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HEADER MEMBRANE PROTEIN 17-JUN-24 9CAR
TITLE HUMAN KIDNEY DIPEPTIDYL PEPTIDASE 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV MEMBRANE FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS HUMAN, KIDNEY, DIPEPTIDYL PEPTIDASE 4, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.LYU,Z.ZHANG
REVDAT 1 06-AUG-25 9CAR 0
JRNL AUTH M.LYU,Z.ZHANG
JRNL TITL HUMAN KIDNEY DIPEPTIDYL PEPTIDASE 4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : PHENIX
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) : 3.020
REMARK 3 NUMBER OF PARTICLES : 11336
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 9CAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1000285111.
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 : DIPEPTIDYL PEPTIDASE 4
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) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00
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) : 3800.00
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
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 LYS A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 TRP A 5
REMARK 465 LYS A 6
REMARK 465 VAL A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 LEU A 12
REMARK 465 GLY A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 VAL A 18
REMARK 465 THR A 19
REMARK 465 ILE A 20
REMARK 465 ILE A 21
REMARK 465 THR A 22
REMARK 465 VAL A 23
REMARK 465 PRO A 24
REMARK 465 VAL A 25
REMARK 465 VAL A 26
REMARK 465 LEU A 27
REMARK 465 LEU A 28
REMARK 465 ASN A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 THR A 32
REMARK 465 ASP A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 THR A 36
REMARK 465 ALA A 37
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 TRP B 5
REMARK 465 LYS B 6
REMARK 465 VAL B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 LEU B 12
REMARK 465 GLY B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 VAL B 18
REMARK 465 THR B 19
REMARK 465 ILE B 20
REMARK 465 ILE B 21
REMARK 465 THR B 22
REMARK 465 VAL B 23
REMARK 465 PRO B 24
REMARK 465 VAL B 25
REMARK 465 VAL B 26
REMARK 465 LEU B 27
REMARK 465 LEU B 28
REMARK 465 ASN B 29
REMARK 465 LYS B 30
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 ASP B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 THR B 36
REMARK 465 ALA B 37
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 GLN A 123 -85.19 -109.92
REMARK 500 TRP A 124 -150.50 -105.37
REMARK 500 ILE A 193 -79.41 -132.49
REMARK 500 GLU A 206 -64.39 -135.43
REMARK 500 SER A 242 -124.76 45.38
REMARK 500 PRO A 255 106.10 -58.86
REMARK 500 ALA A 306 -61.40 -105.31
REMARK 500 THR A 307 -168.82 -122.94
REMARK 500 ASN A 321 19.17 -145.15
REMARK 500 TRP A 402 -158.39 -100.07
REMARK 500 TYR A 547 -49.94 -131.11
REMARK 500 ASP A 556 -164.12 -125.83
REMARK 500 ASN A 562 -167.33 -120.37
REMARK 500 ARG A 597 61.04 -150.26
REMARK 500 THR A 600 -86.85 -120.41
REMARK 500 SER A 630 -123.30 56.73
REMARK 500 ASN A 679 23.69 47.67
REMARK 500 ALA A 707 59.50 -102.44
REMARK 500 ASN A 710 -71.11 -86.97
REMARK 500 MET A 733 110.54 -160.64
REMARK 500 ILE A 742 52.62 39.48
REMARK 500 GLN B 123 -85.62 -109.95
REMARK 500 TRP B 124 -151.53 -104.95
REMARK 500 ILE B 193 -80.05 -132.22
REMARK 500 GLU B 206 -59.94 -127.04
REMARK 500 SER B 242 -131.78 49.20
REMARK 500 PRO B 255 106.90 -58.69
REMARK 500 ALA B 306 -62.98 -104.30
REMARK 500 THR B 307 -169.71 -121.54
REMARK 500 ASN B 321 18.81 -142.61
REMARK 500 TRP B 402 -157.58 -99.92
REMARK 500 LEU B 449 -70.80 -88.14
REMARK 500 TYR B 547 -50.35 -130.39
REMARK 500 ASP B 556 -163.67 -123.73
REMARK 500 ASN B 562 -167.01 -119.98
REMARK 500 ARG B 597 62.11 -151.05
REMARK 500 THR B 600 -86.85 -121.09
REMARK 500 SER B 630 -123.46 56.85
REMARK 500 SER B 657 -60.46 -99.80
REMARK 500 ASN B 679 27.58 41.35
REMARK 500 SER B 686 48.02 -108.00
REMARK 500 ALA B 707 51.42 -105.68
REMARK 500 ASN B 710 -75.50 -86.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 40 0.09 SIDE CHAIN
REMARK 500 ARG A 54 0.19 SIDE CHAIN
REMARK 500 ARG A 140 0.11 SIDE CHAIN
REMARK 500 ARG A 253 0.15 SIDE CHAIN
REMARK 500 ARG A 317 0.13 SIDE CHAIN
REMARK 500 ARG A 429 0.11 SIDE CHAIN
REMARK 500 ARG A 597 0.12 SIDE CHAIN
REMARK 500 ARG A 658 0.20 SIDE CHAIN
REMARK 500 ARG A 684 0.13 SIDE CHAIN
REMARK 500 ARG B 40 0.09 SIDE CHAIN
REMARK 500 ARG B 54 0.20 SIDE CHAIN
REMARK 500 ARG B 140 0.10 SIDE CHAIN
REMARK 500 ARG B 253 0.11 SIDE CHAIN
REMARK 500 ARG B 429 0.11 SIDE CHAIN
REMARK 500 ARG B 596 0.08 SIDE CHAIN
REMARK 500 ARG B 597 0.12 SIDE CHAIN
REMARK 500 ARG B 658 0.08 SIDE CHAIN
REMARK 500 ARG B 684 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-45401 RELATED DB: EMDB
REMARK 900 HUMAN KIDNEY DIPEPTIDYL PEPTIDASE 4
DBREF 9CAR A 1 766 UNP P27487 DPP4_HUMAN 1 766
DBREF 9CAR B 1 766 UNP P27487 DPP4_HUMAN 1 766
SEQRES 1 A 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 A 766 ALA ALA ALA LEU VAL THR ILE ILE THR VAL PRO VAL VAL
SEQRES 3 A 766 LEU LEU ASN LYS GLY THR ASP ASP ALA THR ALA ASP SER
SEQRES 4 A 766 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 5 A 766 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 6 A 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 7 A 766 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 8 A 766 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 9 A 766 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 10 A 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 A 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 A 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 13 A 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 A 766 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 15 A 766 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 16 A 766 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 A 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 A 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 A 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 A 766 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 21 A 766 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 22 A 766 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 23 A 766 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 24 A 766 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 25 A 766 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 26 A 766 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 27 A 766 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 28 A 766 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 29 A 766 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 A 766 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 31 A 766 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 32 A 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 A 766 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 34 A 766 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 35 A 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 A 766 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 37 A 766 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 A 766 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 39 A 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 40 A 766 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 41 A 766 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 A 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 43 A 766 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 44 A 766 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 A 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 A 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 A 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 48 A 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 49 A 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 A 766 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 A 766 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 52 A 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 A 766 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 54 A 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 A 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 A 766 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 57 A 766 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 A 766 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 A 766 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 B 766 ALA ALA ALA LEU VAL THR ILE ILE THR VAL PRO VAL VAL
SEQRES 3 B 766 LEU LEU ASN LYS GLY THR ASP ASP ALA THR ALA ASP SER
SEQRES 4 B 766 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 5 B 766 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 6 B 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 7 B 766 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 8 B 766 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 9 B 766 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 10 B 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 B 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 B 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 13 B 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 B 766 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 15 B 766 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 16 B 766 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 B 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 B 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 B 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 B 766 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 21 B 766 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 22 B 766 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 23 B 766 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 24 B 766 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 25 B 766 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 26 B 766 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 27 B 766 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 28 B 766 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 29 B 766 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 B 766 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 31 B 766 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 32 B 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 B 766 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 34 B 766 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 35 B 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 B 766 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 37 B 766 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 B 766 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 39 B 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 40 B 766 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 41 B 766 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 B 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 43 B 766 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 44 B 766 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 B 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 B 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 B 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 48 B 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 49 B 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 B 766 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 B 766 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 52 B 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 B 766 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 54 B 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 B 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 B 766 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 57 B 766 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 B 766 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 B 766 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG A 801 14
HET NAG A 802 14
HET NAG B 801 14
HET NAG B 802 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
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 3 NAG 24(C8 H15 N O6)
FORMUL 3 BMA 2(C6 H12 O6)
HELIX 1 AA1 THR A 44 LYS A 50 1 7
HELIX 2 AA2 GLU A 91 ASP A 96 5 6
HELIX 3 AA3 ASP A 200 GLU A 206 1 7
HELIX 4 AA4 ASP A 274 LEU A 276 5 3
HELIX 5 AA5 PRO A 290 ILE A 295 1 6
HELIX 6 AA6 GLU A 421 MET A 425 5 5
HELIX 7 AA7 ASN A 497 VAL A 507 1 11
HELIX 8 AA8 ASN A 562 THR A 570 1 9
HELIX 9 AA9 GLY A 587 HIS A 592 1 6
HELIX 10 AB1 ALA A 593 ASN A 595 5 3
HELIX 11 AB2 THR A 600 LYS A 615 1 16
HELIX 12 AB3 TYR A 631 GLY A 641 1 11
HELIX 13 AB4 ASP A 663 GLY A 672 1 10
HELIX 14 AB5 ASN A 679 SER A 686 1 8
HELIX 15 AB6 THR A 687 VAL A 698 5 12
HELIX 16 AB7 HIS A 712 GLY A 727 1 16
HELIX 17 AB8 SER A 744 PHE A 763 1 20
HELIX 18 AB9 THR B 44 LYS B 50 1 7
HELIX 19 AC1 GLU B 91 GLY B 99 5 9
HELIX 20 AC2 ASP B 200 GLU B 206 1 7
HELIX 21 AC3 ASP B 274 LEU B 276 5 3
HELIX 22 AC4 PRO B 290 ILE B 295 1 6
HELIX 23 AC5 GLU B 421 MET B 425 5 5
HELIX 24 AC6 ASN B 497 VAL B 507 1 11
HELIX 25 AC7 ASN B 562 THR B 570 1 9
HELIX 26 AC8 GLY B 587 HIS B 592 1 6
HELIX 27 AC9 ALA B 593 ASN B 595 5 3
HELIX 28 AD1 THR B 600 LYS B 615 1 16
HELIX 29 AD2 TYR B 631 GLY B 641 1 11
HELIX 30 AD3 ARG B 658 TYR B 662 5 5
HELIX 31 AD4 ASP B 663 GLY B 672 1 10
HELIX 32 AD5 ASN B 679 SER B 686 1 8
HELIX 33 AD6 THR B 687 VAL B 698 5 12
HELIX 34 AD7 HIS B 712 GLY B 727 1 16
HELIX 35 AD8 SER B 744 PHE B 763 1 20
SHEET 1 AA1 3 GLU A 67 GLN A 72 0
SHEET 2 AA1 3 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 3 AA1 3 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AA2 3 ASP A 104 ILE A 107 0
SHEET 2 AA2 3 PHE A 113 LYS A 122 -1 O GLU A 117 N ASP A 104
SHEET 3 AA2 3 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 1 AA3 4 TRP A 154 TRP A 157 0
SHEET 2 AA3 4 LEU A 164 VAL A 167 -1 O ALA A 165 N THR A 156
SHEET 3 AA3 4 ILE A 172 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 AA3 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA4 3 ILE A 194 ASN A 196 0
SHEET 2 AA4 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA4 3 TRP A 215 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA5 4 ILE A 194 ASN A 196 0
SHEET 2 AA5 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 4 THR A 265 ASN A 272 -1 O LYS A 267 N GLN A 227
SHEET 4 AA5 4 SER A 284 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 AA6 2 LEU A 235 PHE A 240 0
SHEET 2 AA6 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AA7 4 HIS A 298 TRP A 305 0
SHEET 2 AA7 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA7 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA7 4 ARG A 336 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 AA8 4 HIS A 298 TRP A 305 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA8 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA8 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AA9 4 HIS A 363 PHE A 364 0
SHEET 2 AA9 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AA9 4 ARG A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AA9 4 LYS A 391 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB1 4 VAL A 404 LEU A 410 0
SHEET 2 AB1 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AB1 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB1 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB2 4 CYS A 454 PHE A 461 0
SHEET 2 AB2 4 TYR A 467 PRO A 475 -1 O GLY A 474 N GLN A 455
SHEET 3 AB2 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 AB2 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB3 8 SER A 511 LEU A 519 0
SHEET 2 AB3 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 AB3 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB3 8 TYR A 540 ASP A 545 1 N LEU A 543 O ILE A 574
SHEET 5 AB3 8 VAL A 619 SER A 630 1 O ALA A 625 N LEU A 542
SHEET 6 AB3 8 CYS A 649 PRO A 655 1 O VAL A 653 N GLY A 628
SHEET 7 AB3 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 654
SHEET 8 AB3 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB4 4 ARG B 61 TRP B 62 0
SHEET 2 AB4 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 AB4 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 AB4 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 AB5 3 ASP B 104 ILE B 107 0
SHEET 2 AB5 3 PHE B 113 LYS B 122 -1 O GLU B 117 N ASP B 104
SHEET 3 AB5 3 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 1 AB6 4 TRP B 154 TRP B 157 0
SHEET 2 AB6 4 LEU B 164 VAL B 167 -1 O ALA B 165 N THR B 156
SHEET 3 AB6 4 ILE B 172 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 AB6 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AB7 3 ILE B 194 ASN B 196 0
SHEET 2 AB7 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB7 3 TRP B 215 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AB8 4 ILE B 194 ASN B 196 0
SHEET 2 AB8 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB8 4 THR B 265 ASN B 272 -1 O LYS B 267 N GLN B 227
SHEET 4 AB8 4 SER B 284 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 AB9 2 LEU B 235 PHE B 240 0
SHEET 2 AB9 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AC1 4 HIS B 298 THR B 307 0
SHEET 2 AC1 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 AC1 4 TYR B 322 ASP B 331 -1 O ASP B 326 N LEU B 313
SHEET 4 AC1 4 ARG B 336 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 AC2 4 HIS B 298 THR B 307 0
SHEET 2 AC2 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 AC2 4 TYR B 322 ASP B 331 -1 O ASP B 326 N LEU B 313
SHEET 4 AC2 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 AC3 4 HIS B 363 PHE B 364 0
SHEET 2 AC3 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC3 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 AC3 4 LYS B 391 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AC4 4 VAL B 404 LEU B 410 0
SHEET 2 AC4 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 AC4 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC4 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC5 4 CYS B 454 PHE B 461 0
SHEET 2 AC5 4 TYR B 467 PRO B 475 -1 O GLY B 474 N GLN B 455
SHEET 3 AC5 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 AC5 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AC6 8 SER B 511 LEU B 519 0
SHEET 2 AC6 8 THR B 522 LEU B 530 -1 O TYR B 526 N ASP B 515
SHEET 3 AC6 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 AC6 8 TYR B 540 ASP B 545 1 N LEU B 543 O ILE B 574
SHEET 5 AC6 8 VAL B 619 SER B 630 1 O ALA B 625 N LEU B 542
SHEET 6 AC6 8 CYS B 649 PRO B 655 1 O VAL B 653 N GLY B 628
SHEET 7 AC6 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 654
SHEET 8 AC6 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 385 CYS A 394 1555 1555 2.02
SSBOND 2 CYS A 454 CYS A 472 1555 1555 2.03
SSBOND 3 CYS A 649 CYS A 762 1555 1555 2.03
SSBOND 4 CYS B 385 CYS B 394 1555 1555 2.02
SSBOND 5 CYS B 454 CYS B 472 1555 1555 2.03
SSBOND 6 CYS B 649 CYS B 762 1555 1555 2.03
LINK ND2 ASN A 85 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN A 92 C1 NAG A 802 1555 1555 1.44
LINK ND2 ASN A 150 C1 NAG A 801 1555 1555 1.43
LINK ND2 ASN A 219 C1 NAG E 1 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN A 321 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN B 85 C1 NAG L 1 1555 1555 1.43
LINK ND2 ASN B 92 C1 NAG B 802 1555 1555 1.43
LINK ND2 ASN B 150 C1 NAG B 801 1555 1555 1.44
LINK ND2 ASN B 219 C1 NAG J 1 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG I 1 1555 1555 1.43
LINK ND2 ASN B 321 C1 NAG K 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
CISPEP 1 GLY A 474 PRO A 475 0 13.35
CISPEP 2 GLY B 474 PRO B 475 0 15.03
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
TER 5972 PRO A 766
TER 11944 PRO B 766
MASTER 275 0 26 35 95 0 0 612300 2 384 118
END |