HEADER TRANSPORT PROTEIN 30-SEP-18 6MMG
TITLE DIHETEROMERIC NMDA RECEPTOR GLUN1/GLUN2A IN THE '2-KNUCKLE-SYMMETRIC'
TITLE 2 CONFORMATION, IN COMPLEX WITH GLYCINE AND GLUTAMATE, IN THE PRESENCE
TITLE 3 OF 1 MILLIMOLAR EDTA, AND AT PH 7.4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 1-838;
COMPND 5 SYNONYM: GLUN1,GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1,N-METHYL-D-
COMPND 6 ASPARTATE RECEPTOR SUBUNIT NR1,NMD-R1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 1-837;
COMPND 12 SYNONYM: GLUN2A,GLUTAMATE [NMDA] RECEPTOR SUBUNIT EPSILON-1,N-METHYL
COMPND 13 D-ASPARTATE RECEPTOR SUBTYPE 2A,NR2A;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GRIN1, NMDAR1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: TSA-201;
SOURCE 10 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: RAT;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 GENE: GRIN2A;
SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: TSA-201;
SOURCE 20 EXPRESSION_SYSTEM_ORGAN: KIDNEY
KEYWDS LIGAND-GATED ION CHANNEL, NMDA RECEPTOR, IONOTROPIC GLUTAMATE
KEYWDS 2 RECEPTORS, MEMBRANE PROTEIN, TRANSPORT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR F.JALALI-YAZDI,S.CHOWDHURY,C.YOSHIOKA,E.GOUAUX
REVDAT 4 29-JUL-20 6MMG 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 27-NOV-19 6MMG 1 REMARK
REVDAT 2 19-DEC-18 6MMG 1 JRNL
REVDAT 1 28-NOV-18 6MMG 0
JRNL AUTH F.JALALI-YAZDI,S.CHOWDHURY,C.YOSHIOKA,E.GOUAUX
JRNL TITL MECHANISMS FOR ZINC AND PROTON INHIBITION OF THE
JRNL TITL 2 GLUN1/GLUN2A NMDA RECEPTOR.
JRNL REF CELL V. 175 1520 2018
JRNL REFN ISSN 1097-4172
JRNL PMID 30500536
JRNL DOI 10.1016/J.CELL.2018.10.043
REMARK 2
REMARK 2 RESOLUTION. 6.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SERIALEM, GCTF, UCSF CHIMERA, PYMOL,
REMARK 3 PHENIX, COOT, RELION, RELION, RELION,
REMARK 3 CISTEM
REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 4PE5
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
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) : 6.230
REMARK 3 NUMBER OF PARTICLES : 88979
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 6MMG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237211.
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 : DIHETEROMERIC NMDA RECEPTOR
REMARK 245 GLUN1/GLUN2A IN THE '2-KNUCKLE-
REMARK 245 SYMMETRIC' CONFORMATION, IN
REMARK 245 COMPLEX WITH GLYCINE AND
REMARK 245 GLUTAMATE, IN THE PRESENCE OF 1
REMARK 245 MILLIOMOLAR EDTA, AND AT PH 7.4
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 4.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : SAMPLE WAS BLOTTED FOR 3
REMARK 245 SECONDS AT BLOT FORCE 1.
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : SAMPLE WAS HETEROLOGOUSLY
REMARK 245 EXPRESSED IN TSA-201 CELLS, DETERGENT SOLUBILIZED, AND AFFINITY
REMARK 245 PURIFIED
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 2667
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 BASE (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 55.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
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: TETRAMERIC
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 SER A 2
REMARK 465 THR A 3
REMARK 465 MET A 4
REMARK 465 HIS A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 THR A 8
REMARK 465 PHE A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 LEU A 12
REMARK 465 PHE A 13
REMARK 465 SER A 14
REMARK 465 CYS A 15
REMARK 465 SER A 16
REMARK 465 PHE A 17
REMARK 465 ALA A 18
REMARK 465 ARG A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 CYS A 22
REMARK 465 ASP A 23
REMARK 465 PRO A 24
REMARK 465 GLU A 545
REMARK 465 ILE A 546
REMARK 465 PRO A 547
REMARK 465 ARG A 548
REMARK 465 SER A 549
REMARK 465 THR A 550
REMARK 465 LEU A 551
REMARK 465 ASP A 552
REMARK 465 SER A 553
REMARK 465 PHE A 554
REMARK 465 MET A 555
REMARK 465 GLN A 556
REMARK 465 PRO A 557
REMARK 465 PHE A 558
REMARK 465 GLN A 559
REMARK 465 PHE A 586
REMARK 465 GLY A 587
REMARK 465 ARG A 588
REMARK 465 PHE A 589
REMARK 465 LYS A 590
REMARK 465 VAL A 591
REMARK 465 ASN A 592
REMARK 465 SER A 593
REMARK 465 GLU A 594
REMARK 465 GLU A 595
REMARK 465 GLU A 596
REMARK 465 GLU A 597
REMARK 465 GLU A 598
REMARK 465 ASP A 599
REMARK 465 ALA A 600
REMARK 465 LEU A 601
REMARK 465 GLU A 621
REMARK 465 GLY A 622
REMARK 465 ALA A 623
REMARK 465 PRO A 624
REMARK 465 ARG A 625
REMARK 465 SER A 626
REMARK 465 CYS A 798
REMARK 465 ASP A 799
REMARK 465 SER A 800
REMARK 465 ARG A 801
REMARK 465 SER A 802
REMARK 465 ASN A 803
REMARK 465 ALA A 804
REMARK 465 PRO A 805
REMARK 465 ALA A 806
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 LEU B 4
REMARK 465 GLY B 5
REMARK 465 TYR B 6
REMARK 465 TRP B 7
REMARK 465 THR B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 VAL B 11
REMARK 465 LEU B 12
REMARK 465 PRO B 13
REMARK 465 ALA B 14
REMARK 465 LEU B 15
REMARK 465 LEU B 16
REMARK 465 VAL B 17
REMARK 465 TRP B 18
REMARK 465 ARG B 19
REMARK 465 ASP B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 GLN B 23
REMARK 465 ASN B 24
REMARK 465 ALA B 25
REMARK 465 ALA B 26
REMARK 465 ALA B 27
REMARK 465 GLU B 28
REMARK 465 LYS B 29
REMARK 465 GLY B 30
REMARK 465 PRO B 31
REMARK 465 PRO B 32
REMARK 465 ALA B 33
REMARK 465 ARG B 539
REMARK 465 SER B 540
REMARK 465 ASN B 541
REMARK 465 GLY B 542
REMARK 465 THR B 543
REMARK 465 VAL B 544
REMARK 465 SER B 545
REMARK 465 PRO B 546
REMARK 465 SER B 547
REMARK 465 ALA B 548
REMARK 465 PHE B 549
REMARK 465 LEU B 550
REMARK 465 GLU B 551
REMARK 465 PRO B 552
REMARK 465 PHE B 553
REMARK 465 SER B 554
REMARK 465 SER B 580
REMARK 465 PRO B 581
REMARK 465 VAL B 582
REMARK 465 GLY B 583
REMARK 465 TYR B 584
REMARK 465 ASN B 585
REMARK 465 ARG B 586
REMARK 465 ASN B 587
REMARK 465 LEU B 588
REMARK 465 ALA B 589
REMARK 465 LYS B 590
REMARK 465 GLY B 591
REMARK 465 LYS B 592
REMARK 465 ALA B 593
REMARK 465 PRO B 594
REMARK 465 HIS B 595
REMARK 465 GLY B 596
REMARK 465 PRO B 597
REMARK 465 VAL B 619
REMARK 465 GLN B 620
REMARK 465 HIS B 801
REMARK 465 ASN B 802
REMARK 465 GLU B 803
REMARK 465 LYS B 804
REMARK 465 ASN B 805
REMARK 465 GLU B 806
REMARK 465 VAL B 807
REMARK 465 MET B 808
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 THR C 3
REMARK 465 MET C 4
REMARK 465 HIS C 5
REMARK 465 LEU C 6
REMARK 465 LEU C 7
REMARK 465 THR C 8
REMARK 465 PHE C 9
REMARK 465 ALA C 10
REMARK 465 LEU C 11
REMARK 465 LEU C 12
REMARK 465 PHE C 13
REMARK 465 SER C 14
REMARK 465 CYS C 15
REMARK 465 SER C 16
REMARK 465 PHE C 17
REMARK 465 ALA C 18
REMARK 465 ARG C 19
REMARK 465 ALA C 20
REMARK 465 ALA C 21
REMARK 465 CYS C 22
REMARK 465 ASP C 23
REMARK 465 PRO C 24
REMARK 465 GLU C 545
REMARK 465 ILE C 546
REMARK 465 PRO C 547
REMARK 465 ARG C 548
REMARK 465 SER C 549
REMARK 465 THR C 550
REMARK 465 LEU C 551
REMARK 465 ASP C 552
REMARK 465 SER C 553
REMARK 465 PHE C 554
REMARK 465 MET C 555
REMARK 465 GLN C 556
REMARK 465 PRO C 557
REMARK 465 PHE C 558
REMARK 465 GLN C 559
REMARK 465 PHE C 586
REMARK 465 GLY C 587
REMARK 465 ARG C 588
REMARK 465 PHE C 589
REMARK 465 LYS C 590
REMARK 465 VAL C 591
REMARK 465 ASN C 592
REMARK 465 SER C 593
REMARK 465 GLU C 594
REMARK 465 GLU C 595
REMARK 465 GLU C 596
REMARK 465 GLU C 597
REMARK 465 GLU C 598
REMARK 465 ASP C 599
REMARK 465 ALA C 600
REMARK 465 SER C 617
REMARK 465 GLY C 618
REMARK 465 ILE C 619
REMARK 465 GLY C 620
REMARK 465 GLU C 621
REMARK 465 GLY C 622
REMARK 465 ALA C 623
REMARK 465 PRO C 624
REMARK 465 ARG C 625
REMARK 465 SER C 626
REMARK 465 CYS C 798
REMARK 465 ASP C 799
REMARK 465 SER C 800
REMARK 465 ARG C 801
REMARK 465 SER C 802
REMARK 465 ASN C 803
REMARK 465 ALA C 804
REMARK 465 PRO C 805
REMARK 465 ALA C 806
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 ARG D 3
REMARK 465 LEU D 4
REMARK 465 GLY D 5
REMARK 465 TYR D 6
REMARK 465 TRP D 7
REMARK 465 THR D 8
REMARK 465 LEU D 9
REMARK 465 LEU D 10
REMARK 465 VAL D 11
REMARK 465 LEU D 12
REMARK 465 PRO D 13
REMARK 465 ALA D 14
REMARK 465 LEU D 15
REMARK 465 LEU D 16
REMARK 465 VAL D 17
REMARK 465 TRP D 18
REMARK 465 ARG D 19
REMARK 465 ASP D 20
REMARK 465 PRO D 21
REMARK 465 ALA D 22
REMARK 465 GLN D 23
REMARK 465 ASN D 24
REMARK 465 ALA D 25
REMARK 465 ALA D 26
REMARK 465 ALA D 27
REMARK 465 GLU D 28
REMARK 465 LYS D 29
REMARK 465 GLY D 30
REMARK 465 PRO D 31
REMARK 465 PRO D 32
REMARK 465 ALA D 33
REMARK 465 ARG D 539
REMARK 465 SER D 540
REMARK 465 ASN D 541
REMARK 465 GLY D 542
REMARK 465 THR D 543
REMARK 465 VAL D 544
REMARK 465 SER D 545
REMARK 465 PRO D 546
REMARK 465 SER D 547
REMARK 465 ALA D 548
REMARK 465 PHE D 549
REMARK 465 LEU D 550
REMARK 465 GLU D 551
REMARK 465 PRO D 552
REMARK 465 PHE D 553
REMARK 465 SER D 554
REMARK 465 SER D 580
REMARK 465 PRO D 581
REMARK 465 VAL D 582
REMARK 465 GLY D 583
REMARK 465 TYR D 584
REMARK 465 ASN D 585
REMARK 465 ARG D 586
REMARK 465 ASN D 587
REMARK 465 LEU D 588
REMARK 465 ALA D 589
REMARK 465 LYS D 590
REMARK 465 GLY D 591
REMARK 465 LYS D 592
REMARK 465 ALA D 593
REMARK 465 PRO D 594
REMARK 465 HIS D 595
REMARK 465 GLY D 596
REMARK 465 PRO D 597
REMARK 465 HIS D 801
REMARK 465 ASN D 802
REMARK 465 GLU D 803
REMARK 465 LYS D 804
REMARK 465 ASN D 805
REMARK 465 GLU D 806
REMARK 465 VAL D 807
REMARK 465 MET D 808
REMARK 465 SER D 809
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 OE2 GLU B 413 NE2 HIS B 485 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO C 95 C PRO C 96 N 0.131
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 PRO A 69 5.54 -65.34
REMARK 500 PRO A 96 47.20 -87.70
REMARK 500 ILE A 133 -60.38 -93.84
REMARK 500 THR A 317 32.17 -94.02
REMARK 500 CYS A 420 -168.83 -126.03
REMARK 500 SER A 493 -7.22 68.60
REMARK 500 PRO A 516 75.82 -69.23
REMARK 500 LYS A 764 -162.29 -77.76
REMARK 500 TRP A 768 41.21 -109.89
REMARK 500 THR B 175 -169.74 -119.53
REMARK 500 LYS B 326 75.48 53.44
REMARK 500 GLN B 336 35.87 -97.64
REMARK 500 MET B 338 40.98 -102.30
REMARK 500 CYS B 399 57.26 -94.87
REMARK 500 ASP B 403 34.03 -141.32
REMARK 500 ASN B 404 40.13 -109.99
REMARK 500 LYS B 472 65.79 60.84
REMARK 500 THR B 600 39.62 -99.86
REMARK 500 THR B 749 -169.80 -78.49
REMARK 500 SER B 752 35.25 -140.54
REMARK 500 PHE B 756 -168.83 -114.31
REMARK 500 THR B 759 -168.32 -127.10
REMARK 500 ASP B 813 16.96 -143.58
REMARK 500 TYR C 88 -52.59 -121.48
REMARK 500 PRO C 96 46.51 -82.42
REMARK 500 ASN C 300 66.48 60.49
REMARK 500 THR C 317 34.08 -96.55
REMARK 500 THR C 335 49.70 -92.35
REMARK 500 TYR C 392 53.01 -94.48
REMARK 500 ASP C 481 -168.65 -125.34
REMARK 500 PRO C 516 77.96 -69.12
REMARK 500 LYS C 764 -160.68 -78.24
REMARK 500 TRP C 768 31.61 -96.83
REMARK 500 GLU C 811 -62.63 -95.08
REMARK 500 ALA D 136 -62.96 -94.24
REMARK 500 ALA D 213 -53.89 -120.44
REMARK 500 LYS D 326 74.27 58.38
REMARK 500 MET D 338 36.68 -99.34
REMARK 500 CYS D 399 52.39 -91.97
REMARK 500 THR D 600 38.43 -99.03
REMARK 500 LYS D 603 35.79 -98.76
REMARK 500 VAL D 619 -66.59 -122.39
REMARK 500 GLN D 620 146.72 -173.51
REMARK 500 ASN D 697 -60.88 -95.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-9150 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9147 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9148 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9149 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9151 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9152 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9153 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9154 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9155 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9156 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9157 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9158 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9159 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9160 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9161 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9162 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9163 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9164 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9165 RELATED DB: EMDB
DBREF 6MMG A 1 838 UNP P35439 NMDZ1_RAT 1 838
DBREF 6MMG B 1 837 UNP Q00959 NMDE1_RAT 1 837
DBREF 6MMG C 1 838 UNP P35439 NMDZ1_RAT 1 838
DBREF 6MMG D 1 837 UNP Q00959 NMDE1_RAT 1 837
SEQADV 6MMG THR B 758 UNP Q00959 SER 758 CONFLICT
SEQADV 6MMG THR D 758 UNP Q00959 SER 758 CONFLICT
SEQRES 1 A 838 MET SER THR MET HIS LEU LEU THR PHE ALA LEU LEU PHE
SEQRES 2 A 838 SER CYS SER PHE ALA ARG ALA ALA CYS ASP PRO LYS ILE
SEQRES 3 A 838 VAL ASN ILE GLY ALA VAL LEU SER THR ARG LYS HIS GLU
SEQRES 4 A 838 GLN MET PHE ARG GLU ALA VAL ASN GLN ALA ASN LYS ARG
SEQRES 5 A 838 HIS GLY SER TRP LYS ILE GLN LEU ASN ALA THR SER VAL
SEQRES 6 A 838 THR HIS LYS PRO ASN ALA ILE GLN MET ALA LEU SER VAL
SEQRES 7 A 838 CYS GLU ASP LEU ILE SER SER GLN VAL TYR ALA ILE LEU
SEQRES 8 A 838 VAL SER HIS PRO PRO THR PRO ASN ASP HIS PHE THR PRO
SEQRES 9 A 838 THR PRO VAL SER TYR THR ALA GLY PHE TYR ARG ILE PRO
SEQRES 10 A 838 VAL LEU GLY LEU THR THR ARG MET SER ILE TYR SER ASP
SEQRES 11 A 838 LYS SER ILE HIS LEU SER PHE LEU ARG THR VAL PRO PRO
SEQRES 12 A 838 TYR SER HIS GLN SER SER VAL TRP PHE GLU MET MET ARG
SEQRES 13 A 838 VAL TYR ASN TRP ASN HIS ILE ILE LEU LEU VAL SER ASP
SEQRES 14 A 838 ASP HIS GLU GLY ARG ALA ALA GLN LYS ARG LEU GLU THR
SEQRES 15 A 838 LEU LEU GLU GLU ARG GLU SER LYS ALA GLU LYS VAL LEU
SEQRES 16 A 838 GLN PHE ASP PRO GLY THR LYS ASN VAL THR ALA LEU LEU
SEQRES 17 A 838 MET GLU ALA ARG GLU LEU GLU ALA ARG VAL ILE ILE LEU
SEQRES 18 A 838 SER ALA SER GLU ASP ASP ALA ALA THR VAL TYR ARG ALA
SEQRES 19 A 838 ALA ALA MET LEU ASN MET THR GLY SER GLY TYR VAL TRP
SEQRES 20 A 838 LEU VAL GLY GLU ARG GLU ILE SER GLY ASN ALA LEU ARG
SEQRES 21 A 838 TYR ALA PRO ASP GLY ILE ILE GLY LEU GLN LEU ILE ASN
SEQRES 22 A 838 GLY LYS ASN GLU SER ALA HIS ILE SER ASP ALA VAL GLY
SEQRES 23 A 838 VAL VAL ALA GLN ALA VAL HIS GLU LEU LEU GLU LYS GLU
SEQRES 24 A 838 ASN ILE THR ASP PRO PRO ARG GLY CYS VAL GLY ASN THR
SEQRES 25 A 838 ASN ILE TRP LYS THR GLY PRO LEU PHE LYS ARG VAL LEU
SEQRES 26 A 838 MET SER SER LYS TYR ALA ASP GLY VAL THR GLY ARG VAL
SEQRES 27 A 838 GLU PHE ASN GLU ASP GLY ASP ARG LYS PHE ALA ASN TYR
SEQRES 28 A 838 SER ILE MET ASN LEU GLN ASN ARG LYS LEU VAL GLN VAL
SEQRES 29 A 838 GLY ILE TYR ASN GLY THR HIS VAL ILE PRO ASN ASP ARG
SEQRES 30 A 838 LYS ILE ILE TRP PRO GLY GLY GLU THR GLU LYS PRO ARG
SEQRES 31 A 838 GLY TYR GLN MET SER THR ARG LEU LYS ILE VAL THR ILE
SEQRES 32 A 838 HIS GLN GLU PRO PHE VAL TYR VAL LYS PRO THR MET SER
SEQRES 33 A 838 ASP GLY THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP
SEQRES 34 A 838 PRO VAL LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR
SEQRES 35 A 838 SER PRO GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS
SEQRES 36 A 838 TYR GLY PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG
SEQRES 37 A 838 THR MET ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP
SEQRES 38 A 838 GLY LYS PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN
SEQRES 39 A 838 LYS LYS GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER
SEQRES 40 A 838 GLY GLN ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN
SEQRES 41 A 838 ASN GLU ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE
SEQRES 42 A 838 LYS TYR GLN GLY LEU THR ILE LEU VAL LYS LYS GLU ILE
SEQRES 43 A 838 PRO ARG SER THR LEU ASP SER PHE MET GLN PRO PHE GLN
SEQRES 44 A 838 SER THR LEU TRP LEU LEU VAL GLY LEU SER VAL HIS VAL
SEQRES 45 A 838 VAL ALA VAL MET LEU TYR LEU LEU ASP ARG PHE SER PRO
SEQRES 46 A 838 PHE GLY ARG PHE LYS VAL ASN SER GLU GLU GLU GLU GLU
SEQRES 47 A 838 ASP ALA LEU THR LEU SER SER ALA MET TRP PHE SER TRP
SEQRES 48 A 838 GLY VAL LEU LEU ASN SER GLY ILE GLY GLU GLY ALA PRO
SEQRES 49 A 838 ARG SER PHE SER ALA ARG ILE LEU GLY MET VAL TRP ALA
SEQRES 50 A 838 GLY PHE ALA MET ILE ILE VAL ALA SER TYR THR ALA ASN
SEQRES 51 A 838 LEU ALA ALA PHE LEU VAL LEU ASP ARG PRO GLU GLU ARG
SEQRES 52 A 838 ILE THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER
SEQRES 53 A 838 ASP LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL
SEQRES 54 A 838 ASP ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET
SEQRES 55 A 838 TYR ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA
SEQRES 56 A 838 GLU ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA
SEQRES 57 A 838 PHE ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER
SEQRES 58 A 838 GLN LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE
SEQRES 59 A 838 ARG SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO
SEQRES 60 A 838 TRP LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS
SEQRES 61 A 838 GLU ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL
SEQRES 62 A 838 ARG TYR GLN GLU CYS ASP SER ARG SER ASN ALA PRO ALA
SEQRES 63 A 838 THR LEU THR PHE GLU ASN MET ALA GLY VAL PHE MET LEU
SEQRES 64 A 838 VAL ALA GLY GLY ILE VAL ALA GLY ILE PHE LEU ILE PHE
SEQRES 65 A 838 ILE GLU ILE ALA TYR LYS
SEQRES 1 B 837 MET GLY ARG LEU GLY TYR TRP THR LEU LEU VAL LEU PRO
SEQRES 2 B 837 ALA LEU LEU VAL TRP ARG ASP PRO ALA GLN ASN ALA ALA
SEQRES 3 B 837 ALA GLU LYS GLY PRO PRO ALA LEU ASN ILE ALA VAL LEU
SEQRES 4 B 837 LEU GLY HIS SER HIS ASP VAL THR GLU ARG GLU LEU ARG
SEQRES 5 B 837 ASN LEU TRP GLY PRO GLU GLN ALA THR GLY LEU PRO LEU
SEQRES 6 B 837 ASP VAL ASN VAL VAL ALA LEU LEU MET ASN ARG THR ASP
SEQRES 7 B 837 PRO LYS SER LEU ILE THR HIS VAL CYS ASP LEU MET SER
SEQRES 8 B 837 GLY ALA ARG ILE HIS GLY LEU VAL PHE GLY ASP ASP THR
SEQRES 9 B 837 ASP GLN GLU ALA VAL ALA GLN MET LEU ASP PHE ILE SER
SEQRES 10 B 837 SER GLN THR PHE ILE PRO ILE LEU GLY ILE HIS GLY GLY
SEQRES 11 B 837 ALA SER MET ILE MET ALA ASP LYS ASP PRO THR SER THR
SEQRES 12 B 837 PHE PHE GLN PHE GLY ALA SER ILE GLN GLN GLN ALA THR
SEQRES 13 B 837 VAL MET LEU LYS ILE MET GLN ASP TYR ASP TRP HIS VAL
SEQRES 14 B 837 PHE SER LEU VAL THR THR ILE PHE PRO GLY TYR ARG ASP
SEQRES 15 B 837 PHE ILE SER PHE ILE LYS THR THR VAL ASP ASN SER PHE
SEQRES 16 B 837 VAL GLY TRP ASP MET GLN ASN VAL ILE THR LEU ASP THR
SEQRES 17 B 837 SER PHE GLU ASP ALA LYS THR GLN VAL GLN LEU LYS LYS
SEQRES 18 B 837 ILE HIS SER SER VAL ILE LEU LEU TYR CYS SER LYS ASP
SEQRES 19 B 837 GLU ALA VAL LEU ILE LEU SER GLU ALA ARG SER LEU GLY
SEQRES 20 B 837 LEU THR GLY TYR ASP PHE PHE TRP ILE VAL PRO SER LEU
SEQRES 21 B 837 VAL SER GLY ASN THR GLU LEU ILE PRO LYS GLU PHE PRO
SEQRES 22 B 837 SER GLY LEU ILE SER VAL SER TYR ASP ASP TRP ASP TYR
SEQRES 23 B 837 SER LEU GLU ALA ARG VAL ARG ASP GLY LEU GLY ILE LEU
SEQRES 24 B 837 THR THR ALA ALA SER SER MET LEU GLU LYS PHE SER TYR
SEQRES 25 B 837 ILE PRO GLU ALA LYS ALA SER CYS TYR GLY GLN ALA GLU
SEQRES 26 B 837 LYS PRO GLU THR PRO LEU HIS THR LEU HIS GLN PHE MET
SEQRES 27 B 837 VAL ASN VAL THR TRP ASP GLY LYS ASP LEU SER PHE THR
SEQRES 28 B 837 GLU GLU GLY TYR GLN VAL HIS PRO ARG LEU VAL VAL ILE
SEQRES 29 B 837 VAL LEU ASN LYS ASP ARG GLU TRP GLU LYS VAL GLY LYS
SEQRES 30 B 837 TRP GLU ASN GLN THR LEU SER LEU ARG HIS ALA VAL TRP
SEQRES 31 B 837 PRO ARG TYR LYS SER PHE SER ASP CYS GLU PRO ASP ASP
SEQRES 32 B 837 ASN HIS LEU SER ILE VAL THR LEU GLU GLU ALA PRO PHE
SEQRES 33 B 837 VAL ILE VAL GLU ASP ILE ASP PRO LEU THR GLU THR CYS
SEQRES 34 B 837 VAL ARG ASN THR VAL PRO CYS ARG LYS PHE VAL LYS ILE
SEQRES 35 B 837 ASN ASN SER THR ASN GLU GLY MET ASN VAL LYS LYS CYS
SEQRES 36 B 837 CYS LYS GLY PHE CYS ILE ASP ILE LEU LYS LYS LEU SER
SEQRES 37 B 837 ARG THR VAL LYS PHE THR TYR ASP LEU TYR LEU VAL THR
SEQRES 38 B 837 ASN GLY LYS HIS GLY LYS LYS VAL ASN ASN VAL TRP ASN
SEQRES 39 B 837 GLY MET ILE GLY GLU VAL VAL TYR GLN ARG ALA VAL MET
SEQRES 40 B 837 ALA VAL GLY SER LEU THR ILE ASN GLU GLU ARG SER GLU
SEQRES 41 B 837 VAL VAL ASP PHE SER VAL PRO PHE VAL GLU THR GLY ILE
SEQRES 42 B 837 SER VAL MET VAL SER ARG SER ASN GLY THR VAL SER PRO
SEQRES 43 B 837 SER ALA PHE LEU GLU PRO PHE SER ALA SER VAL TRP VAL
SEQRES 44 B 837 MET MET PHE VAL MET LEU LEU ILE VAL SER ALA ILE ALA
SEQRES 45 B 837 VAL PHE VAL PHE GLU TYR PHE SER PRO VAL GLY TYR ASN
SEQRES 46 B 837 ARG ASN LEU ALA LYS GLY LYS ALA PRO HIS GLY PRO SER
SEQRES 47 B 837 PHE THR ILE GLY LYS ALA ILE TRP LEU LEU TRP GLY LEU
SEQRES 48 B 837 VAL PHE ASN ASN SER VAL PRO VAL GLN ASN PRO LYS GLY
SEQRES 49 B 837 THR THR SER LYS ILE MET VAL SER VAL TRP ALA PHE PHE
SEQRES 50 B 837 ALA VAL ILE PHE LEU ALA SER TYR THR ALA ASN LEU ALA
SEQRES 51 B 837 ALA PHE MET ILE GLN GLU GLU PHE VAL ASP GLN VAL THR
SEQRES 52 B 837 GLY LEU SER ASP LYS LYS PHE GLN ARG PRO HIS ASP TYR
SEQRES 53 B 837 SER PRO PRO PHE ARG PHE GLY THR VAL PRO ASN GLY SER
SEQRES 54 B 837 THR GLU ARG ASN ILE ARG ASN ASN TYR PRO TYR MET HIS
SEQRES 55 B 837 GLN TYR MET THR ARG PHE ASN GLN ARG GLY VAL GLU ASP
SEQRES 56 B 837 ALA LEU VAL SER LEU LYS THR GLY LYS LEU ASP ALA PHE
SEQRES 57 B 837 ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS ALA GLY ARG
SEQRES 58 B 837 ASP GLU GLY CYS LYS LEU VAL THR ILE GLY SER GLY TYR
SEQRES 59 B 837 ILE PHE ALA THR THR GLY TYR GLY ILE ALA LEU GLN LYS
SEQRES 60 B 837 GLY SER PRO TRP LYS ARG GLN ILE ASP LEU ALA LEU LEU
SEQRES 61 B 837 GLN PHE VAL GLY ASP GLY GLU MET GLU GLU LEU GLU THR
SEQRES 62 B 837 LEU TRP LEU THR GLY ILE CYS HIS ASN GLU LYS ASN GLU
SEQRES 63 B 837 VAL MET SER SER GLN LEU ASP ILE ASP ASN MET ALA GLY
SEQRES 64 B 837 VAL PHE TYR MET LEU ALA ALA ALA MET ALA LEU SER LEU
SEQRES 65 B 837 ILE THR PHE ILE TRP
SEQRES 1 C 838 MET SER THR MET HIS LEU LEU THR PHE ALA LEU LEU PHE
SEQRES 2 C 838 SER CYS SER PHE ALA ARG ALA ALA CYS ASP PRO LYS ILE
SEQRES 3 C 838 VAL ASN ILE GLY ALA VAL LEU SER THR ARG LYS HIS GLU
SEQRES 4 C 838 GLN MET PHE ARG GLU ALA VAL ASN GLN ALA ASN LYS ARG
SEQRES 5 C 838 HIS GLY SER TRP LYS ILE GLN LEU ASN ALA THR SER VAL
SEQRES 6 C 838 THR HIS LYS PRO ASN ALA ILE GLN MET ALA LEU SER VAL
SEQRES 7 C 838 CYS GLU ASP LEU ILE SER SER GLN VAL TYR ALA ILE LEU
SEQRES 8 C 838 VAL SER HIS PRO PRO THR PRO ASN ASP HIS PHE THR PRO
SEQRES 9 C 838 THR PRO VAL SER TYR THR ALA GLY PHE TYR ARG ILE PRO
SEQRES 10 C 838 VAL LEU GLY LEU THR THR ARG MET SER ILE TYR SER ASP
SEQRES 11 C 838 LYS SER ILE HIS LEU SER PHE LEU ARG THR VAL PRO PRO
SEQRES 12 C 838 TYR SER HIS GLN SER SER VAL TRP PHE GLU MET MET ARG
SEQRES 13 C 838 VAL TYR ASN TRP ASN HIS ILE ILE LEU LEU VAL SER ASP
SEQRES 14 C 838 ASP HIS GLU GLY ARG ALA ALA GLN LYS ARG LEU GLU THR
SEQRES 15 C 838 LEU LEU GLU GLU ARG GLU SER LYS ALA GLU LYS VAL LEU
SEQRES 16 C 838 GLN PHE ASP PRO GLY THR LYS ASN VAL THR ALA LEU LEU
SEQRES 17 C 838 MET GLU ALA ARG GLU LEU GLU ALA ARG VAL ILE ILE LEU
SEQRES 18 C 838 SER ALA SER GLU ASP ASP ALA ALA THR VAL TYR ARG ALA
SEQRES 19 C 838 ALA ALA MET LEU ASN MET THR GLY SER GLY TYR VAL TRP
SEQRES 20 C 838 LEU VAL GLY GLU ARG GLU ILE SER GLY ASN ALA LEU ARG
SEQRES 21 C 838 TYR ALA PRO ASP GLY ILE ILE GLY LEU GLN LEU ILE ASN
SEQRES 22 C 838 GLY LYS ASN GLU SER ALA HIS ILE SER ASP ALA VAL GLY
SEQRES 23 C 838 VAL VAL ALA GLN ALA VAL HIS GLU LEU LEU GLU LYS GLU
SEQRES 24 C 838 ASN ILE THR ASP PRO PRO ARG GLY CYS VAL GLY ASN THR
SEQRES 25 C 838 ASN ILE TRP LYS THR GLY PRO LEU PHE LYS ARG VAL LEU
SEQRES 26 C 838 MET SER SER LYS TYR ALA ASP GLY VAL THR GLY ARG VAL
SEQRES 27 C 838 GLU PHE ASN GLU ASP GLY ASP ARG LYS PHE ALA ASN TYR
SEQRES 28 C 838 SER ILE MET ASN LEU GLN ASN ARG LYS LEU VAL GLN VAL
SEQRES 29 C 838 GLY ILE TYR ASN GLY THR HIS VAL ILE PRO ASN ASP ARG
SEQRES 30 C 838 LYS ILE ILE TRP PRO GLY GLY GLU THR GLU LYS PRO ARG
SEQRES 31 C 838 GLY TYR GLN MET SER THR ARG LEU LYS ILE VAL THR ILE
SEQRES 32 C 838 HIS GLN GLU PRO PHE VAL TYR VAL LYS PRO THR MET SER
SEQRES 33 C 838 ASP GLY THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP
SEQRES 34 C 838 PRO VAL LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR
SEQRES 35 C 838 SER PRO GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS
SEQRES 36 C 838 TYR GLY PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG
SEQRES 37 C 838 THR MET ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP
SEQRES 38 C 838 GLY LYS PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN
SEQRES 39 C 838 LYS LYS GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER
SEQRES 40 C 838 GLY GLN ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN
SEQRES 41 C 838 ASN GLU ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE
SEQRES 42 C 838 LYS TYR GLN GLY LEU THR ILE LEU VAL LYS LYS GLU ILE
SEQRES 43 C 838 PRO ARG SER THR LEU ASP SER PHE MET GLN PRO PHE GLN
SEQRES 44 C 838 SER THR LEU TRP LEU LEU VAL GLY LEU SER VAL HIS VAL
SEQRES 45 C 838 VAL ALA VAL MET LEU TYR LEU LEU ASP ARG PHE SER PRO
SEQRES 46 C 838 PHE GLY ARG PHE LYS VAL ASN SER GLU GLU GLU GLU GLU
SEQRES 47 C 838 ASP ALA LEU THR LEU SER SER ALA MET TRP PHE SER TRP
SEQRES 48 C 838 GLY VAL LEU LEU ASN SER GLY ILE GLY GLU GLY ALA PRO
SEQRES 49 C 838 ARG SER PHE SER ALA ARG ILE LEU GLY MET VAL TRP ALA
SEQRES 50 C 838 GLY PHE ALA MET ILE ILE VAL ALA SER TYR THR ALA ASN
SEQRES 51 C 838 LEU ALA ALA PHE LEU VAL LEU ASP ARG PRO GLU GLU ARG
SEQRES 52 C 838 ILE THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER
SEQRES 53 C 838 ASP LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL
SEQRES 54 C 838 ASP ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET
SEQRES 55 C 838 TYR ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA
SEQRES 56 C 838 GLU ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA
SEQRES 57 C 838 PHE ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER
SEQRES 58 C 838 GLN LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE
SEQRES 59 C 838 ARG SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO
SEQRES 60 C 838 TRP LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS
SEQRES 61 C 838 GLU ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL
SEQRES 62 C 838 ARG TYR GLN GLU CYS ASP SER ARG SER ASN ALA PRO ALA
SEQRES 63 C 838 THR LEU THR PHE GLU ASN MET ALA GLY VAL PHE MET LEU
SEQRES 64 C 838 VAL ALA GLY GLY ILE VAL ALA GLY ILE PHE LEU ILE PHE
SEQRES 65 C 838 ILE GLU ILE ALA TYR LYS
SEQRES 1 D 837 MET GLY ARG LEU GLY TYR TRP THR LEU LEU VAL LEU PRO
SEQRES 2 D 837 ALA LEU LEU VAL TRP ARG ASP PRO ALA GLN ASN ALA ALA
SEQRES 3 D 837 ALA GLU LYS GLY PRO PRO ALA LEU ASN ILE ALA VAL LEU
SEQRES 4 D 837 LEU GLY HIS SER HIS ASP VAL THR GLU ARG GLU LEU ARG
SEQRES 5 D 837 ASN LEU TRP GLY PRO GLU GLN ALA THR GLY LEU PRO LEU
SEQRES 6 D 837 ASP VAL ASN VAL VAL ALA LEU LEU MET ASN ARG THR ASP
SEQRES 7 D 837 PRO LYS SER LEU ILE THR HIS VAL CYS ASP LEU MET SER
SEQRES 8 D 837 GLY ALA ARG ILE HIS GLY LEU VAL PHE GLY ASP ASP THR
SEQRES 9 D 837 ASP GLN GLU ALA VAL ALA GLN MET LEU ASP PHE ILE SER
SEQRES 10 D 837 SER GLN THR PHE ILE PRO ILE LEU GLY ILE HIS GLY GLY
SEQRES 11 D 837 ALA SER MET ILE MET ALA ASP LYS ASP PRO THR SER THR
SEQRES 12 D 837 PHE PHE GLN PHE GLY ALA SER ILE GLN GLN GLN ALA THR
SEQRES 13 D 837 VAL MET LEU LYS ILE MET GLN ASP TYR ASP TRP HIS VAL
SEQRES 14 D 837 PHE SER LEU VAL THR THR ILE PHE PRO GLY TYR ARG ASP
SEQRES 15 D 837 PHE ILE SER PHE ILE LYS THR THR VAL ASP ASN SER PHE
SEQRES 16 D 837 VAL GLY TRP ASP MET GLN ASN VAL ILE THR LEU ASP THR
SEQRES 17 D 837 SER PHE GLU ASP ALA LYS THR GLN VAL GLN LEU LYS LYS
SEQRES 18 D 837 ILE HIS SER SER VAL ILE LEU LEU TYR CYS SER LYS ASP
SEQRES 19 D 837 GLU ALA VAL LEU ILE LEU SER GLU ALA ARG SER LEU GLY
SEQRES 20 D 837 LEU THR GLY TYR ASP PHE PHE TRP ILE VAL PRO SER LEU
SEQRES 21 D 837 VAL SER GLY ASN THR GLU LEU ILE PRO LYS GLU PHE PRO
SEQRES 22 D 837 SER GLY LEU ILE SER VAL SER TYR ASP ASP TRP ASP TYR
SEQRES 23 D 837 SER LEU GLU ALA ARG VAL ARG ASP GLY LEU GLY ILE LEU
SEQRES 24 D 837 THR THR ALA ALA SER SER MET LEU GLU LYS PHE SER TYR
SEQRES 25 D 837 ILE PRO GLU ALA LYS ALA SER CYS TYR GLY GLN ALA GLU
SEQRES 26 D 837 LYS PRO GLU THR PRO LEU HIS THR LEU HIS GLN PHE MET
SEQRES 27 D 837 VAL ASN VAL THR TRP ASP GLY LYS ASP LEU SER PHE THR
SEQRES 28 D 837 GLU GLU GLY TYR GLN VAL HIS PRO ARG LEU VAL VAL ILE
SEQRES 29 D 837 VAL LEU ASN LYS ASP ARG GLU TRP GLU LYS VAL GLY LYS
SEQRES 30 D 837 TRP GLU ASN GLN THR LEU SER LEU ARG HIS ALA VAL TRP
SEQRES 31 D 837 PRO ARG TYR LYS SER PHE SER ASP CYS GLU PRO ASP ASP
SEQRES 32 D 837 ASN HIS LEU SER ILE VAL THR LEU GLU GLU ALA PRO PHE
SEQRES 33 D 837 VAL ILE VAL GLU ASP ILE ASP PRO LEU THR GLU THR CYS
SEQRES 34 D 837 VAL ARG ASN THR VAL PRO CYS ARG LYS PHE VAL LYS ILE
SEQRES 35 D 837 ASN ASN SER THR ASN GLU GLY MET ASN VAL LYS LYS CYS
SEQRES 36 D 837 CYS LYS GLY PHE CYS ILE ASP ILE LEU LYS LYS LEU SER
SEQRES 37 D 837 ARG THR VAL LYS PHE THR TYR ASP LEU TYR LEU VAL THR
SEQRES 38 D 837 ASN GLY LYS HIS GLY LYS LYS VAL ASN ASN VAL TRP ASN
SEQRES 39 D 837 GLY MET ILE GLY GLU VAL VAL TYR GLN ARG ALA VAL MET
SEQRES 40 D 837 ALA VAL GLY SER LEU THR ILE ASN GLU GLU ARG SER GLU
SEQRES 41 D 837 VAL VAL ASP PHE SER VAL PRO PHE VAL GLU THR GLY ILE
SEQRES 42 D 837 SER VAL MET VAL SER ARG SER ASN GLY THR VAL SER PRO
SEQRES 43 D 837 SER ALA PHE LEU GLU PRO PHE SER ALA SER VAL TRP VAL
SEQRES 44 D 837 MET MET PHE VAL MET LEU LEU ILE VAL SER ALA ILE ALA
SEQRES 45 D 837 VAL PHE VAL PHE GLU TYR PHE SER PRO VAL GLY TYR ASN
SEQRES 46 D 837 ARG ASN LEU ALA LYS GLY LYS ALA PRO HIS GLY PRO SER
SEQRES 47 D 837 PHE THR ILE GLY LYS ALA ILE TRP LEU LEU TRP GLY LEU
SEQRES 48 D 837 VAL PHE ASN ASN SER VAL PRO VAL GLN ASN PRO LYS GLY
SEQRES 49 D 837 THR THR SER LYS ILE MET VAL SER VAL TRP ALA PHE PHE
SEQRES 50 D 837 ALA VAL ILE PHE LEU ALA SER TYR THR ALA ASN LEU ALA
SEQRES 51 D 837 ALA PHE MET ILE GLN GLU GLU PHE VAL ASP GLN VAL THR
SEQRES 52 D 837 GLY LEU SER ASP LYS LYS PHE GLN ARG PRO HIS ASP TYR
SEQRES 53 D 837 SER PRO PRO PHE ARG PHE GLY THR VAL PRO ASN GLY SER
SEQRES 54 D 837 THR GLU ARG ASN ILE ARG ASN ASN TYR PRO TYR MET HIS
SEQRES 55 D 837 GLN TYR MET THR ARG PHE ASN GLN ARG GLY VAL GLU ASP
SEQRES 56 D 837 ALA LEU VAL SER LEU LYS THR GLY LYS LEU ASP ALA PHE
SEQRES 57 D 837 ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS ALA GLY ARG
SEQRES 58 D 837 ASP GLU GLY CYS LYS LEU VAL THR ILE GLY SER GLY TYR
SEQRES 59 D 837 ILE PHE ALA THR THR GLY TYR GLY ILE ALA LEU GLN LYS
SEQRES 60 D 837 GLY SER PRO TRP LYS ARG GLN ILE ASP LEU ALA LEU LEU
SEQRES 61 D 837 GLN PHE VAL GLY ASP GLY GLU MET GLU GLU LEU GLU THR
SEQRES 62 D 837 LEU TRP LEU THR GLY ILE CYS HIS ASN GLU LYS ASN GLU
SEQRES 63 D 837 VAL MET SER SER GLN LEU ASP ILE ASP ASN MET ALA GLY
SEQRES 64 D 837 VAL PHE TYR MET LEU ALA ALA ALA MET ALA LEU SER LEU
SEQRES 65 D 837 ILE THR PHE ILE TRP
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 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 905 14
HET NAG A 908 14
HET NAG A 909 14
HET NAG A 910 14
HET NAG A 913 14
HET NAG A 916 14
HET NAG B 901 14
HET NAG B 902 14
HET NAG B 903 14
HET NAG B 904 14
HET NAG B 905 14
HET NAG C 903 14
HET NAG C 904 14
HET NAG C 905 14
HET NAG C 906 14
HET NAG C 907 14
HET NAG C 908 14
HET NAG C 909 14
HET NAG C 910 14
HET NAG C 911 14
HET NAG D 901 14
HET NAG D 902 14
HET NAG D 903 14
HET NAG D 904 14
HET NAG D 905 14
HET NAG D 906 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 5 NAG 42(C8 H15 N O6)
HELIX 1 AA1 HIS A 38 ASN A 50 1 13
HELIX 2 AA2 ASN A 70 GLN A 86 1 17
HELIX 3 AA3 PRO A 104 GLY A 112 1 9
HELIX 4 AA4 MET A 125 ASP A 130 5 6
HELIX 5 AA5 PRO A 143 ASN A 159 1 17
HELIX 6 AA6 ASP A 170 LEU A 184 1 15
HELIX 7 AA7 VAL A 204 GLU A 213 1 10
HELIX 8 AA8 SER A 224 MET A 237 1 14
HELIX 9 AA9 GLU A 251 SER A 255 5 5
HELIX 10 AB1 GLY A 256 TYR A 261 1 6
HELIX 11 AB2 GLU A 277 LEU A 296 1 20
HELIX 12 AB3 THR A 317 SER A 327 1 11
HELIX 13 AB4 GLY A 457 MET A 470 1 14
HELIX 14 AB5 ASN A 499 SER A 507 1 9
HELIX 15 AB6 ASN A 520 GLN A 525 1 6
HELIX 16 AB7 THR A 561 PHE A 583 1 23
HELIX 17 AB8 LEU A 603 LEU A 614 1 12
HELIX 18 AB9 SER A 628 LEU A 657 1 30
HELIX 19 AC1 THR A 665 ASN A 668 5 4
HELIX 20 AC2 ASP A 669 ASN A 674 1 6
HELIX 21 AC3 SER A 687 GLN A 696 1 10
HELIX 22 AC4 LEU A 699 GLU A 707 1 9
HELIX 23 AC5 SER A 713 ASP A 723 1 11
HELIX 24 AC6 SER A 733 LYS A 743 1 11
HELIX 25 AC7 LYS A 769 ASN A 782 1 14
HELIX 26 AC8 GLY A 783 TRP A 792 1 10
HELIX 27 AC9 MET A 813 LYS A 838 1 26
HELIX 28 AD1 GLU B 48 LEU B 54 1 7
HELIX 29 AD2 ASP B 78 GLY B 92 1 15
HELIX 30 AD3 GLU B 107 SER B 118 1 12
HELIX 31 AD4 HIS B 128 SER B 132 5 5
HELIX 32 AD5 SER B 150 ASP B 166 1 17
HELIX 33 AD6 TYR B 180 ASN B 193 1 14
HELIX 34 AD7 ALA B 213 LYS B 221 1 9
HELIX 35 AD8 SER B 232 LEU B 246 1 15
HELIX 36 AD9 SER B 287 PHE B 310 1 24
HELIX 37 AE1 GLY B 458 VAL B 471 1 14
HELIX 38 AE2 ASN B 494 TYR B 502 1 9
HELIX 39 AE3 ASN B 515 VAL B 522 1 8
HELIX 40 AE4 SER B 556 PHE B 579 1 24
HELIX 41 AE5 LYS B 603 ASN B 614 1 12
HELIX 42 AE6 GLY B 624 GLN B 655 1 32
HELIX 43 AE7 ASP B 667 GLN B 671 5 5
HELIX 44 AE8 GLY B 688 TYR B 698 1 11
HELIX 45 AE9 TYR B 698 ARG B 707 1 10
HELIX 46 AF1 GLY B 712 THR B 722 1 11
HELIX 47 AF2 ALA B 732 GLY B 740 1 9
HELIX 48 AF3 TRP B 771 ASP B 785 1 15
HELIX 49 AF4 GLY B 786 TRP B 795 1 10
HELIX 50 AF5 ASP B 813 PHE B 835 1 23
HELIX 51 AF6 THR C 35 ALA C 49 1 15
HELIX 52 AF7 ASN C 70 SER C 84 1 15
HELIX 53 AF8 PRO C 104 GLY C 112 1 9
HELIX 54 AF9 MET C 125 ASP C 130 5 6
HELIX 55 AG1 TYR C 144 TYR C 158 1 15
HELIX 56 AG2 ASP C 169 GLU C 185 1 17
HELIX 57 AG3 VAL C 204 GLU C 213 1 10
HELIX 58 AG4 SER C 224 MET C 237 1 14
HELIX 59 AG5 GLY C 250 ILE C 254 5 5
HELIX 60 AG6 GLY C 256 TYR C 261 1 6
HELIX 61 AG7 ASN C 276 LEU C 296 1 21
HELIX 62 AG8 THR C 317 SER C 327 1 11
HELIX 63 AG9 GLY C 457 MET C 470 1 14
HELIX 64 AH1 ASN C 499 SER C 507 1 9
HELIX 65 AH2 ASN C 520 ILE C 527 1 8
HELIX 66 AH3 THR C 561 SER C 584 1 24
HELIX 67 AH4 THR C 602 ASN C 616 1 15
HELIX 68 AH5 SER C 628 VAL C 656 1 29
HELIX 69 AH6 ASP C 669 ASN C 674 1 6
HELIX 70 AH7 SER C 687 GLN C 696 1 10
HELIX 71 AH8 LEU C 699 GLU C 707 1 9
HELIX 72 AH9 SER C 713 ASP C 723 1 11
HELIX 73 AI1 SER C 733 LYS C 743 1 11
HELIX 74 AI2 LYS C 769 ASN C 782 1 14
HELIX 75 AI3 GLY C 783 TRP C 792 1 10
HELIX 76 AI4 ASN C 812 LYS C 838 1 27
HELIX 77 AI5 GLU D 48 GLY D 56 1 9
HELIX 78 AI6 ASP D 78 GLY D 92 1 15
HELIX 79 AI7 GLU D 107 PHE D 121 1 15
HELIX 80 AI8 HIS D 128 SER D 132 5 5
HELIX 81 AI9 SER D 150 ASP D 166 1 17
HELIX 82 AJ1 TYR D 180 ASP D 192 1 13
HELIX 83 AJ2 LYS D 214 LYS D 220 1 7
HELIX 84 AJ3 SER D 232 LEU D 246 1 15
HELIX 85 AJ4 SER D 287 PHE D 310 1 24
HELIX 86 AJ5 GLY D 458 LYS D 472 1 15
HELIX 87 AJ6 ASN D 494 TYR D 502 1 9
HELIX 88 AJ7 ASN D 515 VAL D 522 1 8
HELIX 89 AJ8 SER D 556 PHE D 579 1 24
HELIX 90 AJ9 LYS D 603 GLY D 610 1 8
HELIX 91 AK1 GLY D 624 GLN D 655 1 32
HELIX 92 AK2 ASP D 667 GLN D 671 5 5
HELIX 93 AK3 ARG D 672 TYR D 676 5 5
HELIX 94 AK4 GLY D 688 TYR D 698 1 11
HELIX 95 AK5 TYR D 698 ARG D 707 1 10
HELIX 96 AK6 GLY D 712 GLY D 723 1 12
HELIX 97 AK7 ALA D 732 ARG D 741 1 10
HELIX 98 AK8 PRO D 770 ASP D 785 1 16
HELIX 99 AK9 GLY D 786 LEU D 796 1 11
HELIX 100 AL1 ASP D 813 PHE D 835 1 23
SHEET 1 AA1 5 GLN A 59 VAL A 65 0
SHEET 2 AA1 5 ILE A 26 VAL A 32 1 N ILE A 29 O THR A 63
SHEET 3 AA1 5 ALA A 89 LEU A 91 1 O ALA A 89 N GLY A 30
SHEET 4 AA1 5 VAL A 118 GLY A 120 1 O LEU A 119 N ILE A 90
SHEET 5 AA1 5 PHE A 137 ARG A 139 1 O LEU A 138 N VAL A 118
SHEET 1 AA2 3 ILE A 164 VAL A 167 0
SHEET 2 AA2 3 VAL A 218 SER A 222 1 O SER A 222 N LEU A 166
SHEET 3 AA2 3 VAL A 246 LEU A 248 1 O VAL A 246 N ILE A 219
SHEET 1 AA3 4 ILE A 267 LEU A 271 0
SHEET 2 AA3 4 TYR A 351 LEU A 356 -1 O SER A 352 N GLN A 270
SHEET 3 AA3 4 LEU A 361 ASN A 368 -1 O VAL A 364 N ILE A 353
SHEET 4 AA3 4 HIS A 371 PRO A 374 -1 O ILE A 373 N ILE A 366
SHEET 1 AA4 7 THR A 473 VAL A 476 0
SHEET 2 AA4 7 ARG A 397 VAL A 401 1 N ILE A 400 O GLU A 475
SHEET 3 AA4 7 MET A 512 THR A 518 1 O VAL A 514 N VAL A 401
SHEET 4 AA4 7 PHE A 753 GLY A 761 -1 O GLY A 761 N ILE A 513
SHEET 5 AA4 7 LYS A 534 VAL A 542 -1 N LEU A 538 O PHE A 753
SHEET 6 AA4 7 ALA A 728 ASP A 732 -1 O TRP A 731 N THR A 539
SHEET 7 AA4 7 TYR A 681 ALA A 682 1 N ALA A 682 O ALA A 728
SHEET 1 AA5 6 THR A 473 VAL A 476 0
SHEET 2 AA5 6 ARG A 397 VAL A 401 1 N ILE A 400 O GLU A 475
SHEET 3 AA5 6 MET A 512 THR A 518 1 O VAL A 514 N VAL A 401
SHEET 4 AA5 6 PHE A 753 GLY A 761 -1 O GLY A 761 N ILE A 513
SHEET 5 AA5 6 LYS A 534 VAL A 542 -1 N LEU A 538 O PHE A 753
SHEET 6 AA5 6 VAL A 747 THR A 748 -1 O VAL A 747 N VAL A 542
SHEET 1 AA6 3 TYR A 410 LYS A 412 0
SHEET 2 AA6 3 VAL A 451 TYR A 456 -1 O CYS A 454 N LYS A 412
SHEET 3 AA6 3 VAL A 434 GLY A 438 -1 N VAL A 434 O CYS A 455
SHEET 1 AA7 2 GLU A 488 ARG A 489 0
SHEET 2 AA7 2 LYS A 496 GLU A 497 -1 O GLU A 497 N GLU A 488
SHEET 1 AA8 5 ASN B 68 MET B 74 0
SHEET 2 AA8 5 ASN B 35 GLY B 41 1 N LEU B 40 O MET B 74
SHEET 3 AA8 5 GLY B 97 ASP B 102 1 O GLY B 97 N ALA B 37
SHEET 4 AA8 5 ILE B 124 GLY B 126 1 O LEU B 125 N LEU B 98
SHEET 5 AA8 5 PHE B 144 PHE B 145 1 O PHE B 145 N ILE B 124
SHEET 1 AA9 8 ILE B 204 THR B 205 0
SHEET 2 AA9 8 PHE B 170 THR B 174 1 N LEU B 172 O ILE B 204
SHEET 3 AA9 8 VAL B 226 TYR B 230 1 O LEU B 228 N VAL B 173
SHEET 4 AA9 8 PHE B 254 VAL B 257 1 O PHE B 254 N ILE B 227
SHEET 5 AA9 8 ILE B 277 SER B 280 1 O ILE B 277 N VAL B 257
SHEET 6 AA9 8 VAL B 362 LEU B 366 -1 O ILE B 364 N SER B 278
SHEET 7 AA9 8 TRP B 372 TRP B 378 -1 O GLU B 373 N VAL B 365
SHEET 8 AA9 8 LEU B 383 LEU B 385 -1 O SER B 384 N LYS B 377
SHEET 1 AB1 2 THR B 342 TRP B 343 0
SHEET 2 AB1 2 LYS B 346 ASP B 347 -1 O LYS B 346 N TRP B 343
SHEET 1 AB2 2 SER B 407 THR B 410 0
SHEET 2 AB2 2 ASP B 476 LEU B 479 1 O ASP B 476 N ILE B 408
SHEET 1 AB3 3 ILE B 418 GLU B 420 0
SHEET 2 AB3 3 GLY B 449 LYS B 457 -1 O LYS B 457 N ILE B 418
SHEET 3 AB3 3 VAL B 434 LYS B 441 -1 N VAL B 434 O CYS B 456
SHEET 1 AB4 3 MET B 507 ALA B 508 0
SHEET 2 AB4 3 ALA B 764 LEU B 765 -1 O ALA B 764 N ALA B 508
SHEET 3 AB4 3 ASP B 523 PHE B 524 -1 N ASP B 523 O LEU B 765
SHEET 1 AB5 2 ILE B 533 MET B 536 0
SHEET 2 AB5 2 PHE B 728 ASP B 731 -1 O TYR B 730 N SER B 534
SHEET 1 AB6 5 GLN C 59 VAL C 65 0
SHEET 2 AB6 5 ILE C 26 VAL C 32 1 N VAL C 27 O GLN C 59
SHEET 3 AB6 5 VAL C 87 VAL C 92 1 O TYR C 88 N ASN C 28
SHEET 4 AB6 5 VAL C 118 GLY C 120 1 O LEU C 119 N ILE C 90
SHEET 5 AB6 5 PHE C 137 ARG C 139 1 O LEU C 138 N VAL C 118
SHEET 1 AB7 4 LYS C 193 GLN C 196 0
SHEET 2 AB7 4 ILE C 164 VAL C 167 1 N VAL C 167 O LEU C 195
SHEET 3 AB7 4 VAL C 218 SER C 222 1 O ILE C 220 N ILE C 164
SHEET 4 AB7 4 VAL C 246 LEU C 248 1 O VAL C 246 N ILE C 219
SHEET 1 AB8 4 ILE C 267 LEU C 271 0
SHEET 2 AB8 4 TYR C 351 LEU C 356 -1 O SER C 352 N GLN C 270
SHEET 3 AB8 4 LEU C 361 ASN C 368 -1 O VAL C 362 N ASN C 355
SHEET 4 AB8 4 HIS C 371 PRO C 374 -1 O ILE C 373 N ILE C 366
SHEET 1 AB9 7 THR C 473 LEU C 478 0
SHEET 2 AB9 7 ARG C 397 THR C 402 1 N ILE C 400 O GLU C 475
SHEET 3 AB9 7 MET C 512 THR C 518 1 O MET C 512 N LYS C 399
SHEET 4 AB9 7 PHE C 753 GLY C 761 -1 O GLY C 761 N ILE C 513
SHEET 5 AB9 7 LYS C 534 LYS C 543 -1 N LEU C 538 O PHE C 753
SHEET 6 AB9 7 ALA C 728 ASP C 732 -1 O PHE C 729 N LEU C 541
SHEET 7 AB9 7 TYR C 681 ALA C 682 1 N ALA C 682 O ILE C 730
SHEET 1 AC1 6 THR C 473 LEU C 478 0
SHEET 2 AC1 6 ARG C 397 THR C 402 1 N ILE C 400 O GLU C 475
SHEET 3 AC1 6 MET C 512 THR C 518 1 O MET C 512 N LYS C 399
SHEET 4 AC1 6 PHE C 753 GLY C 761 -1 O GLY C 761 N ILE C 513
SHEET 5 AC1 6 LYS C 534 LYS C 543 -1 N LEU C 538 O PHE C 753
SHEET 6 AC1 6 LEU C 746 VAL C 747 -1 O VAL C 747 N VAL C 542
SHEET 1 AC2 3 TYR C 410 LYS C 412 0
SHEET 2 AC2 3 VAL C 451 TYR C 456 -1 O CYS C 454 N LYS C 412
SHEET 3 AC2 3 VAL C 434 GLY C 438 -1 N GLY C 438 O VAL C 451
SHEET 1 AC3 2 GLU C 488 ARG C 489 0
SHEET 2 AC3 2 LYS C 496 GLU C 497 -1 O GLU C 497 N GLU C 488
SHEET 1 AC4 5 ASN D 68 MET D 74 0
SHEET 2 AC4 5 ASN D 35 GLY D 41 1 N VAL D 38 O VAL D 70
SHEET 3 AC4 5 GLY D 97 ASP D 102 1 O GLY D 97 N ALA D 37
SHEET 4 AC4 5 ILE D 124 GLY D 126 1 O LEU D 125 N PHE D 100
SHEET 5 AC4 5 PHE D 144 PHE D 145 1 O PHE D 145 N ILE D 124
SHEET 1 AC5 3 ASP D 199 MET D 200 0
SHEET 2 AC5 3 VAL D 169 THR D 174 1 N PHE D 170 O ASP D 199
SHEET 3 AC5 3 ILE D 204 THR D 205 1 O ILE D 204 N THR D 174
SHEET 1 AC6 8 ASP D 199 MET D 200 0
SHEET 2 AC6 8 VAL D 169 THR D 174 1 N PHE D 170 O ASP D 199
SHEET 3 AC6 8 VAL D 226 TYR D 230 1 O LEU D 228 N VAL D 173
SHEET 4 AC6 8 TRP D 255 VAL D 257 1 O ILE D 256 N LEU D 229
SHEET 5 AC6 8 ILE D 277 SER D 280 1 O ILE D 277 N VAL D 257
SHEET 6 AC6 8 LEU D 361 LEU D 366 -1 O ILE D 364 N SER D 278
SHEET 7 AC6 8 TRP D 372 GLU D 379 -1 O GLU D 373 N VAL D 365
SHEET 8 AC6 8 THR D 382 LEU D 383 -1 O THR D 382 N GLU D 379
SHEET 1 AC7 2 THR D 342 TRP D 343 0
SHEET 2 AC7 2 LYS D 346 ASP D 347 -1 O LYS D 346 N TRP D 343
SHEET 1 AC8 4 ASP D 476 LEU D 479 0
SHEET 2 AC8 4 SER D 407 THR D 410 1 N ILE D 408 O ASP D 476
SHEET 3 AC8 4 MET D 507 ALA D 508 1 N MET D 507 O SER D 407
SHEET 4 AC8 4 ALA D 764 LEU D 765 -1 O ALA D 764 N ALA D 508
SHEET 1 AC9 3 ILE D 418 GLU D 420 0
SHEET 2 AC9 3 GLY D 449 LYS D 457 -1 O LYS D 457 N ILE D 418
SHEET 3 AC9 3 VAL D 434 LYS D 441 -1 N VAL D 440 O MET D 450
SHEET 1 AD1 4 PHE D 682 GLY D 683 0
SHEET 2 AD1 4 ALA D 727 ASP D 731 1 O ILE D 729 N GLY D 683
SHEET 3 AD1 4 ILE D 533 VAL D 537 -1 N SER D 534 O TYR D 730
SHEET 4 AD1 4 VAL D 748 THR D 749 -1 O VAL D 748 N VAL D 537
SSBOND 1 CYS A 420 CYS A 454 1555 1555 2.03
SSBOND 2 CYS A 436 CYS A 455 1555 1555 2.03
SSBOND 3 CYS B 87 CYS B 320 1555 1555 2.03
SSBOND 4 CYS B 429 CYS B 455 1555 1555 2.03
SSBOND 5 CYS B 745 CYS B 800 1555 1555 2.03
SSBOND 6 CYS C 420 CYS C 454 1555 1555 2.03
SSBOND 7 CYS C 436 CYS C 455 1555 1555 2.03
SSBOND 8 CYS D 87 CYS D 320 1555 1555 2.03
SSBOND 9 CYS D 429 CYS D 455 1555 1555 2.03
SSBOND 10 CYS D 745 CYS D 800 1555 1555 2.03
LINK ND2 ASN A 61 C1 NAG E 1 1555 1555 1.46
LINK ND2 ASN A 203 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN A 239 C1 NAG A 905 1555 1555 1.45
LINK ND2 ASN A 276 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN A 300 C1 NAG A 908 1555 1555 1.45
LINK ND2 ASN A 350 C1 NAG A 909 1555 1555 1.45
LINK ND2 ASN A 368 C1 NAG A 910 1555 1555 1.45
LINK ND2 ASN A 440 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN A 471 C1 NAG A 913 1555 1555 1.44
LINK ND2 ASN A 491 C1 NAG A 916 1555 1555 1.44
LINK ND2 ASN A 771 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN B 75 C1 NAG B 901 1555 1555 1.44
LINK ND2 ASN B 340 C1 NAG B 902 1555 1555 1.44
LINK ND2 ASN B 380 C1 NAG B 903 1555 1555 1.44
LINK ND2 ASN B 443 C1 NAG B 904 1555 1555 1.44
LINK ND2 ASN B 444 C1 NAG B 905 1555 1555 1.46
LINK ND2 ASN B 687 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN C 61 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN C 203 C1 NAG C 903 1555 1555 1.44
LINK ND2 ASN C 239 C1 NAG C 904 1555 1555 1.44
LINK ND2 ASN C 276 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN C 300 C1 NAG C 905 1555 1555 1.46
LINK ND2 ASN C 350 C1 NAG C 906 1555 1555 1.44
LINK ND2 ASN C 368 C1 NAG C 907 1555 1555 1.45
LINK ND2 ASN C 440 C1 NAG C 908 1555 1555 1.44
LINK ND2 ASN C 471 C1 NAG C 909 1555 1555 1.44
LINK ND2 ASN C 491 C1 NAG C 911 1555 1555 1.45
LINK ND2 ASN C 771 C1 NAG C 910 1555 1555 1.44
LINK ND2 ASN D 75 C1 NAG D 901 1555 1555 1.45
LINK ND2 ASN D 340 C1 NAG D 902 1555 1555 1.44
LINK ND2 ASN D 380 C1 NAG D 903 1555 1555 1.44
LINK ND2 ASN D 443 C1 NAG D 904 1555 1555 1.44
LINK ND2 ASN D 444 C1 NAG D 905 1555 1555 1.45
LINK ND2 ASN D 687 C1 NAG D 906 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 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
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 1.45
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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
(ATOM LINES ARE NOT SHOWN.)
END
