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HEADER HYDROLASE 10-AUG-23 8TRX
TITLE CRYSTAL STRUCTURE OF A CE15 GLUCURONOYL ESTERASE FROM PIROMYCES
TITLE 2 RHIZINFLATUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CE15 GLUCURONOYL ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: N-TERMINAL HIS-TAGGED CONSTRUCT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PIROMYCES RHIZINFLATUS;
SOURCE 3 ORGANISM_TAXID: 73428;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CARBOHYDRATE, ESTERASE, GLUCURONYL ESTERASE, RUMEN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.GRUNINGER,D.R.JONES
REVDAT 1 28-AUG-24 8TRX 0
JRNL AUTH R.J.GRUNINGER,M.KEVORKOVA,K.E.LOW,D.R.JONES,L.WORRALL,
JRNL AUTH 2 T.A.MCALLISTER,D.W.ABBOTT
JRNL TITL STRUCTURAL, BIOCHEMICAL, AND PHYLOGENETIC ANALYSIS OF
JRNL TITL 2 BACTERIAL AND FUNGAL CARBOHYDRATE ESTERASE FAMILY 15
JRNL TITL 3 GLUCURONOYL ESTERASES IN THE RUMEN.
JRNL REF PROTEIN J. 2024
JRNL REFN ISSN 1572-3887
JRNL PMID 39153129
JRNL DOI 10.1007/S10930-024-10221-0
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45939
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2296
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 46.7450 - 6.3954 1.00 2776 146 0.2132 0.2462
REMARK 3 2 6.3954 - 5.0782 1.00 2750 145 0.2139 0.2186
REMARK 3 3 5.0782 - 4.4369 1.00 2743 144 0.1901 0.2320
REMARK 3 4 4.4369 - 4.0314 1.00 2738 144 0.1929 0.2437
REMARK 3 5 4.0314 - 3.7426 1.00 2737 144 0.2093 0.2798
REMARK 3 6 3.7426 - 3.5220 1.00 2713 143 0.2374 0.2556
REMARK 3 7 3.5220 - 3.3457 1.00 2730 143 0.2475 0.2873
REMARK 3 8 3.3457 - 3.2001 1.00 2725 143 0.2606 0.2972
REMARK 3 9 3.2001 - 3.0769 1.00 2716 143 0.2744 0.3329
REMARK 3 10 3.0769 - 2.9708 1.00 2725 144 0.2888 0.3768
REMARK 3 11 2.9708 - 2.8779 1.00 2715 142 0.2897 0.3444
REMARK 3 12 2.8779 - 2.7956 1.00 2708 143 0.2802 0.2897
REMARK 3 13 2.7956 - 2.7221 1.00 2737 144 0.2780 0.3213
REMARK 3 14 2.7221 - 2.6556 1.00 2713 143 0.2691 0.3262
REMARK 3 15 2.6556 - 2.5953 1.00 2714 143 0.2805 0.3348
REMARK 3 16 2.5953 - 2.5401 1.00 2703 142 0.2843 0.3450
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.89
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 : 0.010 5998
REMARK 3 ANGLE : 1.083 8176
REMARK 3 CHIRALITY : 0.061 865
REMARK 3 PLANARITY : 0.007 1082
REMARK 3 DIHEDRAL : 3.106 4135
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 8TRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1000276543.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00334
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45952
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 46.745
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.08133
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.0300
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) : 2.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.57
REMARK 200 R MERGE FOR SHELL (I) : 0.82000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.760
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG10000, 100 MM HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.94333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.88667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.91500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 104.85833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 20.97167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 ILE A 11
REMARK 465 THR A 12
REMARK 465 SER A 13
REMARK 465 LEU A 14
REMARK 465 TYR A 15
REMARK 465 LYS A 16
REMARK 465 LYS A 17
REMARK 465 ALA A 18
REMARK 465 GLY A 19
REMARK 465 MET A 20
REMARK 465 ALA A 21
REMARK 465 SER A 409
REMARK 465 THR A 410
REMARK 465 THR A 411
REMARK 465 THR A 412
REMARK 465 THR A 413
REMARK 465 PRO A 414
REMARK 465 GLU A 415
REMARK 465 ASP A 416
REMARK 465 PRO A 417
REMARK 465 ALA A 418
REMARK 465 PHE A 419
REMARK 465 LEU A 420
REMARK 465 TYR A 421
REMARK 465 LYS A 422
REMARK 465 VAL A 423
REMARK 465 MET B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 ILE B 11
REMARK 465 THR B 12
REMARK 465 SER B 13
REMARK 465 LEU B 14
REMARK 465 TYR B 15
REMARK 465 LYS B 16
REMARK 465 LYS B 17
REMARK 465 ALA B 18
REMARK 465 GLY B 19
REMARK 465 MET B 20
REMARK 465 ALA B 21
REMARK 465 GLU B 22
REMARK 465 SER B 409
REMARK 465 THR B 410
REMARK 465 THR B 411
REMARK 465 THR B 412
REMARK 465 THR B 413
REMARK 465 PRO B 414
REMARK 465 GLU B 415
REMARK 465 ASP B 416
REMARK 465 PRO B 417
REMARK 465 ALA B 418
REMARK 465 PHE B 419
REMARK 465 LEU B 420
REMARK 465 TYR B 421
REMARK 465 LYS B 422
REMARK 465 VAL B 423
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 GLU A 22 CG CD OE1 OE2
REMARK 470 GLU A 34 CG CD OE1 OE2
REMARK 470 LYS A 37 NZ
REMARK 470 GLN A 43 OE1 NE2
REMARK 470 LYS A 90 NZ
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 LYS A 123 CD CE NZ
REMARK 470 LYS A 181 CE NZ
REMARK 470 ASN A 266 CG OD1 ND2
REMARK 470 LYS A 292 CE NZ
REMARK 470 GLU A 318 CG CD OE1 OE2
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 LYS A 368 CE NZ
REMARK 470 ASN A 394 OD1 ND2
REMARK 470 LYS A 401 CG CD CE NZ
REMARK 470 SER A 408 OG
REMARK 470 GLU B 34 CG CD OE1 OE2
REMARK 470 LYS B 37 CG CD CE NZ
REMARK 470 SER B 46 OG
REMARK 470 SER B 49 OG
REMARK 470 VAL B 50 CG1 CG2
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 GLU B 58 CG CD OE1 OE2
REMARK 470 LYS B 67 CG CD CE NZ
REMARK 470 LYS B 90 NZ
REMARK 470 LYS B 99 CG CD CE NZ
REMARK 470 LYS B 123 CD CE NZ
REMARK 470 VAL B 126 CG1 CG2
REMARK 470 SER B 128 OG
REMARK 470 SER B 130 OG
REMARK 470 SER B 152 OG
REMARK 470 GLN B 172 CG CD OE1 NE2
REMARK 470 LYS B 181 CE NZ
REMARK 470 LYS B 292 CG CD CE NZ
REMARK 470 LYS B 323 CG CD CE NZ
REMARK 470 LYS B 337 CE NZ
REMARK 470 LYS B 368 CG CD CE NZ
REMARK 470 LYS B 377 CE NZ
REMARK 470 VAL B 379 CG1 CG2
REMARK 470 SER B 382 OG
REMARK 470 ASN B 394 CG OD1 ND2
REMARK 470 SER B 395 OG
REMARK 470 LYS B 401 CE NZ
REMARK 470 SER B 408 OG
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 VAL B 66 OH TYR B 403 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY B 171 C - N - CA ANGL. DEV. = -14.7 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 THR A 143 6.55 53.96
REMARK 500 CYS A 164 -60.80 -107.29
REMARK 500 SER A 226 -120.86 68.79
REMARK 500 TYR A 275 45.43 -107.07
REMARK 500 LYS A 289 54.40 -152.63
REMARK 500 ASN A 314 84.70 -154.42
REMARK 500 MET A 384 71.35 -110.13
REMARK 500 LYS A 401 147.50 -177.11
REMARK 500 THR A 407 51.01 -104.49
REMARK 500 GLU B 34 2.73 -63.75
REMARK 500 PRO B 48 -179.40 -61.13
REMARK 500 SER B 49 56.72 -118.12
REMARK 500 VAL B 50 104.71 -57.72
REMARK 500 SER B 63 54.86 -95.23
REMARK 500 SER B 141 157.16 179.99
REMARK 500 THR B 143 13.61 58.06
REMARK 500 SER B 226 -119.74 65.88
REMARK 500 LYS B 269 -169.81 -128.90
REMARK 500 LYS B 289 39.00 -78.72
REMARK 500 PRO B 294 1.92 -63.88
REMARK 500 ASN B 314 89.45 -168.80
REMARK 500 ASN B 348 96.45 -163.19
REMARK 500 SER B 387 118.22 -176.47
REMARK 500 SER B 388 31.49 -80.27
REMARK 500 ASP B 392 82.39 -69.53
REMARK 500 ALA B 398 -54.93 -137.29
REMARK 500 TRP B 400 19.21 -147.94
REMARK 500 THR B 407 58.82 -100.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8TRX A 4 423 PDB 8TRX 8TRX 4 423
DBREF 8TRX B 4 423 PDB 8TRX 8TRX 4 423
SEQRES 1 A 420 MET HIS HIS HIS HIS HIS HIS ILE THR SER LEU TYR LYS
SEQRES 2 A 420 LYS ALA GLY MET ALA GLU VAL PRO LEU VAL TYR PRO LYS
SEQRES 3 A 420 GLU ASN MET GLY GLU SER CYS LYS ALA PRO THR LEU PRO
SEQRES 4 A 420 GLN PRO ALA SER CYS PRO SER VAL PRO LYS LEU PRO ASP
SEQRES 5 A 420 PRO PHE GLU TRP SER ASP GLY SER GLY ARG VAL LYS ASN
SEQRES 6 A 420 LEU ALA ASP TRP GLU CYS ARG ARG ASN GLU ILE LYS ALA
SEQRES 7 A 420 GLU ILE GLU ASN TYR GLU LEU GLY LYS LYS PRO ALA PRO
SEQRES 8 A 420 PRO GLN SER LEU LYS ALA THR TYR SER GLY GLY THR LEU
SEQRES 9 A 420 THR VAL VAL VAL ASN ASP ASN GLY GLY SER LEU THR LEU
SEQRES 10 A 420 THR SER LYS ILE SER VAL PRO SER GLY SER GLY PRO PHE
SEQRES 11 A 420 PRO VAL ILE ILE GLY MET ASN SER ASN THR GLY SER LEU
SEQRES 12 A 420 SER ALA GLY GLN PHE SER ASP PHE ILE GLN VAL PRO PHE
SEQRES 13 A 420 ASN HIS ASP GLN CYS ALA GLN TYR SER MET THR GLY GLN
SEQRES 14 A 420 LYS ASN THR ASN ALA PRO PHE TYR LYS LEU TYR PRO ASN
SEQRES 15 A 420 LEU ARG ASP ALA GLY ASP TYR ILE ALA TRP SER TRP GLY
SEQRES 16 A 420 ILE SER ARG LEU ILE ASP GLY ILE GLU GLN VAL LYS ASP
SEQRES 17 A 420 GLN ILE HIS ALA ASP MET ASN HIS ILE GLY VAL THR GLY
SEQRES 18 A 420 CYS SER TYR ALA GLY LYS MET ALA LEU PHE GLY GLY ALA
SEQRES 19 A 420 PHE ASP GLU ARG VAL ALA LEU THR ILE PRO GLN GLU SER
SEQRES 20 A 420 GLY GLY GLY GLY ILE ASN ALA TRP ARG VAL SER ASP THR
SEQRES 21 A 420 ILE GLY ASN VAL GLU LYS ILE ASP ASN THR ASN TYR SER
SEQRES 22 A 420 TRP PHE MET GLN ALA LEU LYS ASN ASN PHE ASN GLY LYS
SEQRES 23 A 420 SER ASP LYS LEU PRO TYR ASP HIS HIS GLU LEU ILE ALA
SEQRES 24 A 420 MET VAL ALA PRO ARG ALA PHE PHE THR MET GLY ASN PRO
SEQRES 25 A 420 ASP TYR GLU TRP LEU GLY ASP LYS SER GLY TYR THR SER
SEQRES 26 A 420 ALA MET ALA ALA LEU GLU VAL TRP LYS ALA MET GLY VAL
SEQRES 27 A 420 GLU ASP ARG PHE GLY PHE ASN PHE VAL GLY GLY HIS MET
SEQRES 28 A 420 HIS CYS SER ALA ALA GLY THR GLN VAL ASN ASP VAL ASN
SEQRES 29 A 420 LYS PHE ILE ASP ARG PHE LEU ARG GLY LYS SER VAL SER
SEQRES 30 A 420 THR SER ASN MET LEU SER SER SER VAL THR ASN ASP TYR
SEQRES 31 A 420 ASN SER TRP ILE ALA ALA TRP LYS GLY TYR THR ILE ASP
SEQRES 32 A 420 THR SER SER THR THR THR THR PRO GLU ASP PRO ALA PHE
SEQRES 33 A 420 LEU TYR LYS VAL
SEQRES 1 B 420 MET HIS HIS HIS HIS HIS HIS ILE THR SER LEU TYR LYS
SEQRES 2 B 420 LYS ALA GLY MET ALA GLU VAL PRO LEU VAL TYR PRO LYS
SEQRES 3 B 420 GLU ASN MET GLY GLU SER CYS LYS ALA PRO THR LEU PRO
SEQRES 4 B 420 GLN PRO ALA SER CYS PRO SER VAL PRO LYS LEU PRO ASP
SEQRES 5 B 420 PRO PHE GLU TRP SER ASP GLY SER GLY ARG VAL LYS ASN
SEQRES 6 B 420 LEU ALA ASP TRP GLU CYS ARG ARG ASN GLU ILE LYS ALA
SEQRES 7 B 420 GLU ILE GLU ASN TYR GLU LEU GLY LYS LYS PRO ALA PRO
SEQRES 8 B 420 PRO GLN SER LEU LYS ALA THR TYR SER GLY GLY THR LEU
SEQRES 9 B 420 THR VAL VAL VAL ASN ASP ASN GLY GLY SER LEU THR LEU
SEQRES 10 B 420 THR SER LYS ILE SER VAL PRO SER GLY SER GLY PRO PHE
SEQRES 11 B 420 PRO VAL ILE ILE GLY MET ASN SER ASN THR GLY SER LEU
SEQRES 12 B 420 SER ALA GLY GLN PHE SER ASP PHE ILE GLN VAL PRO PHE
SEQRES 13 B 420 ASN HIS ASP GLN CYS ALA GLN TYR SER MET THR GLY GLN
SEQRES 14 B 420 LYS ASN THR ASN ALA PRO PHE TYR LYS LEU TYR PRO ASN
SEQRES 15 B 420 LEU ARG ASP ALA GLY ASP TYR ILE ALA TRP SER TRP GLY
SEQRES 16 B 420 ILE SER ARG LEU ILE ASP GLY ILE GLU GLN VAL LYS ASP
SEQRES 17 B 420 GLN ILE HIS ALA ASP MET ASN HIS ILE GLY VAL THR GLY
SEQRES 18 B 420 CYS SER TYR ALA GLY LYS MET ALA LEU PHE GLY GLY ALA
SEQRES 19 B 420 PHE ASP GLU ARG VAL ALA LEU THR ILE PRO GLN GLU SER
SEQRES 20 B 420 GLY GLY GLY GLY ILE ASN ALA TRP ARG VAL SER ASP THR
SEQRES 21 B 420 ILE GLY ASN VAL GLU LYS ILE ASP ASN THR ASN TYR SER
SEQRES 22 B 420 TRP PHE MET GLN ALA LEU LYS ASN ASN PHE ASN GLY LYS
SEQRES 23 B 420 SER ASP LYS LEU PRO TYR ASP HIS HIS GLU LEU ILE ALA
SEQRES 24 B 420 MET VAL ALA PRO ARG ALA PHE PHE THR MET GLY ASN PRO
SEQRES 25 B 420 ASP TYR GLU TRP LEU GLY ASP LYS SER GLY TYR THR SER
SEQRES 26 B 420 ALA MET ALA ALA LEU GLU VAL TRP LYS ALA MET GLY VAL
SEQRES 27 B 420 GLU ASP ARG PHE GLY PHE ASN PHE VAL GLY GLY HIS MET
SEQRES 28 B 420 HIS CYS SER ALA ALA GLY THR GLN VAL ASN ASP VAL ASN
SEQRES 29 B 420 LYS PHE ILE ASP ARG PHE LEU ARG GLY LYS SER VAL SER
SEQRES 30 B 420 THR SER ASN MET LEU SER SER SER VAL THR ASN ASP TYR
SEQRES 31 B 420 ASN SER TRP ILE ALA ALA TRP LYS GLY TYR THR ILE ASP
SEQRES 32 B 420 THR SER SER THR THR THR THR PRO GLU ASP PRO ALA PHE
SEQRES 33 B 420 LEU TYR LYS VAL
FORMUL 3 HOH *83(H2 O)
HELIX 1 AA1 GLN A 43 CYS A 47 5 5
HELIX 2 AA2 ASN A 68 GLU A 87 1 20
HELIX 3 AA3 SER A 147 SER A 152 5 6
HELIX 4 AA4 ASN A 160 CYS A 164 5 5
HELIX 5 AA5 ALA A 177 TYR A 183 1 7
HELIX 6 AA6 PRO A 184 ARG A 187 5 4
HELIX 7 AA7 GLY A 190 VAL A 209 1 20
HELIX 8 AA8 VAL A 209 HIS A 214 1 6
HELIX 9 AA9 SER A 226 PHE A 238 1 13
HELIX 10 AB1 ALA A 257 ILE A 264 1 8
HELIX 11 AB2 MET A 279 ASN A 287 1 9
HELIX 12 AB3 LYS A 289 LEU A 293 5 5
HELIX 13 AB4 ASP A 296 MET A 303 1 8
HELIX 14 AB5 TYR A 317 LEU A 320 5 4
HELIX 15 AB6 GLY A 321 MET A 339 1 19
HELIX 16 AB7 VAL A 341 ASP A 343 5 3
HELIX 17 AB8 ALA A 359 LEU A 374 1 16
HELIX 18 AB9 TYR A 393 ALA A 398 1 6
HELIX 19 AC1 ASN B 68 GLU B 87 1 20
HELIX 20 AC2 SER B 147 SER B 152 5 6
HELIX 21 AC3 ASN B 160 CYS B 164 5 5
HELIX 22 AC4 ALA B 177 TYR B 183 1 7
HELIX 23 AC5 PRO B 184 ARG B 187 5 4
HELIX 24 AC6 GLY B 190 VAL B 209 1 20
HELIX 25 AC7 VAL B 209 HIS B 214 1 6
HELIX 26 AC8 SER B 226 ASP B 239 1 14
HELIX 27 AC9 ALA B 257 ILE B 264 1 8
HELIX 28 AD1 MET B 279 ASN B 287 1 9
HELIX 29 AD2 LYS B 289 LEU B 293 5 5
HELIX 30 AD3 ASP B 296 MET B 303 1 8
HELIX 31 AD4 TYR B 317 LEU B 320 5 4
HELIX 32 AD5 GLY B 321 LYS B 337 1 17
HELIX 33 AD6 ALA B 338 GLY B 340 5 3
HELIX 34 AD7 VAL B 341 ASP B 343 5 3
HELIX 35 AD8 ALA B 359 LEU B 374 1 16
HELIX 36 AD9 ASP B 392 ILE B 397 1 6
SHEET 1 AA1 3 SER A 97 SER A 103 0
SHEET 2 AA1 3 THR A 106 ASP A 113 -1 O ASN A 112 N SER A 97
SHEET 3 AA1 3 GLY A 116 LYS A 123 -1 O SER A 122 N LEU A 107
SHEET 1 AA2 7 ILE A 155 PHE A 159 0
SHEET 2 AA2 7 PHE A 133 MET A 139 1 N GLY A 138 O PHE A 159
SHEET 3 AA2 7 ALA A 215 CYS A 225 1 O GLY A 221 N VAL A 135
SHEET 4 AA2 7 LEU A 244 GLN A 248 1 O GLN A 248 N GLY A 224
SHEET 5 AA2 7 ALA A 308 GLY A 313 1 O PHE A 310 N THR A 245
SHEET 6 AA2 7 PHE A 345 PHE A 349 1 O ASN A 348 N GLY A 313
SHEET 7 AA2 7 LEU A 385 SER A 387 1 O SER A 386 N PHE A 349
SHEET 1 AA3 3 SER B 97 SER B 103 0
SHEET 2 AA3 3 THR B 106 ASP B 113 -1 O THR B 108 N THR B 101
SHEET 3 AA3 3 GLY B 116 LYS B 123 -1 O LEU B 118 N VAL B 111
SHEET 1 AA4 7 ILE B 155 PHE B 159 0
SHEET 2 AA4 7 PHE B 133 MET B 139 1 N PRO B 134 O ILE B 155
SHEET 3 AA4 7 ALA B 215 CYS B 225 1 O GLY B 221 N VAL B 135
SHEET 4 AA4 7 LEU B 244 GLN B 248 1 O GLN B 248 N GLY B 224
SHEET 5 AA4 7 ALA B 308 MET B 312 1 O PHE B 310 N THR B 245
SHEET 6 AA4 7 PHE B 345 PHE B 349 1 O GLY B 346 N PHE B 309
SHEET 7 AA4 7 LEU B 385 SER B 387 1 O SER B 386 N PHE B 349
SSBOND 1 CYS A 36 CYS A 74 1555 1555 2.05
SSBOND 2 CYS A 225 CYS A 356 1555 1555 2.05
SSBOND 3 CYS B 36 CYS B 74 1555 1555 2.03
SSBOND 4 CYS B 225 CYS B 356 1555 1555 2.02
CISPEP 1 GLY A 131 PRO A 132 0 4.00
CISPEP 2 ALA A 305 PRO A 306 0 3.04
CISPEP 3 GLY B 131 PRO B 132 0 2.62
CISPEP 4 ALA B 305 PRO B 306 0 2.53
CRYST1 139.680 139.680 125.830 90.00 90.00 120.00 P 61 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 0.007159 0.004133 0.000000 0.00000
SCALE2 0.000000 0.008267 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007947 0.00000
TER 2939 SER A 408
TER 5837 SER B 408
MASTER 415 0 0 36 20 0 0 6 5912 2 8 66
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