C 120 GLU C 187 ALA C 188
SITE 2 AC7 8 HIS C 317 ILE C 321 NPO C 401 HOH C 644
SITE 1 AC8 9 LEU D 24 GLY D 108 GLY D 109 ALA D 188
SITE 2 AC8 9 GLY D 189 TYR D 219 LEU D 240 LEU D 242
SITE 3 AC8 9 IMD D 402
SITE 1 AC9 5 LEU D 113 TYR D 120 ALA D 188 HIS D 317
SITE 2 AC9 5 NPO D 401
CRYST1 81.646 121.934 150.267 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012248 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008201 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006655 0.00000
TER 2616 GLY A 344
TER 5221 GLY B 344
TER 7835 GLY C 344
TER 10446 GLY D 344
MASTER 469 0 9 63 34 0 21 611339 4 110 116
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