| content |
HEADER HYDROLASE 09-MAY-17 5XKS
TITLE CRYSTAL STRUCTURE OF MONOACYLGLYCEROL LIPASE FROM THERMOPHILIC
TITLE 2 GEOBACILLUS SP. 12AMOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.1.1.23;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS SP. 12AMOR1;
SOURCE 3 ORGANISM_TAXID: 1629723;
SOURCE 4 GENE: GARCT_00911;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR
SOURCE 6 PPPARG4;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1182032
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.WANG,D.M.LAN
REVDAT 1 09-MAY-18 5XKS 0
JRNL AUTH Y.H.WANG,D.M.LAN
JRNL TITL CRYSTAL STRUCTURE OF MONOACYLGLYCEROL LIPASE FROM
JRNL TITL 2 THERMOPHILIC GEOBACILLUS SP. 12AMOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX PHENIX.REFINE: 1.9_1692
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 74115
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3554
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.63
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 5XKS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1300003668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 0.978530
REMARK 200 MONOCHROMATOR : MD2
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74128
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.189
REMARK 200 RESOLUTION RANGE LOW (A) : 43.063
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.843
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.71
REMARK 200 R MERGE FOR SHELL (I) : 0.62600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.020
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: 4LHE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M MES
REMARK 280 MONOHYDRATE PH 6.5, 30%(W/V) POLYETHYLENE GLYCOL MONOMETHYL
REMARK 280 ETHER 5,000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 68.10350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 HIS A 256
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 465 HIS B 255
REMARK 465 HIS B 256
REMARK 465 HIS C 253
REMARK 465 HIS C 254
REMARK 465 HIS C 255
REMARK 465 HIS C 256
REMARK 465 HIS D 252
REMARK 465 HIS D 253
REMARK 465 HIS D 254
REMARK 465 HIS D 255
REMARK 465 HIS D 256
REMARK 465 HIS E 252
REMARK 465 HIS E 253
REMARK 465 HIS E 254
REMARK 465 HIS E 255
REMARK 465 HIS E 256
REMARK 465 HIS F 254
REMARK 465 HIS F 255
REMARK 465 HIS F 256
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 2 CG2
REMARK 470 THR B 2 CG2
REMARK 470 THR C 2 CG2
REMARK 470 THR D 2 CG2
REMARK 470 THR E 2 CG2
REMARK 470 THR F 2 CG2
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 310 O HOH D 403 1.72
REMARK 500 O HOH C 364 O HOH F 382 1.82
REMARK 500 O HOH D 323 O HOH D 390 1.83
REMARK 500 OD2 ASP B 239 O HOH B 301 1.88
REMARK 500 O HOH F 355 O HOH F 356 1.90
REMARK 500 O GLU A 112 O HOH A 301 1.90
REMARK 500 O HOH E 326 O HOH E 363 1.90
REMARK 500 O HOH F 361 O HOH F 401 1.91
REMARK 500 OD1 ASP B 209 O HOH B 302 1.91
REMARK 500 O HOH F 339 O HOH F 414 1.93
REMARK 500 O TYR D 48 O HOH D 301 1.94
REMARK 500 NZ LYS A 247 O HOH A 302 1.94
REMARK 500 OD1 ASP A 137 O HOH A 303 1.96
REMARK 500 O HOH D 352 O HOH D 412 1.97
REMARK 500 O HOH F 367 O HOH F 406 2.00
REMARK 500 O HOH B 405 O HOH B 411 2.01
REMARK 500 O GLU E 3 O HOH E 301 2.01
REMARK 500 O HOH E 356 O HOH E 363 2.04
REMARK 500 O ASP F 194 O HOH F 301 2.04
REMARK 500 OE1 GLU E 175 O HOH E 302 2.05
REMARK 500 O HOH B 384 O HOH B 387 2.05
REMARK 500 OG1 THR E 90 O HOH E 303 2.07
REMARK 500 OE2 GLU F 17 O HOH F 302 2.08
REMARK 500 O HOH C 354 O HOH C 363 2.08
REMARK 500 OE2 GLU D 82 O HOH D 302 2.09
REMARK 500 O HOH F 379 O HOH F 404 2.09
REMARK 500 O HOH E 326 O HOH E 356 2.09
REMARK 500 O HOH F 329 O HOH F 398 2.09
REMARK 500 OE2 GLU B 41 O HOH B 303 2.10
REMARK 500 OE1 GLN D 71 O HOH D 303 2.10
REMARK 500 O HOH D 379 O HOH D 414 2.11
REMARK 500 O HOH A 417 O HOH A 419 2.11
REMARK 500 O HOH A 416 O HOH B 404 2.11
REMARK 500 OD1 ASP C 209 O HOH C 301 2.12
REMARK 500 OD1 ASP C 72 O HOH C 302 2.13
REMARK 500 O HOH F 390 O HOH F 401 2.13
REMARK 500 OD2 ASP D 239 O HOH D 304 2.13
REMARK 500 O LEU D 242 O HOH D 305 2.14
REMARK 500 O GLY A 146 O HOH A 304 2.14
REMARK 500 OE2 GLU F 195 O HOH F 303 2.16
REMARK 500 OE2 GLU E 112 O HOH E 304 2.16
REMARK 500 OH TYR D 43 O HOH D 306 2.16
REMARK 500 O ILE D 211 O HOH D 307 2.17
REMARK 500 O GLU D 17 O HOH D 308 2.17
REMARK 500 OD1 ASP F 250 O HOH F 304 2.17
REMARK 500 O HOH F 313 O HOH F 393 2.18
REMARK 500 OE2 GLU A 12 O HOH A 305 2.18
REMARK 500 O HOH B 339 O HOH B 395 2.18
REMARK 500 O CYS D 186 OG SER D 213 2.19
REMARK 500 O HOH F 372 O HOH F 408 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 359 O HOH C 373 1455 1.90
REMARK 500 O HOH E 371 O HOH E 373 1455 1.92
REMARK 500 O HOH A 390 O HOH B 396 27410 1.97
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 ASN A 19 -163.78 -78.34
REMARK 500 THR A 30 -1.45 65.77
REMARK 500 THR A 60 -74.00 -123.97
REMARK 500 SER A 97 -115.08 59.86
REMARK 500 VAL A 135 -18.06 92.17
REMARK 500 VAL A 198 -59.35 -120.60
REMARK 500 TYR A 225 -159.97 -94.96
REMARK 500 ASN B 19 -166.81 -76.41
REMARK 500 THR B 30 -1.60 65.53
REMARK 500 THR B 60 -73.91 -120.07
REMARK 500 SER B 97 -120.71 59.79
REMARK 500 VAL B 198 -61.28 -109.14
REMARK 500 ASN C 19 -169.14 -79.94
REMARK 500 THR C 30 -1.88 69.43
REMARK 500 THR C 60 -74.85 -125.94
REMARK 500 SER C 97 -115.88 59.45
REMARK 500 VAL C 135 -16.02 86.90
REMARK 500 VAL C 198 -61.49 -121.23
REMARK 500 ASN D 19 -169.06 -74.99
REMARK 500 THR D 30 -0.92 71.43
REMARK 500 THR D 60 -70.92 -129.75
REMARK 500 SER D 97 -120.59 58.22
REMARK 500 VAL D 135 -16.81 85.22
REMARK 500 THR E 30 -3.50 65.63
REMARK 500 THR E 60 -76.71 -122.94
REMARK 500 SER E 97 -117.58 56.10
REMARK 500 VAL E 198 -62.15 -122.93
REMARK 500 THR F 30 -4.59 65.38
REMARK 500 THR F 60 -78.19 -118.55
REMARK 500 SER F 97 -117.17 60.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5XK2 RELATED DB: PDB
DBREF1 5XKS A 1 251 UNP A0A0G3XXB4_9BACI
DBREF2 5XKS A A0A0G3XXB4 1 251
DBREF1 5XKS B 1 251 UNP A0A0G3XXB4_9BACI
DBREF2 5XKS B A0A0G3XXB4 1 251
DBREF1 5XKS C 1 251 UNP A0A0G3XXB4_9BACI
DBREF2 5XKS C A0A0G3XXB4 1 251
DBREF1 5XKS D 1 251 UNP A0A0G3XXB4_9BACI
DBREF2 5XKS D A0A0G3XXB4 1 251
DBREF1 5XKS E 1 251 UNP A0A0G3XXB4_9BACI
DBREF2 5XKS E A0A0G3XXB4 1 251
DBREF1 5XKS F 1 251 UNP A0A0G3XXB4_9BACI
DBREF2 5XKS F A0A0G3XXB4 1 251
SEQADV 5XKS HIS A 252 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS A 253 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS A 254 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS A 255 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS A 256 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS B 252 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS B 253 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS B 254 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS B 255 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS B 256 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS C 252 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS C 253 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS C 254 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS C 255 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS C 256 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS D 252 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS D 253 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS D 254 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS D 255 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS D 256 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS E 252 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS E 253 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS E 254 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS E 255 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS E 256 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS F 252 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS F 253 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS F 254 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS F 255 UNP A0A0G3XXB EXPRESSION TAG
SEQADV 5XKS HIS F 256 UNP A0A0G3XXB EXPRESSION TAG
SEQRES 1 A 256 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 A 256 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 A 256 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 A 256 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 A 256 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 A 256 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 A 256 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 A 256 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 A 256 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 A 256 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 A 256 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 A 256 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 A 256 LEU ALA TYR GLU LYS THR PRO ALA ALA SER ILE ARG GLN
SEQRES 14 A 256 ILE VAL GLN LEU MET GLU ARG VAL LYS THR ASP LEU HIS
SEQRES 15 A 256 LYS ILE THR CYS PRO ALA ILE LEU PHE CYS SER ASP GLU
SEQRES 16 A 256 ASP HIS VAL VAL PRO PRO ASP ASN ALA PRO PHE ILE TYR
SEQRES 17 A 256 ASP HIS ILE ALA SER ALA ASP LYS LYS LEU VAL ARG LEU
SEQRES 18 A 256 PRO ASP SER TYR HIS VAL ALA THR LEU ASP ASN ASP ARG
SEQRES 19 A 256 GLN LYS ILE ILE ASP THR SER LEU ALA PHE PHE LYS LYS
SEQRES 20 A 256 HIS ALA ASP ARG HIS HIS HIS HIS HIS
SEQRES 1 B 256 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 B 256 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 B 256 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 B 256 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 B 256 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 B 256 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 B 256 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 B 256 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 B 256 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 B 256 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 B 256 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 B 256 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 B 256 LEU ALA TYR GLU LYS THR PRO ALA ALA SER ILE ARG GLN
SEQRES 14 B 256 ILE VAL GLN LEU MET GLU ARG VAL LYS THR ASP LEU HIS
SEQRES 15 B 256 LYS ILE THR CYS PRO ALA ILE LEU PHE CYS SER ASP GLU
SEQRES 16 B 256 ASP HIS VAL VAL PRO PRO ASP ASN ALA PRO PHE ILE TYR
SEQRES 17 B 256 ASP HIS ILE ALA SER ALA ASP LYS LYS LEU VAL ARG LEU
SEQRES 18 B 256 PRO ASP SER TYR HIS VAL ALA THR LEU ASP ASN ASP ARG
SEQRES 19 B 256 GLN LYS ILE ILE ASP THR SER LEU ALA PHE PHE LYS LYS
SEQRES 20 B 256 HIS ALA ASP ARG HIS HIS HIS HIS HIS
SEQRES 1 C 256 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 C 256 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 C 256 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 C 256 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 C 256 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 C 256 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 C 256 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 C 256 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 C 256 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 C 256 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 C 256 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 C 256 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 C 256 LEU ALA TYR GLU LYS THR PRO ALA ALA SER ILE ARG GLN
SEQRES 14 C 256 ILE VAL GLN LEU MET GLU ARG VAL LYS THR ASP LEU HIS
SEQRES 15 C 256 LYS ILE THR CYS PRO ALA ILE LEU PHE CYS SER ASP GLU
SEQRES 16 C 256 ASP HIS VAL VAL PRO PRO ASP ASN ALA PRO PHE ILE TYR
SEQRES 17 C 256 ASP HIS ILE ALA SER ALA ASP LYS LYS LEU VAL ARG LEU
SEQRES 18 C 256 PRO ASP SER TYR HIS VAL ALA THR LEU ASP ASN ASP ARG
SEQRES 19 C 256 GLN LYS ILE ILE ASP THR SER LEU ALA PHE PHE LYS LYS
SEQRES 20 C 256 HIS ALA ASP ARG HIS HIS HIS HIS HIS
SEQRES 1 D 256 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 D 256 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 D 256 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 D 256 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 D 256 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 D 256 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 D 256 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 D 256 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 D 256 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 D 256 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 D 256 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 D 256 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 D 256 LEU ALA TYR GLU LYS THR PRO ALA ALA SER ILE ARG GLN
SEQRES 14 D 256 ILE VAL GLN LEU MET GLU ARG VAL LYS THR ASP LEU HIS
SEQRES 15 D 256 LYS ILE THR CYS PRO ALA ILE LEU PHE CYS SER ASP GLU
SEQRES 16 D 256 ASP HIS VAL VAL PRO PRO ASP ASN ALA PRO PHE ILE TYR
SEQRES 17 D 256 ASP HIS ILE ALA SER ALA ASP LYS LYS LEU VAL ARG LEU
SEQRES 18 D 256 PRO ASP SER TYR HIS VAL ALA THR LEU ASP ASN ASP ARG
SEQRES 19 D 256 GLN LYS ILE ILE ASP THR SER LEU ALA PHE PHE LYS LYS
SEQRES 20 D 256 HIS ALA ASP ARG HIS HIS HIS HIS HIS
SEQRES 1 E 256 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 E 256 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 E 256 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 E 256 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 E 256 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 E 256 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 E 256 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 E 256 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 E 256 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 E 256 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 E 256 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 E 256 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 E 256 LEU ALA TYR GLU LYS THR PRO ALA ALA SER ILE ARG GLN
SEQRES 14 E 256 ILE VAL GLN LEU MET GLU ARG VAL LYS THR ASP LEU HIS
SEQRES 15 E 256 LYS ILE THR CYS PRO ALA ILE LEU PHE CYS SER ASP GLU
SEQRES 16 E 256 ASP HIS VAL VAL PRO PRO ASP ASN ALA PRO PHE ILE TYR
SEQRES 17 E 256 ASP HIS ILE ALA SER ALA ASP LYS LYS LEU VAL ARG LEU
SEQRES 18 E 256 PRO ASP SER TYR HIS VAL ALA THR LEU ASP ASN ASP ARG
SEQRES 19 E 256 GLN LYS ILE ILE ASP THR SER LEU ALA PHE PHE LYS LYS
SEQRES 20 E 256 HIS ALA ASP ARG HIS HIS HIS HIS HIS
SEQRES 1 F 256 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 F 256 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 F 256 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 F 256 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 F 256 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 F 256 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 F 256 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 F 256 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 F 256 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 F 256 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 F 256 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 F 256 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 F 256 LEU ALA TYR GLU LYS THR PRO ALA ALA SER ILE ARG GLN
SEQRES 14 F 256 ILE VAL GLN LEU MET GLU ARG VAL LYS THR ASP LEU HIS
SEQRES 15 F 256 LYS ILE THR CYS PRO ALA ILE LEU PHE CYS SER ASP GLU
SEQRES 16 F 256 ASP HIS VAL VAL PRO PRO ASP ASN ALA PRO PHE ILE TYR
SEQRES 17 F 256 ASP HIS ILE ALA SER ALA ASP LYS LYS LEU VAL ARG LEU
SEQRES 18 F 256 PRO ASP SER TYR HIS VAL ALA THR LEU ASP ASN ASP ARG
SEQRES 19 F 256 GLN LYS ILE ILE ASP THR SER LEU ALA PHE PHE LYS LYS
SEQRES 20 F 256 HIS ALA ASP ARG HIS HIS HIS HIS HIS
FORMUL 7 HOH *645(H2 O)
HELIX 1 AA1 SER A 32 SER A 35 5 4
HELIX 2 AA2 MET A 36 ALA A 46 1 11
HELIX 3 AA3 HIS A 61 LYS A 67 1 7
HELIX 4 AA4 THR A 69 CYS A 88 1 20
HELIX 5 AA5 SER A 97 HIS A 110 1 14
HELIX 6 AA6 MET A 125 GLY A 134 1 10
HELIX 7 AA7 ALA A 164 ASP A 180 1 17
HELIX 8 AA8 LEU A 181 ILE A 184 5 4
HELIX 9 AA9 ASP A 202 ILE A 211 1 10
HELIX 10 AB1 VAL A 227 ASP A 231 5 5
HELIX 11 AB2 ASP A 233 HIS A 252 1 20
HELIX 12 AB3 SER B 32 SER B 35 5 4
HELIX 13 AB4 MET B 36 ALA B 46 1 11
HELIX 14 AB5 HIS B 61 LYS B 67 1 7
HELIX 15 AB6 THR B 69 CYS B 88 1 20
HELIX 16 AB7 SER B 97 HIS B 110 1 14
HELIX 17 AB8 MET B 125 LEU B 132 1 8
HELIX 18 AB9 GLY B 134 LEU B 138 5 5
HELIX 19 AC1 SER B 166 ASP B 180 1 15
HELIX 20 AC2 LEU B 181 ILE B 184 5 4
HELIX 21 AC3 ASP B 202 ILE B 211 1 10
HELIX 22 AC4 VAL B 227 ASP B 231 5 5
HELIX 23 AC5 ASP B 233 ARG B 251 1 19
HELIX 24 AC6 SER C 32 SER C 35 5 4
HELIX 25 AC7 MET C 36 ALA C 46 1 11
HELIX 26 AC8 HIS C 61 LYS C 67 1 7
HELIX 27 AC9 THR C 69 CYS C 88 1 20
HELIX 28 AD1 SER C 97 HIS C 110 1 14
HELIX 29 AD2 MET C 125 GLY C 134 1 10
HELIX 30 AD3 ALA C 165 ASP C 180 1 16
HELIX 31 AD4 LEU C 181 ILE C 184 5 4
HELIX 32 AD5 ASP C 202 ILE C 211 1 10
HELIX 33 AD6 VAL C 227 ASP C 231 5 5
HELIX 34 AD7 ASP C 233 ARG C 251 1 19
HELIX 35 AD8 SER D 32 SER D 35 5 4
HELIX 36 AD9 MET D 36 ALA D 46 1 11
HELIX 37 AE1 HIS D 61 THR D 68 1 8
HELIX 38 AE2 THR D 69 CYS D 88 1 20
HELIX 39 AE3 SER D 97 HIS D 110 1 14
HELIX 40 AE4 MET D 125 ALA D 131 1 7
HELIX 41 AE5 ALA D 164 ASP D 180 1 17
HELIX 42 AE6 LEU D 181 ILE D 184 5 4
HELIX 43 AE7 ASP D 202 ILE D 211 1 10
HELIX 44 AE8 VAL D 227 ASP D 231 5 5
HELIX 45 AE9 ASP D 233 ASP D 250 1 18
HELIX 46 AF1 SER E 32 SER E 35 5 4
HELIX 47 AF2 MET E 36 ALA E 46 1 11
HELIX 48 AF3 HIS E 61 LYS E 67 1 7
HELIX 49 AF4 THR E 69 CYS E 88 1 20
HELIX 50 AF5 SER E 97 HIS E 110 1 14
HELIX 51 AF6 MET E 125 LEU E 132 1 8
HELIX 52 AF7 ALA E 164 ASP E 180 1 17
HELIX 53 AF8 LEU E 181 ILE E 184 5 4
HELIX 54 AF9 ASP E 202 ILE E 211 1 10
HELIX 55 AG1 ASP E 233 ASP E 250 1 18
HELIX 56 AG2 SER F 32 SER F 35 5 4
HELIX 57 AG3 MET F 36 ALA F 46 1 11
HELIX 58 AG4 HIS F 61 LYS F 67 1 7
HELIX 59 AG5 THR F 69 CYS F 88 1 20
HELIX 60 AG6 SER F 97 HIS F 110 1 14
HELIX 61 AG7 MET F 125 LEU F 132 1 8
HELIX 62 AG8 ALA F 164 ASP F 180 1 17
HELIX 63 AG9 LEU F 181 ILE F 184 5 4
HELIX 64 AH1 ASP F 202 ILE F 211 1 10
HELIX 65 AH2 VAL F 227 ASN F 232 5 6
HELIX 66 AH3 ASP F 233 ARG F 251 1 19
SHEET 1 AA1 5 PHE A 14 PHE A 16 0
SHEET 2 AA1 5 THR A 49 GLY A 52 -1 O VAL A 50 N PHE A 16
SHEET 3 AA1 5 ILE A 21 LEU A 26 1 N ILE A 23 O CYS A 51
SHEET 4 AA1 5 THR A 90 LEU A 96 1 O THR A 90 N GLY A 22
SHEET 5 AA1 5 GLY A 115 ILE A 119 1 O ILE A 119 N GLY A 95
SHEET 1 AA2 2 PHE A 141 ASP A 143 0
SHEET 2 AA2 2 LYS A 161 PRO A 163 -1 O THR A 162 N LEU A 142
SHEET 1 AA3 2 ALA A 188 SER A 193 0
SHEET 2 AA3 2 LYS A 216 LEU A 221 1 O VAL A 219 N LEU A 190
SHEET 1 AA4 5 PHE B 14 PHE B 16 0
SHEET 2 AA4 5 THR B 49 GLY B 52 -1 O VAL B 50 N PHE B 16
SHEET 3 AA4 5 ILE B 21 LEU B 26 1 N ILE B 23 O THR B 49
SHEET 4 AA4 5 THR B 90 LEU B 96 1 O THR B 94 N LEU B 24
SHEET 5 AA4 5 GLY B 115 ILE B 119 1 O ILE B 119 N GLY B 95
SHEET 1 AA5 2 PHE B 141 ASP B 143 0
SHEET 2 AA5 2 LYS B 161 PRO B 163 -1 O THR B 162 N LEU B 142
SHEET 1 AA6 2 ALA B 188 SER B 193 0
SHEET 2 AA6 2 LYS B 216 LEU B 221 1 O LYS B 217 N LEU B 190
SHEET 1 AA7 5 PHE C 14 PHE C 16 0
SHEET 2 AA7 5 THR C 49 GLY C 52 -1 O VAL C 50 N PHE C 16
SHEET 3 AA7 5 ILE C 21 LEU C 26 1 N ILE C 23 O THR C 49
SHEET 4 AA7 5 THR C 90 LEU C 96 1 O THR C 90 N GLY C 22
SHEET 5 AA7 5 GLY C 115 ILE C 119 1 O ILE C 119 N GLY C 95
SHEET 1 AA8 2 PHE C 141 ASP C 143 0
SHEET 2 AA8 2 LYS C 161 PRO C 163 -1 O THR C 162 N LEU C 142
SHEET 1 AA9 2 ALA C 188 SER C 193 0
SHEET 2 AA9 2 LYS C 216 LEU C 221 1 O LYS C 217 N LEU C 190
SHEET 1 AB1 5 PHE D 14 PHE D 16 0
SHEET 2 AB1 5 THR D 49 GLY D 52 -1 O VAL D 50 N PHE D 16
SHEET 3 AB1 5 ILE D 21 LEU D 26 1 N VAL D 25 O CYS D 51
SHEET 4 AB1 5 THR D 90 LEU D 96 1 O PHE D 92 N LEU D 24
SHEET 5 AB1 5 GLY D 115 ILE D 119 1 O ILE D 119 N GLY D 95
SHEET 1 AB2 2 PHE D 141 ASP D 143 0
SHEET 2 AB2 2 LYS D 161 PRO D 163 -1 O THR D 162 N LEU D 142
SHEET 1 AB3 2 ALA D 188 SER D 193 0
SHEET 2 AB3 2 LYS D 216 LEU D 221 1 O LYS D 217 N LEU D 190
SHEET 1 AB4 5 PHE E 14 PHE E 16 0
SHEET 2 AB4 5 THR E 49 GLY E 52 -1 O VAL E 50 N PHE E 16
SHEET 3 AB4 5 ILE E 21 LEU E 26 1 N ILE E 23 O CYS E 51
SHEET 4 AB4 5 THR E 90 LEU E 96 1 O THR E 90 N GLY E 22
SHEET 5 AB4 5 GLY E 115 ILE E 119 1 O ILE E 119 N GLY E 95
SHEET 1 AB5 2 PHE E 141 ASP E 143 0
SHEET 2 AB5 2 LYS E 161 PRO E 163 -1 O THR E 162 N LEU E 142
SHEET 1 AB6 2 ALA E 188 SER E 193 0
SHEET 2 AB6 2 LYS E 216 LEU E 221 1 O LEU E 221 N CYS E 192
SHEET 1 AB7 5 PHE F 14 PHE F 16 0
SHEET 2 AB7 5 THR F 49 GLY F 52 -1 O VAL F 50 N PHE F 16
SHEET 3 AB7 5 ILE F 21 LEU F 26 1 N VAL F 25 O CYS F 51
SHEET 4 AB7 5 THR F 90 LEU F 96 1 O THR F 90 N GLY F 22
SHEET 5 AB7 5 GLY F 115 ILE F 119 1 O ILE F 119 N GLY F 95
SHEET 1 AB8 2 PHE F 141 ASP F 143 0
SHEET 2 AB8 2 LYS F 161 PRO F 163 -1 O THR F 162 N LEU F 142
SHEET 1 AB9 2 ALA F 188 SER F 193 0
SHEET 2 AB9 2 LYS F 216 LEU F 221 1 O VAL F 219 N LEU F 190
CISPEP 1 ILE A 145 GLY A 146 0 -19.54
CISPEP 2 ALA E 133 GLY E 134 0 -8.56
CISPEP 3 ILE E 145 GLY E 146 0 -7.21
CISPEP 4 ILE F 145 GLY F 146 0 -3.29
CISPEP 5 HIS F 252 HIS F 253 0 27.05
CRYST1 43.091 136.207 126.525 90.00 92.06 90.00 P 1 21 1 12
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 0.023207 0.000000 0.000836 0.00000
SCALE2 0.000000 0.007342 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007909 0.00000
TER 1949 HIS A 252
TER 3888 ARG B 251
TER 5837 HIS C 252
TER 7776 ARG D 251
TER 9715 ARG E 251
TER 11674 HIS F 253
MASTER 400 0 0 66 54 0 0 612313 6 0 120
END |