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HEADER HYDROLASE 04-OCT-22 8EOR
TITLE LIVER CARBOXYLESTERASE 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ACYL-COENZYME A:CHOLESTEROL ACYLTRANSFERASE,ACAT,BRAIN
COMPND 5 CARBOXYLESTERASE HBR1,CARBOXYLESTERASE 1,CE-1,HCE-1,CHOLESTERYL ESTER
COMPND 6 HYDROLASE,CEH,COCAINE CARBOXYLESTERASE,EGASYN,HMSE,
COMPND 7 METHYLUMBELLIFERYL-ACETATE DEACETYLASE 1,MONOCYTE/MACROPHAGE SERINE
COMPND 8 ESTERASE,RETINYL ESTER HYDROLASE,REH,SERINE ESTERASE 1,
COMPND 9 TRIACYLGLYCEROL HYDROLASE,TGH;
COMPND 10 EC: 3.1.1.1,3.1.1.13,3.1.1.56
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS CARBOXYLESTERASE, HUMAN LIVER, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR Z.ZHANG,E.YU
REVDAT 1 03-MAY-23 8EOR 0
JRNL AUTH Z.ZHANG
JRNL TITL LIVER CARBOXYLESTERASE 1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.670
REMARK 3 NUMBER OF PARTICLES : 210633
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 8EOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1000269129.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : LIVER CARBOXYLESTERASE 1
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 170.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3291.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4125.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 81000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: TRIMERIC
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 MET A 1
REMARK 465 TRP A 2
REMARK 465 LEU A 3
REMARK 465 ARG A 4
REMARK 465 ALA A 5
REMARK 465 PHE A 6
REMARK 465 ILE A 7
REMARK 465 LEU A 8
REMARK 465 ALA A 9
REMARK 465 THR A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 ALA A 13
REMARK 465 SER A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 TRP A 17
REMARK 465 GLY A 18
REMARK 465 HIS A 19
REMARK 465 PRO A 20
REMARK 465 SER A 21
REMARK 465 LYS A 554
REMARK 465 ALA A 555
REMARK 465 VAL A 556
REMARK 465 GLU A 557
REMARK 465 LYS A 558
REMARK 465 PRO A 559
REMARK 465 PRO A 560
REMARK 465 GLN A 561
REMARK 465 THR A 562
REMARK 465 GLU A 563
REMARK 465 HIS A 564
REMARK 465 ILE A 565
REMARK 465 GLU A 566
REMARK 465 LEU A 567
REMARK 465 MET B 1
REMARK 465 TRP B 2
REMARK 465 LEU B 3
REMARK 465 ARG B 4
REMARK 465 ALA B 5
REMARK 465 PHE B 6
REMARK 465 ILE B 7
REMARK 465 LEU B 8
REMARK 465 ALA B 9
REMARK 465 THR B 10
REMARK 465 LEU B 11
REMARK 465 SER B 12
REMARK 465 ALA B 13
REMARK 465 SER B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 TRP B 17
REMARK 465 GLY B 18
REMARK 465 HIS B 19
REMARK 465 PRO B 20
REMARK 465 SER B 21
REMARK 465 LYS B 554
REMARK 465 ALA B 555
REMARK 465 VAL B 556
REMARK 465 GLU B 557
REMARK 465 LYS B 558
REMARK 465 PRO B 559
REMARK 465 PRO B 560
REMARK 465 GLN B 561
REMARK 465 THR B 562
REMARK 465 GLU B 563
REMARK 465 HIS B 564
REMARK 465 ILE B 565
REMARK 465 GLU B 566
REMARK 465 LEU B 567
REMARK 465 MET C 1
REMARK 465 TRP C 2
REMARK 465 LEU C 3
REMARK 465 ARG C 4
REMARK 465 ALA C 5
REMARK 465 PHE C 6
REMARK 465 ILE C 7
REMARK 465 LEU C 8
REMARK 465 ALA C 9
REMARK 465 THR C 10
REMARK 465 LEU C 11
REMARK 465 SER C 12
REMARK 465 ALA C 13
REMARK 465 SER C 14
REMARK 465 ALA C 15
REMARK 465 ALA C 16
REMARK 465 TRP C 17
REMARK 465 GLY C 18
REMARK 465 HIS C 19
REMARK 465 PRO C 20
REMARK 465 SER C 21
REMARK 465 LYS C 554
REMARK 465 ALA C 555
REMARK 465 VAL C 556
REMARK 465 GLU C 557
REMARK 465 LYS C 558
REMARK 465 PRO C 559
REMARK 465 PRO C 560
REMARK 465 GLN C 561
REMARK 465 THR C 562
REMARK 465 GLU C 563
REMARK 465 HIS C 564
REMARK 465 ILE C 565
REMARK 465 GLU C 566
REMARK 465 LEU C 567
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 314 CG CD OE1 OE2
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 GLU C 314 CG CD OE1 OE2
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 177 32.59 -140.79
REMARK 500 SER A 221 -117.43 62.78
REMARK 500 TRP A 357 -52.91 -124.81
REMARK 500 LYS A 462 -1.86 79.27
REMARK 500 LYS A 538 61.88 61.00
REMARK 500 PHE B 177 32.63 -140.52
REMARK 500 SER B 221 -115.75 62.59
REMARK 500 TRP B 357 -52.35 -127.97
REMARK 500 LYS B 462 -2.92 75.03
REMARK 500 LYS B 538 61.38 60.74
REMARK 500 PHE C 177 30.64 -140.22
REMARK 500 SER C 221 -116.52 62.89
REMARK 500 TRP C 357 -53.15 -124.18
REMARK 500 LYS C 462 -1.04 76.63
REMARK 500 LYS C 538 61.79 60.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG D 1
REMARK 610 NAG F 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-23427 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-28465 RELATED DB: EMDB
REMARK 900 LIVER CARBOXYLESTERASE 1
DBREF 8EOR A 1 567 UNP P23141 EST1_HUMAN 1 567
DBREF 8EOR B 1 567 UNP P23141 EST1_HUMAN 1 567
DBREF 8EOR C 1 567 UNP P23141 EST1_HUMAN 1 567
SEQRES 1 A 567 MET TRP LEU ARG ALA PHE ILE LEU ALA THR LEU SER ALA
SEQRES 2 A 567 SER ALA ALA TRP GLY HIS PRO SER SER PRO PRO VAL VAL
SEQRES 3 A 567 ASP THR VAL HIS GLY LYS VAL LEU GLY LYS PHE VAL SER
SEQRES 4 A 567 LEU GLU GLY PHE ALA GLN PRO VAL ALA ILE PHE LEU GLY
SEQRES 5 A 567 ILE PRO PHE ALA LYS PRO PRO LEU GLY PRO LEU ARG PHE
SEQRES 6 A 567 THR PRO PRO GLN PRO ALA GLU PRO TRP SER PHE VAL LYS
SEQRES 7 A 567 ASN ALA THR SER TYR PRO PRO MET CYS THR GLN ASP PRO
SEQRES 8 A 567 LYS ALA GLY GLN LEU LEU SER GLU LEU PHE THR ASN ARG
SEQRES 9 A 567 LYS GLU ASN ILE PRO LEU LYS LEU SER GLU ASP CYS LEU
SEQRES 10 A 567 TYR LEU ASN ILE TYR THR PRO ALA ASP LEU THR LYS LYS
SEQRES 11 A 567 ASN ARG LEU PRO VAL MET VAL TRP ILE HIS GLY GLY GLY
SEQRES 12 A 567 LEU MET VAL GLY ALA ALA SER THR TYR ASP GLY LEU ALA
SEQRES 13 A 567 LEU ALA ALA HIS GLU ASN VAL VAL VAL VAL THR ILE GLN
SEQRES 14 A 567 TYR ARG LEU GLY ILE TRP GLY PHE PHE SER THR GLY ASP
SEQRES 15 A 567 GLU HIS SER ARG GLY ASN TRP GLY HIS LEU ASP GLN VAL
SEQRES 16 A 567 ALA ALA LEU ARG TRP VAL GLN ASP ASN ILE ALA SER PHE
SEQRES 17 A 567 GLY GLY ASN PRO GLY SER VAL THR ILE PHE GLY GLU SER
SEQRES 18 A 567 ALA GLY GLY GLU SER VAL SER VAL LEU VAL LEU SER PRO
SEQRES 19 A 567 LEU ALA LYS ASN LEU PHE HIS ARG ALA ILE SER GLU SER
SEQRES 20 A 567 GLY VAL ALA LEU THR SER VAL LEU VAL LYS LYS GLY ASP
SEQRES 21 A 567 VAL LYS PRO LEU ALA GLU GLN ILE ALA ILE THR ALA GLY
SEQRES 22 A 567 CYS LYS THR THR THR SER ALA VAL MET VAL HIS CYS LEU
SEQRES 23 A 567 ARG GLN LYS THR GLU GLU GLU LEU LEU GLU THR THR LEU
SEQRES 24 A 567 LYS MET LYS PHE LEU SER LEU ASP LEU GLN GLY ASP PRO
SEQRES 25 A 567 ARG GLU SER GLN PRO LEU LEU GLY THR VAL ILE ASP GLY
SEQRES 26 A 567 MET LEU LEU LEU LYS THR PRO GLU GLU LEU GLN ALA GLU
SEQRES 27 A 567 ARG ASN PHE HIS THR VAL PRO TYR MET VAL GLY ILE ASN
SEQRES 28 A 567 LYS GLN GLU PHE GLY TRP LEU ILE PRO MET GLN LEU MET
SEQRES 29 A 567 SER TYR PRO LEU SER GLU GLY GLN LEU ASP GLN LYS THR
SEQRES 30 A 567 ALA MET SER LEU LEU TRP LYS SER TYR PRO LEU VAL CYS
SEQRES 31 A 567 ILE ALA LYS GLU LEU ILE PRO GLU ALA THR GLU LYS TYR
SEQRES 32 A 567 LEU GLY GLY THR ASP ASP THR VAL LYS LYS LYS ASP LEU
SEQRES 33 A 567 PHE LEU ASP LEU ILE ALA ASP VAL MET PHE GLY VAL PRO
SEQRES 34 A 567 SER VAL ILE VAL ALA ARG ASN HIS ARG ASP ALA GLY ALA
SEQRES 35 A 567 PRO THR TYR MET TYR GLU PHE GLN TYR ARG PRO SER PHE
SEQRES 36 A 567 SER SER ASP MET LYS PRO LYS THR VAL ILE GLY ASP HIS
SEQRES 37 A 567 GLY ASP GLU LEU PHE SER VAL PHE GLY ALA PRO PHE LEU
SEQRES 38 A 567 LYS GLU GLY ALA SER GLU GLU GLU ILE ARG LEU SER LYS
SEQRES 39 A 567 MET VAL MET LYS PHE TRP ALA ASN PHE ALA ARG ASN GLY
SEQRES 40 A 567 ASN PRO ASN GLY GLU GLY LEU PRO HIS TRP PRO GLU TYR
SEQRES 41 A 567 ASN GLN LYS GLU GLY TYR LEU GLN ILE GLY ALA ASN THR
SEQRES 42 A 567 GLN ALA ALA GLN LYS LEU LYS ASP LYS GLU VAL ALA PHE
SEQRES 43 A 567 TRP THR ASN LEU PHE ALA LYS LYS ALA VAL GLU LYS PRO
SEQRES 44 A 567 PRO GLN THR GLU HIS ILE GLU LEU
SEQRES 1 B 567 MET TRP LEU ARG ALA PHE ILE LEU ALA THR LEU SER ALA
SEQRES 2 B 567 SER ALA ALA TRP GLY HIS PRO SER SER PRO PRO VAL VAL
SEQRES 3 B 567 ASP THR VAL HIS GLY LYS VAL LEU GLY LYS PHE VAL SER
SEQRES 4 B 567 LEU GLU GLY PHE ALA GLN PRO VAL ALA ILE PHE LEU GLY
SEQRES 5 B 567 ILE PRO PHE ALA LYS PRO PRO LEU GLY PRO LEU ARG PHE
SEQRES 6 B 567 THR PRO PRO GLN PRO ALA GLU PRO TRP SER PHE VAL LYS
SEQRES 7 B 567 ASN ALA THR SER TYR PRO PRO MET CYS THR GLN ASP PRO
SEQRES 8 B 567 LYS ALA GLY GLN LEU LEU SER GLU LEU PHE THR ASN ARG
SEQRES 9 B 567 LYS GLU ASN ILE PRO LEU LYS LEU SER GLU ASP CYS LEU
SEQRES 10 B 567 TYR LEU ASN ILE TYR THR PRO ALA ASP LEU THR LYS LYS
SEQRES 11 B 567 ASN ARG LEU PRO VAL MET VAL TRP ILE HIS GLY GLY GLY
SEQRES 12 B 567 LEU MET VAL GLY ALA ALA SER THR TYR ASP GLY LEU ALA
SEQRES 13 B 567 LEU ALA ALA HIS GLU ASN VAL VAL VAL VAL THR ILE GLN
SEQRES 14 B 567 TYR ARG LEU GLY ILE TRP GLY PHE PHE SER THR GLY ASP
SEQRES 15 B 567 GLU HIS SER ARG GLY ASN TRP GLY HIS LEU ASP GLN VAL
SEQRES 16 B 567 ALA ALA LEU ARG TRP VAL GLN ASP ASN ILE ALA SER PHE
SEQRES 17 B 567 GLY GLY ASN PRO GLY SER VAL THR ILE PHE GLY GLU SER
SEQRES 18 B 567 ALA GLY GLY GLU SER VAL SER VAL LEU VAL LEU SER PRO
SEQRES 19 B 567 LEU ALA LYS ASN LEU PHE HIS ARG ALA ILE SER GLU SER
SEQRES 20 B 567 GLY VAL ALA LEU THR SER VAL LEU VAL LYS LYS GLY ASP
SEQRES 21 B 567 VAL LYS PRO LEU ALA GLU GLN ILE ALA ILE THR ALA GLY
SEQRES 22 B 567 CYS LYS THR THR THR SER ALA VAL MET VAL HIS CYS LEU
SEQRES 23 B 567 ARG GLN LYS THR GLU GLU GLU LEU LEU GLU THR THR LEU
SEQRES 24 B 567 LYS MET LYS PHE LEU SER LEU ASP LEU GLN GLY ASP PRO
SEQRES 25 B 567 ARG GLU SER GLN PRO LEU LEU GLY THR VAL ILE ASP GLY
SEQRES 26 B 567 MET LEU LEU LEU LYS THR PRO GLU GLU LEU GLN ALA GLU
SEQRES 27 B 567 ARG ASN PHE HIS THR VAL PRO TYR MET VAL GLY ILE ASN
SEQRES 28 B 567 LYS GLN GLU PHE GLY TRP LEU ILE PRO MET GLN LEU MET
SEQRES 29 B 567 SER TYR PRO LEU SER GLU GLY GLN LEU ASP GLN LYS THR
SEQRES 30 B 567 ALA MET SER LEU LEU TRP LYS SER TYR PRO LEU VAL CYS
SEQRES 31 B 567 ILE ALA LYS GLU LEU ILE PRO GLU ALA THR GLU LYS TYR
SEQRES 32 B 567 LEU GLY GLY THR ASP ASP THR VAL LYS LYS LYS ASP LEU
SEQRES 33 B 567 PHE LEU ASP LEU ILE ALA ASP VAL MET PHE GLY VAL PRO
SEQRES 34 B 567 SER VAL ILE VAL ALA ARG ASN HIS ARG ASP ALA GLY ALA
SEQRES 35 B 567 PRO THR TYR MET TYR GLU PHE GLN TYR ARG PRO SER PHE
SEQRES 36 B 567 SER SER ASP MET LYS PRO LYS THR VAL ILE GLY ASP HIS
SEQRES 37 B 567 GLY ASP GLU LEU PHE SER VAL PHE GLY ALA PRO PHE LEU
SEQRES 38 B 567 LYS GLU GLY ALA SER GLU GLU GLU ILE ARG LEU SER LYS
SEQRES 39 B 567 MET VAL MET LYS PHE TRP ALA ASN PHE ALA ARG ASN GLY
SEQRES 40 B 567 ASN PRO ASN GLY GLU GLY LEU PRO HIS TRP PRO GLU TYR
SEQRES 41 B 567 ASN GLN LYS GLU GLY TYR LEU GLN ILE GLY ALA ASN THR
SEQRES 42 B 567 GLN ALA ALA GLN LYS LEU LYS ASP LYS GLU VAL ALA PHE
SEQRES 43 B 567 TRP THR ASN LEU PHE ALA LYS LYS ALA VAL GLU LYS PRO
SEQRES 44 B 567 PRO GLN THR GLU HIS ILE GLU LEU
SEQRES 1 C 567 MET TRP LEU ARG ALA PHE ILE LEU ALA THR LEU SER ALA
SEQRES 2 C 567 SER ALA ALA TRP GLY HIS PRO SER SER PRO PRO VAL VAL
SEQRES 3 C 567 ASP THR VAL HIS GLY LYS VAL LEU GLY LYS PHE VAL SER
SEQRES 4 C 567 LEU GLU GLY PHE ALA GLN PRO VAL ALA ILE PHE LEU GLY
SEQRES 5 C 567 ILE PRO PHE ALA LYS PRO PRO LEU GLY PRO LEU ARG PHE
SEQRES 6 C 567 THR PRO PRO GLN PRO ALA GLU PRO TRP SER PHE VAL LYS
SEQRES 7 C 567 ASN ALA THR SER TYR PRO PRO MET CYS THR GLN ASP PRO
SEQRES 8 C 567 LYS ALA GLY GLN LEU LEU SER GLU LEU PHE THR ASN ARG
SEQRES 9 C 567 LYS GLU ASN ILE PRO LEU LYS LEU SER GLU ASP CYS LEU
SEQRES 10 C 567 TYR LEU ASN ILE TYR THR PRO ALA ASP LEU THR LYS LYS
SEQRES 11 C 567 ASN ARG LEU PRO VAL MET VAL TRP ILE HIS GLY GLY GLY
SEQRES 12 C 567 LEU MET VAL GLY ALA ALA SER THR TYR ASP GLY LEU ALA
SEQRES 13 C 567 LEU ALA ALA HIS GLU ASN VAL VAL VAL VAL THR ILE GLN
SEQRES 14 C 567 TYR ARG LEU GLY ILE TRP GLY PHE PHE SER THR GLY ASP
SEQRES 15 C 567 GLU HIS SER ARG GLY ASN TRP GLY HIS LEU ASP GLN VAL
SEQRES 16 C 567 ALA ALA LEU ARG TRP VAL GLN ASP ASN ILE ALA SER PHE
SEQRES 17 C 567 GLY GLY ASN PRO GLY SER VAL THR ILE PHE GLY GLU SER
SEQRES 18 C 567 ALA GLY GLY GLU SER VAL SER VAL LEU VAL LEU SER PRO
SEQRES 19 C 567 LEU ALA LYS ASN LEU PHE HIS ARG ALA ILE SER GLU SER
SEQRES 20 C 567 GLY VAL ALA LEU THR SER VAL LEU VAL LYS LYS GLY ASP
SEQRES 21 C 567 VAL LYS PRO LEU ALA GLU GLN ILE ALA ILE THR ALA GLY
SEQRES 22 C 567 CYS LYS THR THR THR SER ALA VAL MET VAL HIS CYS LEU
SEQRES 23 C 567 ARG GLN LYS THR GLU GLU GLU LEU LEU GLU THR THR LEU
SEQRES 24 C 567 LYS MET LYS PHE LEU SER LEU ASP LEU GLN GLY ASP PRO
SEQRES 25 C 567 ARG GLU SER GLN PRO LEU LEU GLY THR VAL ILE ASP GLY
SEQRES 26 C 567 MET LEU LEU LEU LYS THR PRO GLU GLU LEU GLN ALA GLU
SEQRES 27 C 567 ARG ASN PHE HIS THR VAL PRO TYR MET VAL GLY ILE ASN
SEQRES 28 C 567 LYS GLN GLU PHE GLY TRP LEU ILE PRO MET GLN LEU MET
SEQRES 29 C 567 SER TYR PRO LEU SER GLU GLY GLN LEU ASP GLN LYS THR
SEQRES 30 C 567 ALA MET SER LEU LEU TRP LYS SER TYR PRO LEU VAL CYS
SEQRES 31 C 567 ILE ALA LYS GLU LEU ILE PRO GLU ALA THR GLU LYS TYR
SEQRES 32 C 567 LEU GLY GLY THR ASP ASP THR VAL LYS LYS LYS ASP LEU
SEQRES 33 C 567 PHE LEU ASP LEU ILE ALA ASP VAL MET PHE GLY VAL PRO
SEQRES 34 C 567 SER VAL ILE VAL ALA ARG ASN HIS ARG ASP ALA GLY ALA
SEQRES 35 C 567 PRO THR TYR MET TYR GLU PHE GLN TYR ARG PRO SER PHE
SEQRES 36 C 567 SER SER ASP MET LYS PRO LYS THR VAL ILE GLY ASP HIS
SEQRES 37 C 567 GLY ASP GLU LEU PHE SER VAL PHE GLY ALA PRO PHE LEU
SEQRES 38 C 567 LYS GLU GLY ALA SER GLU GLU GLU ILE ARG LEU SER LYS
SEQRES 39 C 567 MET VAL MET LYS PHE TRP ALA ASN PHE ALA ARG ASN GLY
SEQRES 40 C 567 ASN PRO ASN GLY GLU GLY LEU PRO HIS TRP PRO GLU TYR
SEQRES 41 C 567 ASN GLN LYS GLU GLY TYR LEU GLN ILE GLY ALA ASN THR
SEQRES 42 C 567 GLN ALA ALA GLN LYS LEU LYS ASP LYS GLU VAL ALA PHE
SEQRES 43 C 567 TRP THR ASN LEU PHE ALA LYS LYS ALA VAL GLU LYS PRO
SEQRES 44 C 567 PRO GLN THR GLU HIS ILE GLU LEU
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET EEE A 601 6
HET EEE B 601 6
HET EEE C 601 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM EEE ETHYL ACETATE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 4 NAG 6(C8 H15 N O6)
FORMUL 4 BMA 3(C6 H12 O6)
FORMUL 7 EEE 3(C4 H8 O2)
HELIX 1 AA1 LEU A 60 ARG A 64 5 5
HELIX 2 AA2 ASP A 90 THR A 102 1 13
HELIX 3 AA3 ALA A 148 TYR A 152 5 5
HELIX 4 AA4 GLY A 154 ASN A 162 1 9
HELIX 5 AA5 LEU A 172 PHE A 178 1 7
HELIX 6 AA6 ASN A 188 ILE A 205 1 18
HELIX 7 AA7 SER A 221 SER A 233 1 13
HELIX 8 AA8 VAL A 261 GLY A 273 1 13
HELIX 9 AA9 THR A 278 GLN A 288 1 11
HELIX 10 AB1 THR A 290 LYS A 302 1 13
HELIX 11 AB2 THR A 331 ARG A 339 1 9
HELIX 12 AB3 TRP A 357 GLN A 362 1 6
HELIX 13 AB4 PRO A 367 GLY A 371 5 5
HELIX 14 AB5 ASP A 374 SER A 385 1 12
HELIX 15 AB6 GLU A 394 GLY A 405 1 12
HELIX 16 AB7 ASP A 409 PHE A 426 1 18
HELIX 17 AB8 PHE A 426 ALA A 440 1 15
HELIX 18 AB9 GLU A 471 PHE A 476 1 6
HELIX 19 AC1 GLY A 477 LYS A 482 1 6
HELIX 20 AC2 SER A 486 GLY A 507 1 22
HELIX 21 AC3 LYS A 540 ALA A 552 1 13
HELIX 22 AC4 LEU B 60 ARG B 64 5 5
HELIX 23 AC5 ASP B 90 THR B 102 1 13
HELIX 24 AC6 ALA B 148 TYR B 152 5 5
HELIX 25 AC7 GLY B 154 ASN B 162 1 9
HELIX 26 AC8 LEU B 172 PHE B 178 1 7
HELIX 27 AC9 ASN B 188 ILE B 205 1 18
HELIX 28 AD1 ALA B 206 PHE B 208 5 3
HELIX 29 AD2 SER B 221 SER B 233 1 13
HELIX 30 AD3 VAL B 261 GLY B 273 1 13
HELIX 31 AD4 THR B 278 GLN B 288 1 11
HELIX 32 AD5 THR B 290 LYS B 302 1 13
HELIX 33 AD6 THR B 331 GLU B 338 1 8
HELIX 34 AD7 TRP B 357 GLN B 362 1 6
HELIX 35 AD8 PRO B 367 GLY B 371 5 5
HELIX 36 AD9 ASP B 374 SER B 385 1 12
HELIX 37 AE1 GLU B 394 GLY B 405 1 12
HELIX 38 AE2 ASP B 409 PHE B 426 1 18
HELIX 39 AE3 PHE B 426 ALA B 440 1 15
HELIX 40 AE4 GLU B 471 PHE B 476 1 6
HELIX 41 AE5 GLY B 477 LYS B 482 1 6
HELIX 42 AE6 SER B 486 GLY B 507 1 22
HELIX 43 AE7 LYS B 540 ALA B 552 1 13
HELIX 44 AE8 LEU C 60 ARG C 64 5 5
HELIX 45 AE9 ASP C 90 THR C 102 1 13
HELIX 46 AF1 GLY C 154 ASN C 162 1 9
HELIX 47 AF2 LEU C 172 PHE C 178 1 7
HELIX 48 AF3 ASN C 188 ILE C 205 1 18
HELIX 49 AF4 SER C 221 SER C 233 1 13
HELIX 50 AF5 VAL C 261 GLY C 273 1 13
HELIX 51 AF6 THR C 278 GLN C 288 1 11
HELIX 52 AF7 THR C 290 LYS C 302 1 13
HELIX 53 AF8 THR C 331 ARG C 339 1 9
HELIX 54 AF9 TRP C 357 GLN C 362 1 6
HELIX 55 AG1 PRO C 367 GLY C 371 5 5
HELIX 56 AG2 ASP C 374 SER C 385 1 12
HELIX 57 AG3 GLU C 394 GLY C 405 1 12
HELIX 58 AG4 ASP C 409 PHE C 426 1 18
HELIX 59 AG5 PHE C 426 ALA C 440 1 15
HELIX 60 AG6 GLU C 471 PHE C 476 1 6
HELIX 61 AG7 GLY C 477 LYS C 482 1 6
HELIX 62 AG8 SER C 486 GLY C 507 1 22
HELIX 63 AG9 LYS C 540 ALA C 552 1 13
SHEET 1 AA1 3 VAL A 25 THR A 28 0
SHEET 2 AA1 3 GLY A 31 LEU A 34 -1 O VAL A 33 N VAL A 26
SHEET 3 AA1 3 LYS A 78 ASN A 79 1 O LYS A 78 N LYS A 32
SHEET 1 AA211 LYS A 36 VAL A 38 0
SHEET 2 AA211 VAL A 47 PRO A 54 -1 O VAL A 47 N VAL A 38
SHEET 3 AA211 TYR A 118 THR A 123 -1 O LEU A 119 N ILE A 53
SHEET 4 AA211 VAL A 164 ILE A 168 -1 O VAL A 165 N TYR A 122
SHEET 5 AA211 LEU A 133 ILE A 139 1 N TRP A 138 O VAL A 166
SHEET 6 AA211 GLY A 210 GLU A 220 1 O THR A 216 N VAL A 137
SHEET 7 AA211 ARG A 242 GLU A 246 1 O ILE A 244 N ILE A 217
SHEET 8 AA211 TYR A 346 ASN A 351 1 O MET A 347 N SER A 245
SHEET 9 AA211 THR A 444 GLN A 450 1 O TYR A 445 N VAL A 348
SHEET 10 AA211 GLY A 525 GLY A 530 1 O ILE A 529 N GLN A 450
SHEET 11 AA211 GLN A 534 GLN A 537 -1 O GLN A 534 N GLN A 528
SHEET 1 AA3 2 MET A 86 CYS A 87 0
SHEET 2 AA3 2 LEU A 112 SER A 113 1 O SER A 113 N MET A 86
SHEET 1 AA4 3 VAL B 25 ASP B 27 0
SHEET 2 AA4 3 LYS B 32 LEU B 34 -1 O VAL B 33 N VAL B 26
SHEET 3 AA4 3 LYS B 78 ASN B 79 1 O LYS B 78 N LYS B 32
SHEET 1 AA511 LYS B 36 VAL B 38 0
SHEET 2 AA511 VAL B 47 PRO B 54 -1 O VAL B 47 N VAL B 38
SHEET 3 AA511 TYR B 118 THR B 123 -1 O LEU B 119 N ILE B 53
SHEET 4 AA511 VAL B 164 ILE B 168 -1 O THR B 167 N ASN B 120
SHEET 5 AA511 LEU B 133 ILE B 139 1 N TRP B 138 O VAL B 166
SHEET 6 AA511 GLY B 210 GLU B 220 1 O THR B 216 N VAL B 137
SHEET 7 AA511 ARG B 242 GLU B 246 1 O ILE B 244 N ILE B 217
SHEET 8 AA511 TYR B 346 ASN B 351 1 O MET B 347 N SER B 245
SHEET 9 AA511 THR B 444 GLN B 450 1 O TYR B 445 N VAL B 348
SHEET 10 AA511 GLY B 525 GLY B 530 1 O ILE B 529 N GLN B 450
SHEET 11 AA511 GLN B 534 GLN B 537 -1 O GLN B 534 N GLN B 528
SHEET 1 AA6 2 MET B 86 CYS B 87 0
SHEET 2 AA6 2 LEU B 112 SER B 113 1 O SER B 113 N MET B 86
SHEET 1 AA7 3 VAL C 25 THR C 28 0
SHEET 2 AA7 3 GLY C 31 LEU C 34 -1 O VAL C 33 N VAL C 26
SHEET 3 AA7 3 LYS C 78 ASN C 79 1 O LYS C 78 N LYS C 32
SHEET 1 AA811 LYS C 36 VAL C 38 0
SHEET 2 AA811 VAL C 47 PRO C 54 -1 O VAL C 47 N VAL C 38
SHEET 3 AA811 TYR C 118 THR C 123 -1 O LEU C 119 N ILE C 53
SHEET 4 AA811 VAL C 164 ILE C 168 -1 O THR C 167 N ASN C 120
SHEET 5 AA811 LEU C 133 ILE C 139 1 N TRP C 138 O VAL C 166
SHEET 6 AA811 GLY C 210 GLU C 220 1 O THR C 216 N VAL C 137
SHEET 7 AA811 ARG C 242 GLU C 246 1 O ARG C 242 N ILE C 217
SHEET 8 AA811 TYR C 346 ASN C 351 1 O MET C 347 N SER C 245
SHEET 9 AA811 THR C 444 GLN C 450 1 O TYR C 445 N VAL C 348
SHEET 10 AA811 GLY C 525 GLY C 530 1 O ILE C 529 N GLN C 450
SHEET 11 AA811 GLN C 534 GLN C 537 -1 O GLN C 534 N GLN C 528
SHEET 1 AA9 2 MET C 86 CYS C 87 0
SHEET 2 AA9 2 LEU C 112 SER C 113 1 O SER C 113 N MET C 86
SSBOND 1 CYS A 87 CYS A 116 1555 1555 2.03
SSBOND 2 CYS A 274 CYS A 285 1555 1555 2.03
SSBOND 3 CYS B 87 CYS B 116 1555 1555 2.03
SSBOND 4 CYS B 274 CYS B 285 1555 1555 2.03
SSBOND 5 CYS C 87 CYS C 116 1555 1555 2.03
SSBOND 6 CYS C 274 CYS C 285 1555 1555 2.03
LINK ND2 ASN B 79 C1 NAG E 1 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MTRIX1 1 -0.499924 0.866068 0.001116 35.40668 1
MTRIX2 1 -0.866069 -0.499924 -0.000345 163.05530 1
MTRIX3 1 0.000259 -0.001139 0.999999 0.04321 1
MTRIX1 2 -0.500664 -0.865641 0.001070 158.96245 1
MTRIX2 2 0.865641 -0.500665 -0.000844 50.88750 1
MTRIX3 2 0.001266 0.000503 0.999999 -0.10558 1
TER 4130 LYS A 553
TER 8260 LYS B 553
TER 12390 LYS C 553
MASTER 260 0 12 63 48 0 0 1212522 3 148 132
END |