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HEADER HYDROLASE 13-MAR-22 7X8L
TITLE MICROBIAL FAMILY VII CARBOXYLESTERASE E93 WILD-TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALTERICROCEIBACTERIUM INDICUM;
SOURCE 3 ORGANISM_TAXID: 374177;
SOURCE 4 GENE: GRI39_13840;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE, CPT11, LIPID METABOLISM, ERYTHROBACTER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LI,R.ZHEN,J.LI,X.XU
REVDAT 1 15-MAR-23 7X8L 0
JRNL AUTH L.YANG,R.ZHEN,L.JIXI,X.XUEWEI
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHT INTO A MARINE MICROBIAL
JRNL TITL 2 CARBOXYLESTERASE E93
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 45341
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.410
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 37.8600 - 4.2600 0.99 3291 153 0.1517 0.1590
REMARK 3 2 4.2600 - 3.3800 1.00 3172 145 0.1478 0.1699
REMARK 3 3 3.3800 - 2.9600 1.00 3123 145 0.1714 0.1829
REMARK 3 4 2.9600 - 2.6900 1.00 3127 144 0.1825 0.1919
REMARK 3 5 2.6900 - 2.4900 1.00 3075 142 0.1785 0.2031
REMARK 3 6 2.4900 - 2.3500 1.00 3101 143 0.1770 0.2042
REMARK 3 7 2.3500 - 2.2300 1.00 3094 142 0.1735 0.2180
REMARK 3 8 2.2300 - 2.1300 1.00 3045 141 0.1632 0.1994
REMARK 3 9 2.1300 - 2.0500 1.00 3080 142 0.1691 0.2275
REMARK 3 10 2.0500 - 1.9800 1.00 3072 142 0.1765 0.1999
REMARK 3 11 1.9800 - 1.9200 0.99 3039 140 0.1786 0.2547
REMARK 3 12 1.9200 - 1.8600 0.99 3036 140 0.1875 0.2227
REMARK 3 13 1.8600 - 1.8100 1.00 3055 142 0.1891 0.2232
REMARK 3 14 1.8100 - 1.7700 0.99 3031 139 0.2125 0.2476
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) : 0.171
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.97
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 : 0.008 4075
REMARK 3 ANGLE : 1.004 5571
REMARK 3 CHIRALITY : 0.058 599
REMARK 3 PLANARITY : 0.008 741
REMARK 3 DIHEDRAL : 5.659 558
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 7X8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-22.
REMARK 100 THE DEPOSITION ID IS D_1300028318.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 293.15
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NFPSS
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.996
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45341
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 37.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : 0.09239
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.68470
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1K4Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 MOL/L BIS-TRIS, PH6.5 28% W/V
REMARK 280 PEG2000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K
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 22.42500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.41000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.83500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.41000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.42500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.83500
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 GLY A 268
REMARK 465 GLY A 269
REMARK 465 PHE A 270
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 14 CG CD OE1 OE2
REMARK 470 ARG A 246 CG CD NE CZ NH1 NH2
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 OG SER A 45 O HOH A 601 2.12
REMARK 500 O HOH A 680 O HOH A 855 2.18
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 LEU A 267 CA - CB - CG ANGL. DEV. = 17.6 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 PHE A 35 18.57 58.27
REMARK 500 GLN A 59 -12.39 -160.28
REMARK 500 LEU A 89 -141.55 -92.20
REMARK 500 LEU A 109 -154.41 73.42
REMARK 500 SER A 110 -179.95 -176.28
REMARK 500 ASN A 137 -123.41 45.35
REMARK 500 SER A 189 -123.89 57.45
REMARK 500 GLU A 266 29.33 -74.17
REMARK 500 VAL A 283 97.72 -69.71
REMARK 500 VAL A 286 -64.75 -122.21
REMARK 500 MET A 411 -106.96 60.08
REMARK 500 HIS A 414 131.60 -39.33
REMARK 500 ALA A 415 -4.56 75.85
REMARK 500 THR A 472 -62.24 -107.48
REMARK 500 THR A 472 -62.24 -92.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7X8L A 1 513 UNP A0A845ADQ8_9SPHN
DBREF2 7X8L A A0A845ADQ8 1 513
SEQADV 7X8L PRO A 0 UNP A0A845ADQ EXPRESSION TAG
SEQRES 1 A 514 PRO MET ALA ARG THR ARG TYR GLY PRO VAL ILE GLY LYS
SEQRES 2 A 514 VAL GLU GLN GLY ALA LEU ALA PHE LYS GLY ILE PRO TYR
SEQRES 3 A 514 GLY ALA PRO THR SER GLY SER GLY ARG PHE MET PRO PRO
SEQRES 4 A 514 THR PRO PRO GLN PRO TRP SER THR PRO LEU ARG ALA PHE
SEQRES 5 A 514 ASP TYR GLY PRO THR ALA PRO GLN SER ASP PRO GLN ASP
SEQRES 6 A 514 ALA LEU GLU SER GLY ALA ALA ASP ALA ARG GLU SER GLU
SEQRES 7 A 514 ASP CYS LEU THR LEU ASN VAL TRP THR PRO SER LEU ASN
SEQRES 8 A 514 ASP GLN ARG LYS ARG PRO VAL MET VAL TRP LEU HIS GLY
SEQRES 9 A 514 GLY GLY LEU TRP ARG LEU SER ALA ALA GLY ASP TYR GLN
SEQRES 10 A 514 ALA GLY THR HIS LEU ALA ALA HIS SER ASP VAL VAL MET
SEQRES 11 A 514 VAL SER PRO ASN HIS ARG LEU ASN VAL LEU ALA HIS ALA
SEQRES 12 A 514 TYR LEU ASP GLU TYR ASP PRO ALA PHE ALA GLY SER SER
SEQRES 13 A 514 SER ALA GLY MET LEU ASP LEU VAL LEU ALA LEU LYS TRP
SEQRES 14 A 514 VAL ARG ASP ASN ILE GLU GLU PHE GLY GLY ASP PRO ASP
SEQRES 15 A 514 ASN VAL THR ILE PHE GLY GLN SER GLY GLY GLY GLN LYS
SEQRES 16 A 514 VAL SER PHE LEU MET ALA MET PRO ALA ALA ALA GLY LEU
SEQRES 17 A 514 PHE HIS LYS ALA ILE ILE GLN SER GLY PRO ALA PRO LEU
SEQRES 18 A 514 ALA LEU GLU LYS PRO TYR ALA ARG GLU LEU SER ALA ARG
SEQRES 19 A 514 LEU LEU THR LEU LEU ASP ILE PRO LYS ASN ARG VAL ARG
SEQRES 20 A 514 ASP ILE GLN ASN VAL PRO LEU ASP ALA ILE MET ARG ALA
SEQRES 21 A 514 TYR TYR GLN ILE PHE GLU GLU LEU GLY GLY PHE GLY VAL
SEQRES 22 A 514 MET GLY VAL ILE GLN ASP PHE ALA PRO VAL VAL ASP ASP
SEQRES 23 A 514 VAL ALA LEU PRO GLN HIS PRO PHE TRP ASN GLY ALA SER
SEQRES 24 A 514 PRO LEU SER ARG ASP VAL PRO LEU MET ILE GLY CYS THR
SEQRES 25 A 514 ARG THR GLU MET THR GLU TYR PHE LEU ALA SER ASN PRO
SEQRES 26 A 514 GLY ALA ALA LYS ARG ASP PHE ALA ALA VAL THR ALA GLN
SEQRES 27 A 514 LEU GLU PRO VAL PHE GLY MET GLN ALA PRO ALA VAL VAL
SEQRES 28 A 514 ALA HIS TYR ARG ALA THR HIS PRO THR ALA SER PRO TRP
SEQRES 29 A 514 GLU VAL ASP ALA LEU ILE ARG SER ASP TRP PRO THR ARG
SEQRES 30 A 514 LEU PHE THR GLN ARG ILE ALA ASP GLU GLN VAL LYS LEU
SEQRES 31 A 514 GLY GLY ALA PRO VAL TRP MET TYR ARG MET ASP TRP GLN
SEQRES 32 A 514 THR THR ALA ARG ASP GLY LEU LEU MET SER PRO HIS ALA
SEQRES 33 A 514 ILE ASP ILE PRO PHE VAL LEU ASP THR VAL GLY THR GLU
SEQRES 34 A 514 PRO VAL GLU PRO GLY GLN LEU ALA GLU GLN GLN ARG MET
SEQRES 35 A 514 MET GLN GLN MET ASN ASN ALA TRP VAL SER PHE ALA ARG
SEQRES 36 A 514 ASN GLY ASN PRO GLN ASN LYS TYR ILE PRO PRO TRP GLN
SEQRES 37 A 514 PRO TYR ASN SER THR SER ARG PRO THR MET ILE PHE ASN
SEQRES 38 A 514 LEU HIS SER HIS MET ALA ASN ASP PRO ASP GLY SER ASP
SEQRES 39 A 514 LEU ALA PHE LEU LYS LYS ASP LEU ALA ASN LEU GLU VAL
SEQRES 40 A 514 VAL ALA GLY GLY VAL THR HIS
FORMUL 2 HOH *274(H2 O)
HELIX 1 AA1 SER A 30 ARG A 34 5 5
HELIX 2 AA2 GLY A 113 ALA A 117 5 5
HELIX 3 AA3 GLY A 118 ASP A 126 1 9
HELIX 4 AA4 LEU A 136 ALA A 142 1 7
HELIX 5 AA5 ASP A 148 ALA A 152 5 5
HELIX 6 AA6 GLY A 153 SER A 155 5 3
HELIX 7 AA7 SER A 156 ILE A 173 1 18
HELIX 8 AA8 GLU A 174 PHE A 176 5 3
HELIX 9 AA9 SER A 189 MET A 199 1 11
HELIX 10 AB1 ALA A 200 ALA A 205 5 6
HELIX 11 AB2 GLU A 223 LEU A 238 1 16
HELIX 12 AB3 PRO A 241 ASN A 250 5 10
HELIX 13 AB4 PRO A 252 GLU A 266 1 15
HELIX 14 AB5 SER A 298 ARG A 302 5 5
HELIX 15 AB6 MET A 315 ASN A 323 1 9
HELIX 16 AB7 GLY A 325 ARG A 329 5 5
HELIX 17 AB8 ASP A 330 GLN A 337 1 8
HELIX 18 AB9 LEU A 338 GLY A 343 1 6
HELIX 19 AC1 GLN A 345 HIS A 357 1 13
HELIX 20 AC2 SER A 361 TRP A 373 1 13
HELIX 21 AC3 PRO A 374 LYS A 388 1 15
HELIX 22 AC4 ALA A 405 LEU A 409 5 5
HELIX 23 AC5 ASP A 417 ASP A 423 1 7
HELIX 24 AC6 GLN A 434 GLY A 456 1 23
HELIX 25 AC7 ASP A 490 ASP A 500 1 11
HELIX 26 AC8 LEU A 501 LEU A 504 5 4
SHEET 1 AA1 3 MET A 1 ALA A 2 0
SHEET 2 AA1 3 VAL A 9 ILE A 10 -1 O VAL A 9 N ALA A 2
SHEET 3 AA1 3 LEU A 48 ARG A 49 1 O LEU A 48 N ILE A 10
SHEET 1 AA211 LYS A 12 GLU A 14 0
SHEET 2 AA211 ALA A 17 PRO A 24 -1 O ALA A 17 N GLU A 14
SHEET 3 AA211 THR A 81 THR A 86 -1 O THR A 86 N LEU A 18
SHEET 4 AA211 VAL A 128 PRO A 132 -1 O MET A 129 N TRP A 85
SHEET 5 AA211 ARG A 95 LEU A 101 1 N MET A 98 O VAL A 128
SHEET 6 AA211 GLY A 178 GLN A 188 1 O THR A 184 N VAL A 99
SHEET 7 AA211 LYS A 210 GLN A 214 1 O LYS A 210 N ILE A 185
SHEET 8 AA211 LEU A 306 THR A 311 1 O MET A 307 N ILE A 213
SHEET 9 AA211 VAL A 394 MET A 399 1 O TRP A 395 N ILE A 308
SHEET 10 AA211 PRO A 475 PHE A 479 1 O MET A 477 N MET A 396
SHEET 11 AA211 HIS A 484 ASN A 487 -1 O HIS A 484 N ILE A 478
CISPEP 1 TRP A 373 PRO A 374 0 0.65
CRYST1 44.850 91.670 110.820 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 0.022297 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010909 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009024 0.00000
TER 3958 HIS A 513
MASTER 280 0 0 26 14 0 0 6 4206 1 0 40
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