| content |
HEADER HYDROLASE 16-JAN-20 6XTC
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE VARIANT DHAA177 DOMAIN-
TITLE 2 SWAPPED DIMER TYPE-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE VARIANT DHAA177 DOMAIN-SWAPPED
COMPND 3 DIMER TYPE-3;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MARKOVA,J.DAMBORSKY,M.MAREK
REVDAT 1 27-JAN-21 6XTC 0
JRNL AUTH K.MARKOVA,J.DAMBORSKY,M.MAREK
JRNL TITL STRUCTURES OF HALOALKANE DEHALOGENASE VARIANT DHAA115 AND
JRNL TITL 2 DHAA177
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 65918
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180
REMARK 3 FREE R VALUE TEST SET COUNT : 3413
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 45.5240 - 7.3243 1.00 2837 158 0.1968 0.2202
REMARK 3 2 7.3243 - 5.8174 1.00 2722 146 0.2201 0.3106
REMARK 3 3 5.8174 - 5.0831 1.00 2725 100 0.1837 0.2442
REMARK 3 4 5.0831 - 4.6189 1.00 2681 141 0.1572 0.2339
REMARK 3 5 4.6189 - 4.2881 1.00 2640 168 0.1517 0.2065
REMARK 3 6 4.2881 - 4.0354 1.00 2601 178 0.1596 0.1998
REMARK 3 7 4.0354 - 3.8334 0.97 2505 187 0.2020 0.2332
REMARK 3 8 3.8334 - 3.6666 0.89 2371 122 0.3358 0.4470
REMARK 3 9 3.6666 - 3.5255 0.90 2363 104 0.3504 0.5032
REMARK 3 10 3.5255 - 3.4039 1.00 2667 129 0.2386 0.2901
REMARK 3 11 3.4039 - 3.2975 1.00 2613 159 0.2457 0.3123
REMARK 3 12 3.2975 - 3.2033 1.00 2579 159 0.2358 0.3220
REMARK 3 13 3.2033 - 3.1190 1.00 2605 166 0.2354 0.2931
REMARK 3 14 3.1190 - 3.0429 1.00 2599 132 0.2474 0.3574
REMARK 3 15 3.0429 - 2.9737 1.00 2629 152 0.2512 0.3082
REMARK 3 16 2.9737 - 2.9105 1.00 2611 144 0.2490 0.2854
REMARK 3 17 2.9105 - 2.8522 1.00 2589 152 0.2511 0.3276
REMARK 3 18 2.8522 - 2.7984 1.00 2616 118 0.2593 0.3877
REMARK 3 19 2.7984 - 2.7485 1.00 2625 126 0.2685 0.3406
REMARK 3 20 2.7485 - 2.7019 1.00 2623 134 0.2862 0.4184
REMARK 3 21 2.7019 - 2.6583 1.00 2638 115 0.3054 0.3669
REMARK 3 22 2.6583 - 2.6174 1.00 2586 142 0.3160 0.4520
REMARK 3 23 2.6174 - 2.5789 1.00 2591 130 0.3279 0.4128
REMARK 3 24 2.5789 - 2.5430 0.96 2489 151 0.3429 0.3891
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.03
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 6XTC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1292106266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66790
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 45.524
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.16300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 13.70
REMARK 200 R MERGE FOR SHELL (I) : 1.78800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4HZG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, LITHIUM SULPHATE,
REMARK 280 TRIS, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 60.40450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.94250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.09100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.94250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.40450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.09100
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: 17140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -351.0 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: 15820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -257.0 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 1
REMARK 465 SER A 2
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 HIS C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 HIS D 294
REMARK 465 HIS D 295
REMARK 465 HIS D 296
REMARK 465 HIS D 297
REMARK 465 HIS D 298
REMARK 465 HIS D 299
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 ASP A 11 C - N - CA ANGL. DEV. = -15.3 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 PRO A 9 44.51 -97.47
REMARK 500 PRO A 29 -177.93 -69.21
REMARK 500 PRO A 42 42.29 -99.26
REMARK 500 PRO A 57 45.03 -72.24
REMARK 500 SER A 58 -34.35 -171.97
REMARK 500 LEU A 66 154.40 -49.66
REMARK 500 GLU A 98 -124.91 -93.01
REMARK 500 ASP A 106 -121.30 66.85
REMARK 500 ASN A 119 57.18 -140.49
REMARK 500 VAL A 245 -62.22 -135.38
REMARK 500 LEU A 271 -94.14 -114.06
REMARK 500 ASN A 278 65.58 -157.00
REMARK 500 ALA A 292 30.50 -84.55
REMARK 500 LEU B 18 68.01 29.07
REMARK 500 PRO B 29 161.27 -48.56
REMARK 500 ASP B 31 -179.87 -58.49
REMARK 500 PRO B 42 48.22 -107.20
REMARK 500 THR B 43 -154.33 -101.27
REMARK 500 SER B 44 -163.60 -161.56
REMARK 500 LYS B 74 74.41 -118.48
REMARK 500 GLU B 98 -79.91 -94.18
REMARK 500 GLU B 98 -79.43 -94.18
REMARK 500 ASP B 106 -122.27 64.63
REMARK 500 PRO B 155 -157.04 -80.60
REMARK 500 ASP B 198 4.12 -69.24
REMARK 500 VAL B 245 -65.33 -133.65
REMARK 500 ASN B 261 60.67 63.13
REMARK 500 LEU B 271 -87.14 -117.27
REMARK 500 ILE C 4 98.77 63.27
REMARK 500 LEU C 18 58.97 36.67
REMARK 500 ARG C 30 45.48 -87.73
REMARK 500 PRO C 42 42.21 -109.85
REMARK 500 GLU C 98 -88.34 -107.73
REMARK 500 ASP C 106 -130.44 62.61
REMARK 500 GLU C 121 -60.42 -5.68
REMARK 500 PRO C 155 -145.55 -81.83
REMARK 500 GLN C 231 -43.81 -136.64
REMARK 500 SER C 232 107.28 -49.93
REMARK 500 VAL C 245 -71.21 -140.31
REMARK 500 GLU C 257 47.01 -102.18
REMARK 500 SER C 258 -30.39 -150.28
REMARK 500 LEU C 271 -93.97 -104.77
REMARK 500 ASN C 278 65.44 -166.57
REMARK 500 ALA C 292 27.29 -59.67
REMARK 500 ILE D 4 111.31 64.64
REMARK 500 LEU D 18 45.55 30.14
REMARK 500 ASP D 31 -149.92 -168.55
REMARK 500 THR D 43 -149.02 -89.44
REMARK 500 SER D 44 -157.24 -170.07
REMARK 500 LEU D 66 150.68 -48.81
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 307
DBREF 6XTC A 1 299 PDB 6XTC 6XTC 1 299
DBREF 6XTC B 1 299 PDB 6XTC 6XTC 1 299
DBREF 6XTC C 1 299 PDB 6XTC 6XTC 1 299
DBREF 6XTC D 1 299 PDB 6XTC 6XTC 1 299
SEQRES 1 A 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 A 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 B 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 B 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 B 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 B 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 B 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 B 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 B 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 B 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 B 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 B 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 B 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 B 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 B 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 B 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 B 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 B 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 B 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 B 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 B 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 B 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 B 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 B 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 C 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 C 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 C 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 C 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 C 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 C 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 C 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 C 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 C 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 C 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 C 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 C 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 C 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 C 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 C 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 C 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 C 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 C 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 C 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 C 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 C 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 C 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 D 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 D 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 D 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 D 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 D 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 D 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 D 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 D 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 D 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 D 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 D 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP
SEQRES 13 D 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 D 299 GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 D 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 D 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 D 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 D 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 D 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 D 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 D 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 D 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 D 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET GOL A 301 6
HET GOL A 302 6
HET SO4 A 303 5
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HET SO4 A 307 5
HET SO4 A 308 5
HET SO4 A 309 5
HET SO4 A 310 5
HET SO4 A 311 5
HET SO4 A 312 5
HET SO4 B 301 5
HET SO4 B 302 5
HET SO4 B 303 5
HET SO4 B 304 5
HET SO4 B 305 5
HET SO4 B 306 5
HET SO4 B 307 5
HET SO4 B 308 5
HET SO4 B 309 5
HET SO4 B 310 5
HET SO4 B 311 5
HET SO4 B 312 5
HET SO4 B 313 5
HET SO4 C 301 5
HET SO4 C 302 5
HET SO4 C 303 5
HET SO4 C 304 5
HET SO4 C 305 5
HET SO4 D 301 5
HET SO4 D 302 5
HET SO4 D 303 5
HET SO4 D 304 5
HET SO4 D 305 5
HET SO4 D 306 5
HET SO4 D 307 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 SO4 35(O4 S 2-)
FORMUL 42 HOH *252(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 TRP A 107 ASN A 119 1 13
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 GLY A 171 PHE A 176 1 6
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 LYS A 195 ASP A 198 5 4
HELIX 13 AB4 ARG A 199 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 TYR A 273 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 LEU A 290 1 13
HELIX 18 AB9 SER B 44 ARG B 49 5 6
HELIX 19 AC1 ILE B 51 ALA B 56 1 6
HELIX 20 AC2 PHE B 80 LEU B 95 1 16
HELIX 21 AC3 TRP B 107 ASN B 119 1 13
HELIX 22 AC4 THR B 137 TRP B 141 5 5
HELIX 23 AC5 PRO B 142 ARG B 153 1 12
HELIX 24 AC6 ASP B 156 ILE B 163 1 8
HELIX 25 AC7 ASN B 166 GLY B 171 1 6
HELIX 26 AC8 GLY B 171 PHE B 176 1 6
HELIX 27 AC9 THR B 182 GLU B 191 1 10
HELIX 28 AD1 PRO B 192 LEU B 194 5 3
HELIX 29 AD2 LYS B 195 ASP B 198 5 4
HELIX 30 AD3 ARG B 199 LEU B 209 1 11
HELIX 31 AD4 PRO B 215 SER B 232 1 18
HELIX 32 AD5 PRO B 248 LEU B 259 1 12
HELIX 33 AD6 TYR B 273 ASP B 277 5 5
HELIX 34 AD7 ASN B 278 LEU B 290 1 13
HELIX 35 AD8 SER C 44 ARG C 49 5 6
HELIX 36 AD9 ILE C 51 ALA C 56 1 6
HELIX 37 AE1 PHE C 80 LEU C 95 1 16
HELIX 38 AE2 ASP C 106 ASN C 119 1 14
HELIX 39 AE3 THR C 137 TRP C 141 5 5
HELIX 40 AE4 PRO C 142 ARG C 153 1 12
HELIX 41 AE5 ASP C 156 ILE C 163 1 8
HELIX 42 AE6 ASN C 166 GLY C 171 1 6
HELIX 43 AE7 GLY C 171 PHE C 176 1 6
HELIX 44 AE8 THR C 182 GLU C 191 1 10
HELIX 45 AE9 PRO C 192 LEU C 194 5 3
HELIX 46 AF1 LYS C 195 ASP C 198 5 4
HELIX 47 AF2 ARG C 199 LEU C 209 1 11
HELIX 48 AF3 PRO C 215 HIS C 230 1 16
HELIX 49 AF4 PRO C 248 GLU C 257 1 10
HELIX 50 AF5 TYR C 273 ASN C 278 1 6
HELIX 51 AF6 ASN C 278 LEU C 290 1 13
HELIX 52 AF7 SER D 44 ARG D 49 5 6
HELIX 53 AF8 ILE D 51 ALA D 56 1 6
HELIX 54 AF9 PHE D 80 LEU D 95 1 16
HELIX 55 AG1 HIS D 105 ASN D 119 1 15
HELIX 56 AG2 THR D 137 TRP D 141 5 5
HELIX 57 AG3 PRO D 142 ARG D 153 1 12
HELIX 58 AG4 ASP D 156 ILE D 163 1 8
HELIX 59 AG5 ASN D 166 GLY D 171 1 6
HELIX 60 AG6 GLY D 171 PHE D 176 1 6
HELIX 61 AG7 THR D 182 GLU D 191 1 10
HELIX 62 AG8 PRO D 192 LEU D 194 5 3
HELIX 63 AG9 LYS D 195 ASP D 198 5 4
HELIX 64 AH1 ARG D 199 PHE D 205 1 7
HELIX 65 AH2 PRO D 215 HIS D 230 1 16
HELIX 66 AH3 PRO D 248 LEU D 259 1 12
HELIX 67 AH4 TYR D 273 ASN D 278 1 6
HELIX 68 AH5 ASN D 278 LEU D 290 1 13
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O MET A 22 N VAL A 15
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 ASP A 106 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 PHE A 131 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS B 236 PRO B 243 1 O PHE B 239 N CYS A 128
SHEET 8 AA1 8 CYS B 262 GLY B 270 1 O ILE B 267 N TRP B 240
SHEET 1 AA2 8 CYS A 262 GLY A 270 0
SHEET 2 AA2 8 LYS A 236 PRO A 243 1 N LEU A 238 O LYS A 263
SHEET 3 AA2 8 VAL B 123 PHE B 131 1 O CYS B 128 N LEU A 237
SHEET 4 AA2 8 VAL B 100 ASP B 106 1 N VAL B 100 O LYS B 124
SHEET 5 AA2 8 VAL B 35 LEU B 38 1 N LEU B 36 O VAL B 103
SHEET 6 AA2 8 CYS B 61 PRO B 64 1 O ILE B 62 N VAL B 35
SHEET 7 AA2 8 GLU B 20 VAL B 27 -1 N VAL B 27 O CYS B 61
SHEET 8 AA2 8 HIS B 13 VAL B 17 -1 N VAL B 17 O GLU B 20
SHEET 1 AA3 8 HIS C 13 VAL C 17 0
SHEET 2 AA3 8 GLU C 20 VAL C 27 -1 O GLU C 20 N VAL C 17
SHEET 3 AA3 8 CYS C 61 PRO C 64 -1 O CYS C 61 N VAL C 27
SHEET 4 AA3 8 VAL C 35 LEU C 38 1 N PHE C 37 O ILE C 62
SHEET 5 AA3 8 VAL C 100 HIS C 105 1 O VAL C 103 N LEU C 38
SHEET 6 AA3 8 VAL C 123 MET C 129 1 O ALA C 127 N LEU C 102
SHEET 7 AA3 8 LYS D 236 PRO D 243 1 O LEU D 237 N ILE C 126
SHEET 8 AA3 8 CYS D 262 GLY D 270 1 O GLY D 270 N THR D 242
SHEET 1 AA4 8 CYS C 262 GLY C 270 0
SHEET 2 AA4 8 LYS C 236 PRO C 243 1 N LYS C 236 O LYS C 263
SHEET 3 AA4 8 VAL D 123 MET D 129 1 O CYS D 128 N PHE C 239
SHEET 4 AA4 8 VAL D 100 ILE D 104 1 N LEU D 102 O ALA D 127
SHEET 5 AA4 8 VAL D 35 LEU D 38 1 N LEU D 38 O VAL D 103
SHEET 6 AA4 8 CYS D 61 ASP D 65 1 O ILE D 62 N VAL D 35
SHEET 7 AA4 8 GLU D 20 VAL D 27 -1 N VAL D 27 O CYS D 61
SHEET 8 AA4 8 HIS D 13 VAL D 17 -1 N HIS D 13 O TYR D 24
CISPEP 1 ASN A 41 PRO A 42 0 -2.89
CISPEP 2 GLU A 214 PRO A 215 0 -3.24
CISPEP 3 THR A 242 PRO A 243 0 5.10
CISPEP 4 ASN B 41 PRO B 42 0 -2.42
CISPEP 5 GLU B 214 PRO B 215 0 -6.79
CISPEP 6 THR B 242 PRO B 243 0 5.89
CISPEP 7 ASN C 41 PRO C 42 0 -0.81
CISPEP 8 GLU C 214 PRO C 215 0 -3.28
CISPEP 9 THR C 242 PRO C 243 0 6.52
CISPEP 10 ASN D 41 PRO D 42 0 9.16
CISPEP 11 GLU D 214 PRO D 215 0 2.28
CISPEP 12 THR D 242 PRO D 243 0 0.31
SITE 1 AC1 1 ASN A 261
SITE 1 AC2 2 ARG A 118 HOH A 410
SITE 1 AC3 4 TRP A 228 GLN A 231 SER A 232 PRO A 233
SITE 1 AC4 5 ARG A 288 HOH A 414 ASP C 139 GLU C 143
SITE 2 AC4 5 ARG C 146
SITE 1 AC5 1 ARG A 204
SITE 1 AC6 5 GLU A 214 PRO A 215 ALA A 216 HOH A 401
SITE 2 AC6 5 GLU C 3
SITE 1 AC7 4 MET A 226 HIS A 230 ARG B 133 PRO B 134
SITE 1 AC8 3 LEU A 77 ARG A 86 TYR A 87
SITE 1 AC9 3 ASP A 164 PRO A 196 ARG A 199
SITE 1 AD1 4 TRP A 138 ARG A 153 HOH A 419 GLU B 214
SITE 1 AD2 3 ARG A 133 MET B 226 HIS B 230
SITE 1 AD3 1 ARG A 288
SITE 1 AD4 3 GLY B 5 THR B 6 GLY B 7
SITE 1 AD5 3 HIS A 188 GLY B 7 PHE B 8
SITE 1 AD6 3 ILE A 211 TRP B 138 ARG B 153
SITE 1 AD7 2 PRO B 260 ASN B 261
SITE 1 AD8 3 ARG B 288 HOH B 405 ARG D 146
SITE 1 AD9 3 LEU B 77 ARG B 86 TYR B 87
SITE 1 AE1 2 PHE A 80 ARG B 204
SITE 1 AE2 4 GLU B 214 PRO B 215 ALA B 216 HOH B 424
SITE 1 AE3 5 PRO A 120 TRP B 228 GLN B 231 SER B 232
SITE 2 AE3 5 PRO B 233
SITE 1 AE4 5 VAL B 27 GLY B 28 ARG B 30 ARG C 21
SITE 2 AE4 5 SO4 C 301
SITE 1 AE5 4 ASP B 139 TRP B 141 GLU B 143 ARG B 146
SITE 1 AE6 3 PRO B 248 PRO B 249 ALA B 250
SITE 1 AE7 1 ARG B 118
SITE 1 AE8 4 SO4 B 310 TYR C 14 ARG C 21 ASP C 73
SITE 1 AE9 4 TRP C 138 ARG C 153 ILE D 211 GLU D 214
SITE 1 AF1 3 GLY C 5 THR C 6 GLY C 7
SITE 1 AF2 2 LEU C 77 ARG C 86
SITE 1 AF3 1 ARG C 204
SITE 1 AF4 3 LEU D 194 PRO D 196 ARG D 199
SITE 1 AF5 3 TRP D 228 GLN D 231 SER D 232
SITE 1 AF6 3 GLU C 214 TRP D 138 ARG D 153
SITE 1 AF7 1 ARG D 159
SITE 1 AF8 3 PRO D 248 PRO D 249 ALA D 250
SITE 1 AF9 1 ASN D 261
SITE 1 AG1 1 ARG D 204
CRYST1 120.809 124.182 133.885 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 0.008278 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007469 0.00000
TER 2350 LEU A 293
TER 4729 LEU B 293
TER 7079 LEU C 293
TER 9440 LEU D 293
MASTER 503 0 37 68 32 0 41 6 9835 4 187 92
END |