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HEADER HYDROLASE 11-AUG-23 8TSE
TITLE CRYSTAL STRUCTURE OF A CE15 GLUCURONOYL ESTERASE FROM RUMINOCOCCUS
TITLE 2 FLAVEFACIENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDOMAIN ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CE15 GLUCURONOYL ESTERASE DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: C-TERMINAL HIS-TAGGED CONSTRUCT OF CE15 DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RUMINOCOCCUS FLAVEFACIENS 17;
SOURCE 3 ORGANISM_TAXID: 1030842;
SOURCE 4 GENE: CESA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CARBOHYDRATE, ESTERASE, CE15, GLUCURONOYL ESTERASE, RUMEN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.GRUNINGER,D.R.JONES
REVDAT 1 28-AUG-24 8TSE 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. 1.25 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) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 110185
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5507
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 47.9710 - 3.8834 1.00 3765 198 0.1450 0.1699
REMARK 3 2 3.8834 - 3.0825 1.00 3587 188 0.1629 0.1855
REMARK 3 3 3.0825 - 2.6929 1.00 3592 190 0.1729 0.1949
REMARK 3 4 2.6929 - 2.4467 1.00 3523 185 0.1723 0.1936
REMARK 3 5 2.4467 - 2.2713 1.00 3526 185 0.1691 0.1854
REMARK 3 6 2.2713 - 2.1374 1.00 3520 186 0.1632 0.1853
REMARK 3 7 2.1374 - 2.0304 1.00 3492 184 0.1616 0.1671
REMARK 3 8 2.0304 - 1.9420 1.00 3516 185 0.1631 0.1967
REMARK 3 9 1.9420 - 1.8672 1.00 3486 183 0.1607 0.1723
REMARK 3 10 1.8672 - 1.8028 1.00 3485 184 0.1551 0.1631
REMARK 3 11 1.8028 - 1.7464 1.00 3474 182 0.1565 0.1800
REMARK 3 12 1.7464 - 1.6965 1.00 3490 184 0.1568 0.1699
REMARK 3 13 1.6965 - 1.6518 1.00 3476 183 0.1526 0.1777
REMARK 3 14 1.6518 - 1.6115 1.00 3470 183 0.1530 0.1687
REMARK 3 15 1.6115 - 1.5749 1.00 3456 182 0.1584 0.1820
REMARK 3 16 1.5749 - 1.5414 1.00 3472 182 0.1611 0.1846
REMARK 3 17 1.5414 - 1.5105 1.00 3482 183 0.1689 0.2101
REMARK 3 18 1.5105 - 1.4820 1.00 3420 181 0.1820 0.2202
REMARK 3 19 1.4820 - 1.4556 1.00 3481 183 0.1958 0.1972
REMARK 3 20 1.4556 - 1.4309 1.00 3492 184 0.1982 0.2194
REMARK 3 21 1.4309 - 1.4078 1.00 3444 181 0.2046 0.2368
REMARK 3 22 1.4078 - 1.3861 1.00 3447 181 0.2139 0.2356
REMARK 3 23 1.3861 - 1.3658 1.00 3456 182 0.2178 0.2119
REMARK 3 24 1.3658 - 1.3465 1.00 3473 183 0.2197 0.2356
REMARK 3 25 1.3465 - 1.3283 1.00 3416 180 0.2276 0.2415
REMARK 3 26 1.3283 - 1.3111 1.00 3462 182 0.2302 0.2561
REMARK 3 27 1.3111 - 1.2947 1.00 3453 181 0.2325 0.2391
REMARK 3 28 1.2947 - 1.2791 1.00 3470 183 0.2578 0.2711
REMARK 3 29 1.2791 - 1.2642 1.00 3411 178 0.2502 0.2484
REMARK 3 30 1.2642 - 1.2500 1.00 3441 181 0.2659 0.2910
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.60
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 : 0.005 3332
REMARK 3 ANGLE : 0.813 4534
REMARK 3 CHIRALITY : 0.079 465
REMARK 3 PLANARITY : 0.005 589
REMARK 3 DIHEDRAL : 3.049 1874
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 8TSE 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_1000276552.
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 : SINGLE 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 : 110196
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 47.971
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.08816
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.22
REMARK 200 R MERGE FOR SHELL (I) : 0.29400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% ISOPROPANOL, 20% PEG4000, 100 MM
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 25.97500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.49500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.43500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.49500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.97500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.43500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 365
REMARK 465 LYS A 775
REMARK 465 VAL A 776
REMARK 465 PRO A 777
REMARK 465 ALA A 778
REMARK 465 PHE A 779
REMARK 465 LEU A 780
REMARK 465 TYR A 781
REMARK 465 LYS A 782
REMARK 465 VAL A 783
REMARK 465 VAL A 784
REMARK 465 ILE A 785
REMARK 465 MET A 786
REMARK 465 HIS A 787
REMARK 465 HIS A 788
REMARK 465 HIS A 789
REMARK 465 HIS A 790
REMARK 465 HIS A 791
REMARK 465 HIS A 792
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 SER A 366 OG
REMARK 470 ASN A 368 CG OD1 ND2
REMARK 470 LYS A 376 CD CE NZ
REMARK 470 LYS A 379 CD CE NZ
REMARK 470 LYS A 401 NZ
REMARK 470 LYS A 446 CD CE NZ
REMARK 470 GLU A 463 CD OE1 OE2
REMARK 470 ARG A 521 CD NE CZ NH1 NH2
REMARK 470 LYS A 550 CD CE NZ
REMARK 470 LYS A 620 CE NZ
REMARK 470 LYS A 738 CG CD CE NZ
REMARK 470 LYS A 755 CE NZ
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 O1 GOL A 801 O HOH A 901 1.99
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 MET A 414 -53.78 -136.05
REMARK 500 MET A 496 -84.15 -155.37
REMARK 500 SER A 565 -120.44 64.88
REMARK 500 SER A 616 86.92 -155.32
REMARK 500 LYS A 620 -154.49 -86.73
REMARK 500 LYS A 620 -152.89 -86.73
REMARK 500 GLU A 677 54.02 -148.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8TSE A 366 768 UNP Q9RLB8 CESA_RUMFL 366 768
SEQADV 8TSE MET A 365 UNP Q9RLB8 INITIATING METHIONINE
SEQADV 8TSE ASP A 769 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE PRO A 770 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE ALA A 771 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE PHE A 772 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE LEU A 773 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE TYR A 774 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE LYS A 775 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE VAL A 776 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE PRO A 777 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE ALA A 778 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE PHE A 779 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE LEU A 780 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE TYR A 781 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE LYS A 782 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE VAL A 783 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE VAL A 784 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE ILE A 785 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE MET A 786 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE HIS A 787 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE HIS A 788 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE HIS A 789 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE HIS A 790 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE HIS A 791 UNP Q9RLB8 EXPRESSION TAG
SEQADV 8TSE HIS A 792 UNP Q9RLB8 EXPRESSION TAG
SEQRES 1 A 428 MET SER TYR ASN PHE PRO ALA VAL ASN GLN LEU LYS SER
SEQRES 2 A 428 SER LYS ASP ILE PRO ASP PRO PHE ILE PHE MET ASP GLY
SEQRES 3 A 428 SER LYS VAL GLU SER THR ASP ASP TRP TRP LYS ARG GLN
SEQRES 4 A 428 SER GLU ILE SER CYS MET TYR GLU TYR TYR MET TYR GLY
SEQRES 5 A 428 LYS TRP ILE ASP GLY SER ASP ASP GLU THR THR TYR SER
SEQRES 6 A 428 ILE SER GLY ASN SER MET THR ILE ASN VAL LYS ARG LYS
SEQRES 7 A 428 SER THR GLY LYS THR ALA SER PHE LYS ALA VAL ILE ASN
SEQRES 8 A 428 LEU PRO LYS ASN VAL ARG HIS GLU GLY GLY ALA PRO VAL
SEQRES 9 A 428 ILE LEU GLY MET HIS LYS GLY ILE SER GLU SER THR ALA
SEQRES 10 A 428 THR SER ASN GLY TYR ALA VAL ILE THR TYR ASP SER ASP
SEQRES 11 A 428 GLY MET PHE SER ALA PRO GLY THR ALA GLN ASP ASN ASN
SEQRES 12 A 428 GLN HIS LYS GLY ALA PHE TYR ASP LEU TYR PRO TYR GLY
SEQRES 13 A 428 ARG ASN TRP ASP GLU GLN THR GLY ASP LEU MET ALA TRP
SEQRES 14 A 428 SER TRP GLY ILE SER ARG ILE LEU ASP ALA LEU TYR ASN
SEQRES 15 A 428 GLY ALA ALA LYS GLU LEU ASN ILE ASN PRO ASP SER SER
SEQRES 16 A 428 ILE VAL THR GLY VAL SER ARG TYR GLY LYS ALA ALA SER
SEQRES 17 A 428 VAL CYS GLY ALA PHE ASP THR ARG ILE LYS MET CYS ALA
SEQRES 18 A 428 PRO SER CYS SER GLY ALA GLY GLY LEU ALA LEU TYR ARG
SEQRES 19 A 428 TYR SER SER VAL GLY LYS THR TYR ASP PHE SER SER LYS
SEQRES 20 A 428 GLY GLY SER SER SER TYR THR TYR LYS GLU ASN GLU PRO
SEQRES 21 A 428 LEU GLY SER LEU GLN ALA SER GLY GLU GLN GLY TRP PHE
SEQRES 22 A 428 ASN GLY ARG PHE MET GLU PHE ARG ASN ALA GLU GLN PHE
SEQRES 23 A 428 PRO MET ASP GLN HIS MET LEU GLY ALA LEU CYS CYS ASP
SEQRES 24 A 428 PRO ASP ARG TYR LEU PHE ILE ILE GLY SER CYS GLU SER
SEQRES 25 A 428 GLU ASP TRP VAL ASN ALA PRO SER VAL TRP MET ALA TYR
SEQRES 26 A 428 LEU GLY MET LYS HIS VAL TRP ASP TYR VAL GLY ILE SER
SEQRES 27 A 428 ASP HIS LEU ALA ILE ASN ILE HIS LYS SER GLY HIS ALA
SEQRES 28 A 428 VAL ILE ALA GLU ASP ILE GLU LYS MET VAL GLN TYR PHE
SEQRES 29 A 428 ASP TYR HIS VAL TYR GLY ILE GLN PRO LYS MET ASN LEU
SEQRES 30 A 428 GLU GLU LEU GLN THR SER VAL PHE ALA LEU PRO LYS ASN
SEQRES 31 A 428 LYS ASP SER PHE ALA ASP THR PHE ALA SER LYS TRP LEU
SEQRES 32 A 428 TYR ASP PRO ALA PHE LEU TYR LYS VAL PRO ALA PHE LEU
SEQRES 33 A 428 TYR LYS VAL VAL ILE MET HIS HIS HIS HIS HIS HIS
HET GOL A 801 6
HET GOL A 802 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 HOH *335(H2 O)
HELIX 1 AA1 ALA A 371 LEU A 375 5 5
HELIX 2 AA2 SER A 395 MET A 414 1 20
HELIX 3 AA3 SER A 477 ASN A 484 1 8
HELIX 4 AA4 GLY A 511 TYR A 517 1 7
HELIX 5 AA5 ASN A 522 GLN A 526 5 5
HELIX 6 AA6 GLY A 528 ASN A 546 1 19
HELIX 7 AA7 GLY A 547 ASN A 553 1 7
HELIX 8 AA8 SER A 565 ASP A 578 1 14
HELIX 9 AA9 PHE A 608 GLY A 612 5 5
HELIX 10 AB1 PRO A 624 GLN A 629 1 6
HELIX 11 AB2 GLU A 633 PHE A 637 5 5
HELIX 12 AB3 GLY A 639 PHE A 644 5 6
HELIX 13 AB4 ASN A 646 PHE A 650 5 5
HELIX 14 AB5 ASP A 653 LEU A 660 1 8
HELIX 15 AB6 GLU A 677 VAL A 680 5 4
HELIX 16 AB7 ASN A 681 GLY A 700 1 20
HELIX 17 AB8 ILE A 701 ASP A 703 5 3
HELIX 18 AB9 ILE A 717 GLY A 734 1 18
HELIX 19 AC1 ASN A 740 THR A 746 5 7
HELIX 20 AC2 SER A 747 ASP A 756 5 10
HELIX 21 AC3 SER A 757 PHE A 762 1 6
SHEET 1 AA1 9 ASP A 424 SER A 431 0
SHEET 2 AA1 9 SER A 434 ARG A 441 -1 O ASN A 438 N THR A 427
SHEET 3 AA1 9 THR A 447 ASN A 455 -1 O PHE A 450 N ILE A 437
SHEET 4 AA1 9 ALA A 487 TYR A 491 -1 O THR A 490 N VAL A 453
SHEET 5 AA1 9 ALA A 466 GLY A 471 1 N PRO A 467 O ALA A 487
SHEET 6 AA1 9 ILE A 554 VAL A 564 1 O ILE A 560 N LEU A 470
SHEET 7 AA1 9 MET A 583 SER A 587 1 O ALA A 585 N VAL A 561
SHEET 8 AA1 9 TYR A 667 SER A 673 1 O PHE A 669 N CYS A 584
SHEET 9 AA1 9 LEU A 705 HIS A 710 1 O ASN A 708 N ILE A 670
SHEET 1 AA2 2 THR A 605 TYR A 606 0
SHEET 2 AA2 2 TYR A 617 THR A 618 -1 O TYR A 617 N TYR A 606
CRYST1 51.950 60.870 124.990 90.00 90.00 90.00 P 21 21 21 4
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 0.019249 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016428 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008001 0.00000
TER 3223 TYR A 774
MASTER 294 0 2 21 11 0 0 6 3528 1 12 33
END |