HEADER TRANSPORT PROTEIN, MEMBRANE PROTEIN 17-JUL-14 4U2P
TITLE FULL-LENGTH AMPA SUBTYPE IONOTROPIC GLUTAMATE RECEPTOR GLUA2 IN THE
TITLE 2 APO STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR 2;
COMPND 3 CHAIN: A, B, D, C;
COMPND 4 SYNONYM: GLUR-2,AMPA-SELECTIVE GLUTAMATE RECEPTOR 2,GLUR-B,GLUR-K2,
COMPND 5 GLUTAMATE RECEPTOR IONOTROPIC,AMPA 2,GLUA2;
COMPND 6 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: GRIA2, GLUR2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: GNTI-;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S
KEYWDS AMPA RECEPTOR, TRANSPORT PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.DUERR,E.GOUAUX
REVDAT 5 27-DEC-23 4U2P 1 HETSYN
REVDAT 4 29-JUL-20 4U2P 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 22-NOV-17 4U2P 1 COMPND SOURCE REMARK
REVDAT 2 01-OCT-14 4U2P 1 JRNL
REVDAT 1 20-AUG-14 4U2P 0
JRNL AUTH K.L.DURR,L.CHEN,R.A.STEIN,R.DE ZORZI,I.M.FOLEA,T.WALZ,
JRNL AUTH 2 H.S.MCHAOURAB,E.GOUAUX
JRNL TITL STRUCTURE AND DYNAMICS OF AMPA RECEPTOR GLUA2 IN RESTING,
JRNL TITL 2 PRE-OPEN, AND DESENSITIZED STATES.
JRNL REF CELL V. 158 778 2014
JRNL REFN ISSN 1097-4172
JRNL PMID 25109876
JRNL DOI 10.1016/J.CELL.2014.07.023
REMARK 2
REMARK 2 RESOLUTION. 3.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.490
REMARK 3 COMPLETENESS FOR RANGE (%) : 72.2
REMARK 3 NUMBER OF REFLECTIONS : 65917
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 3377
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.0077 - 9.3211 0.95 3714 194 0.2305 0.2419
REMARK 3 2 9.3211 - 7.4066 0.99 3680 189 0.2156 0.2356
REMARK 3 3 7.4066 - 6.4728 0.99 3635 195 0.2304 0.2686
REMARK 3 4 6.4728 - 5.8820 0.99 3657 182 0.2382 0.2881
REMARK 3 5 5.8820 - 5.4610 0.99 3580 198 0.2333 0.2614
REMARK 3 6 5.4610 - 5.1394 0.99 3568 190 0.2211 0.2706
REMARK 3 7 5.1394 - 4.8823 0.98 3592 175 0.2127 0.2674
REMARK 3 8 4.8823 - 4.6699 0.98 3522 185 0.2253 0.2723
REMARK 3 9 4.6699 - 4.4903 0.98 3522 207 0.2361 0.2958
REMARK 3 10 4.4903 - 4.3354 0.98 3534 202 0.2493 0.2921
REMARK 3 11 4.3354 - 4.1999 0.96 3419 186 0.2692 0.2956
REMARK 3 12 4.1999 - 4.0799 0.95 3416 178 0.2971 0.3474
REMARK 3 13 4.0799 - 3.9726 0.88 3150 179 0.3039 0.3942
REMARK 3 14 3.9726 - 3.8757 0.80 2881 165 0.3108 0.3775
REMARK 3 15 3.8757 - 3.7876 0.73 2634 141 0.3362 0.3986
REMARK 3 16 3.7876 - 3.7070 0.67 2373 141 0.3388 0.3793
REMARK 3 17 3.7070 - 3.6329 0.60 2121 124 0.3550 0.4083
REMARK 3 18 3.6329 - 3.5644 0.52 1866 92 0.3644 0.3644
REMARK 3 19 3.5644 - 3.5007 0.45 1603 89 0.3592 0.3741
REMARK 3 20 3.5007 - 3.4414 0.36 1285 72 0.3695 0.3962
REMARK 3 21 3.4414 - 3.3859 0.23 827 40 0.3766 0.3622
REMARK 3 22 3.3859 - 3.3338 0.15 536 36 0.3830 0.4116
REMARK 3 23 3.3338 - 3.2848 0.09 312 12 0.3846 0.4463
REMARK 3 24 3.2848 - 3.2386 0.03 113 5 0.3919 0.5118
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.570
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 107.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 22870
REMARK 3 ANGLE : 0.927 31143
REMARK 3 CHIRALITY : 0.062 3583
REMARK 3 PLANARITY : 0.003 3988
REMARK 3 DIHEDRAL : 10.774 7785
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7617 158.9574 90.5850
REMARK 3 T TENSOR
REMARK 3 T11: 0.9633 T22: 0.6794
REMARK 3 T33: 1.1655 T12: 0.1248
REMARK 3 T13: 0.0661 T23: 0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 0.8357 L22: 1.0400
REMARK 3 L33: 0.2434 L12: 0.2227
REMARK 3 L13: -0.1420 L23: 0.1382
REMARK 3 S TENSOR
REMARK 3 S11: -0.2218 S12: -0.0754 S13: -0.2011
REMARK 3 S21: -0.2756 S22: 0.2128 S23: -0.2540
REMARK 3 S31: 0.0735 S32: 0.0276 S33: 0.0024
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4U2P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202681.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : PH 6.2-6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 3.14
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65917
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 49.002
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 5.8-6.2% PEG6000, 5% TMAO,
REMARK 280 0.1-0.3 M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 53.90500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 176.39500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.56500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 176.39500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.90500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.56500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 138230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -149.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C
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 ASN A 8
REMARK 465 SER A 9
REMARK 465 PHE A 546
REMARK 465 SER A 547
REMARK 465 PRO A 548
REMARK 465 TYR A 549
REMARK 465 GLU A 550
REMARK 465 TRP A 551
REMARK 465 HIS A 552
REMARK 465 THR A 553
REMARK 465 GLU A 554
REMARK 465 GLU A 555
REMARK 465 PHE A 556
REMARK 465 GLU A 557
REMARK 465 ASP A 558
REMARK 465 GLY A 559
REMARK 465 ARG A 560
REMARK 465 GLU A 561
REMARK 465 THR A 562
REMARK 465 GLN A 563
REMARK 465 SER A 564
REMARK 465 SER A 565
REMARK 465 GLU A 566
REMARK 465 SER A 567
REMARK 465 THR A 568
REMARK 465 ASN A 569
REMARK 465 GLU A 570
REMARK 465 PHE A 571
REMARK 465 GLY A 572
REMARK 465 ILE A 573
REMARK 465 PHE A 574
REMARK 465 ASN A 575
REMARK 465 SER A 576
REMARK 465 LEU A 577
REMARK 465 TRP A 578
REMARK 465 PHE A 579
REMARK 465 SER A 580
REMARK 465 LEU A 581
REMARK 465 GLY A 582
REMARK 465 ALA A 583
REMARK 465 PHE A 584
REMARK 465 PHE A 585
REMARK 465 GLN A 586
REMARK 465 GLN A 587
REMARK 465 GLY A 588
REMARK 465 ALA A 589
REMARK 465 ASP A 590
REMARK 465 ILE A 591
REMARK 465 SER A 592
REMARK 465 ILE A 812
REMARK 465 GLU A 813
REMARK 465 PHE A 814
REMARK 465 ALA A 815
REMARK 465 TYR A 816
REMARK 465 LYS A 817
REMARK 465 SER A 818
REMARK 465 ARG A 819
REMARK 465 ALA A 820
REMARK 465 GLU A 821
REMARK 465 ALA A 822
REMARK 465 LYS A 823
REMARK 465 ARG A 824
REMARK 465 MET A 825
REMARK 465 LYS A 826
REMARK 465 GLY A 827
REMARK 465 LEU A 828
REMARK 465 VAL A 829
REMARK 465 PRO A 830
REMARK 465 ARG A 831
REMARK 465 ARG B 545
REMARK 465 PHE B 546
REMARK 465 SER B 547
REMARK 465 PRO B 548
REMARK 465 TYR B 549
REMARK 465 GLU B 550
REMARK 465 TRP B 551
REMARK 465 HIS B 552
REMARK 465 THR B 553
REMARK 465 GLU B 554
REMARK 465 GLU B 555
REMARK 465 PHE B 556
REMARK 465 GLU B 557
REMARK 465 ASP B 558
REMARK 465 GLY B 559
REMARK 465 ARG B 560
REMARK 465 GLU B 561
REMARK 465 THR B 562
REMARK 465 GLN B 563
REMARK 465 SER B 564
REMARK 465 SER B 565
REMARK 465 GLU B 566
REMARK 465 SER B 567
REMARK 465 THR B 568
REMARK 465 ASN B 569
REMARK 465 GLU B 570
REMARK 465 PHE B 571
REMARK 465 GLY B 572
REMARK 465 ILE B 573
REMARK 465 PHE B 574
REMARK 465 ASN B 575
REMARK 465 SER B 576
REMARK 465 LEU B 577
REMARK 465 TRP B 578
REMARK 465 PHE B 579
REMARK 465 SER B 580
REMARK 465 LEU B 581
REMARK 465 GLY B 582
REMARK 465 ALA B 583
REMARK 465 PHE B 584
REMARK 465 PHE B 585
REMARK 465 GLN B 586
REMARK 465 GLN B 587
REMARK 465 GLY B 588
REMARK 465 ALA B 589
REMARK 465 ASP B 590
REMARK 465 ILE B 591
REMARK 465 SER B 592
REMARK 465 LYS B 817
REMARK 465 SER B 818
REMARK 465 ARG B 819
REMARK 465 ALA B 820
REMARK 465 GLU B 821
REMARK 465 ALA B 822
REMARK 465 LYS B 823
REMARK 465 ARG B 824
REMARK 465 MET B 825
REMARK 465 LYS B 826
REMARK 465 GLY B 827
REMARK 465 LEU B 828
REMARK 465 VAL B 829
REMARK 465 PRO B 830
REMARK 465 ARG B 831
REMARK 465 VAL D 543
REMARK 465 SER D 544
REMARK 465 ARG D 545
REMARK 465 PHE D 546
REMARK 465 SER D 547
REMARK 465 PRO D 548
REMARK 465 TYR D 549
REMARK 465 GLU D 550
REMARK 465 TRP D 551
REMARK 465 HIS D 552
REMARK 465 THR D 553
REMARK 465 GLU D 554
REMARK 465 GLU D 555
REMARK 465 PHE D 556
REMARK 465 GLU D 557
REMARK 465 ASP D 558
REMARK 465 GLY D 559
REMARK 465 ARG D 560
REMARK 465 GLU D 561
REMARK 465 THR D 562
REMARK 465 GLN D 563
REMARK 465 SER D 564
REMARK 465 SER D 565
REMARK 465 GLU D 566
REMARK 465 SER D 567
REMARK 465 THR D 568
REMARK 465 ASN D 569
REMARK 465 GLU D 570
REMARK 465 PHE D 571
REMARK 465 GLY D 572
REMARK 465 ILE D 573
REMARK 465 PHE D 574
REMARK 465 ASN D 575
REMARK 465 SER D 576
REMARK 465 LEU D 577
REMARK 465 TRP D 578
REMARK 465 PHE D 579
REMARK 465 SER D 580
REMARK 465 LEU D 581
REMARK 465 GLY D 582
REMARK 465 ALA D 583
REMARK 465 PHE D 584
REMARK 465 PHE D 585
REMARK 465 GLN D 586
REMARK 465 GLN D 587
REMARK 465 GLY D 588
REMARK 465 ALA D 589
REMARK 465 ASP D 590
REMARK 465 ILE D 591
REMARK 465 SER D 592
REMARK 465 PRO D 593
REMARK 465 ARG D 594
REMARK 465 SER D 595
REMARK 465 ILE D 812
REMARK 465 GLU D 813
REMARK 465 PHE D 814
REMARK 465 ALA D 815
REMARK 465 TYR D 816
REMARK 465 LYS D 817
REMARK 465 SER D 818
REMARK 465 ARG D 819
REMARK 465 ALA D 820
REMARK 465 GLU D 821
REMARK 465 ALA D 822
REMARK 465 LYS D 823
REMARK 465 ARG D 824
REMARK 465 MET D 825
REMARK 465 LYS D 826
REMARK 465 GLY D 827
REMARK 465 LEU D 828
REMARK 465 VAL D 829
REMARK 465 PRO D 830
REMARK 465 ARG D 831
REMARK 465 THR C 387
REMARK 465 SER C 388
REMARK 465 GLY C 389
REMARK 465 LEU C 390
REMARK 465 SER C 544
REMARK 465 ARG C 545
REMARK 465 PHE C 546
REMARK 465 SER C 547
REMARK 465 PRO C 548
REMARK 465 TYR C 549
REMARK 465 GLU C 550
REMARK 465 TRP C 551
REMARK 465 HIS C 552
REMARK 465 THR C 553
REMARK 465 GLU C 554
REMARK 465 GLU C 555
REMARK 465 PHE C 556
REMARK 465 GLU C 557
REMARK 465 ASP C 558
REMARK 465 GLY C 559
REMARK 465 ARG C 560
REMARK 465 GLU C 561
REMARK 465 THR C 562
REMARK 465 GLN C 563
REMARK 465 SER C 564
REMARK 465 SER C 565
REMARK 465 GLU C 566
REMARK 465 SER C 567
REMARK 465 THR C 568
REMARK 465 ASN C 569
REMARK 465 GLU C 570
REMARK 465 PHE C 571
REMARK 465 GLY C 572
REMARK 465 ILE C 573
REMARK 465 PHE C 574
REMARK 465 ASN C 575
REMARK 465 SER C 576
REMARK 465 LEU C 577
REMARK 465 TRP C 578
REMARK 465 PHE C 579
REMARK 465 SER C 580
REMARK 465 LEU C 581
REMARK 465 GLY C 582
REMARK 465 ALA C 583
REMARK 465 PHE C 584
REMARK 465 PHE C 585
REMARK 465 GLN C 586
REMARK 465 GLN C 587
REMARK 465 GLY C 588
REMARK 465 ALA C 589
REMARK 465 ASP C 590
REMARK 465 ILE C 591
REMARK 465 SER C 592
REMARK 465 PRO C 593
REMARK 465 LYS C 817
REMARK 465 SER C 818
REMARK 465 ARG C 819
REMARK 465 ALA C 820
REMARK 465 GLU C 821
REMARK 465 ALA C 822
REMARK 465 LYS C 823
REMARK 465 ARG C 824
REMARK 465 MET C 825
REMARK 465 LYS C 826
REMARK 465 GLY C 827
REMARK 465 LEU C 828
REMARK 465 VAL C 829
REMARK 465 PRO C 830
REMARK 465 ARG C 831
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 LYS A 77 CG CD CE NZ
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 ASN A 162 CG OD1 ND2
REMARK 470 ASN A 165 CG OD1 ND2
REMARK 470 LYS A 171 CG CD CE NZ
REMARK 470 GLU A 173 CG CD OE1 OE2
REMARK 470 ARG A 176 CG CD NE CZ NH1 NH2
REMARK 470 SER A 177 OG
REMARK 470 LEU A 178 CG CD1 CD2
REMARK 470 LEU A 184 CG CD1 CD2
REMARK 470 LYS A 185 CG CD CE NZ
REMARK 470 LYS A 186 CG CD CE NZ
REMARK 470 GLU A 187 CG CD OE1 OE2
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 LYS A 211 CG CD CE NZ
REMARK 470 HIS A 212 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 213 CG1 CG2
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 LYS A 232 CG CD CE NZ
REMARK 470 GLN A 234 CG CD OE1 NE2
REMARK 470 PHE A 235 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 239 CG CD OE1 OE2
REMARK 470 ARG A 298 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 ARG A 301 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 303 CG CD OE1 OE2
REMARK 470 ILE A 304 CG1 CG2 CD1
REMARK 470 ARG A 306 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 307 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 344 CG CD CE NZ
REMARK 470 LYS A 350 CG CD CE NZ
REMARK 470 GLU A 360 CG CD OE1 OE2
REMARK 470 LEU A 361 CG CD1 CD2
REMARK 470 LYS A 362 CG CD CE NZ
REMARK 470 ARG A 367 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 ILE A 369 CG1 CG2 CD1
REMARK 470 GLU A 374 CG CD OE1 OE2
REMARK 470 VAL A 375 CG1 CG2
REMARK 470 ASP A 376 CG OD1 OD2
REMARK 470 LYS A 377 CG CD CE NZ
REMARK 470 MET A 378 CG SD CE
REMARK 470 VAL A 379 CG1 CG2
REMARK 470 VAL A 380 CG1 CG2
REMARK 470 THR A 381 OG1 CG2
REMARK 470 LEU A 382 CG CD1 CD2
REMARK 470 THR A 383 OG1 CG2
REMARK 470 GLU A 384 CG CD OE1 OE2
REMARK 470 ASP A 385 CG OD1 OD2
REMARK 470 ASP A 386 CG OD1 OD2
REMARK 470 THR A 387 OG1 CG2
REMARK 470 SER A 388 OG
REMARK 470 LEU A 390 CG CD1 CD2
REMARK 470 GLU A 391 CG CD OE1 OE2
REMARK 470 GLN A 392 CG CD OE1 NE2
REMARK 470 LYS A 393 CG CD CE NZ
REMARK 470 THR A 394 OG1 CG2
REMARK 470 LYS A 410 CB CG CD CE NZ
REMARK 470 MET A 414 CB CG SD CE
REMARK 470 LEU A 415 CG CD1 CD2
REMARK 470 GLU A 416 CB CG CD OE1 OE2
REMARK 470 ASN A 418 CG OD1 ND2
REMARK 470 GLU A 419 CG CD OE1 OE2
REMARK 470 ARG A 420 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 422 CG CD OE1 OE2
REMARK 470 LYS A 439 CB CG CD CE NZ
REMARK 470 LYS A 441 CG CD CE NZ
REMARK 470 LEU A 442 CG CD1 CD2
REMARK 470 LYS A 449 CG CD CE NZ
REMARK 470 ILE A 459 CG1 CG2 CD1
REMARK 470 GLU A 466 CG CD OE1 OE2
REMARK 470 LYS A 471 CG CD CE NZ
REMARK 470 LYS A 505 CG CD CE NZ
REMARK 470 LYS A 506 CG CD CE NZ
REMARK 470 LYS A 509 CG CD CE NZ
REMARK 470 SER A 510 OG
REMARK 470 LYS A 511 CG CD CE NZ
REMARK 470 PHE A 517 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 518 CG CD1 CD2
REMARK 470 ASP A 519 CG OD1 OD2
REMARK 470 GLU A 524 CG CD OE1 OE2
REMARK 470 LEU A 542 CG CD1 CD2
REMARK 470 ARG A 545 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 594 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 596 CG CD1 CD2
REMARK 470 ARG A 599 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 610 CG CD1 CD2
REMARK 470 LEU A 620 CG CD1 CD2
REMARK 470 LEU A 624 CG CD1 CD2
REMARK 470 GLU A 627 CG CD OE1 OE2
REMARK 470 GLU A 634 CG CD OE1 OE2
REMARK 470 SER A 635 OG
REMARK 470 GLU A 637 CG CD OE1 OE2
REMARK 470 ASP A 638 CG OD1 OD2
REMARK 470 LYS A 641 CG CD CE NZ
REMARK 470 THR A 643 CB OG1 CG2
REMARK 470 SER A 652 OG
REMARK 470 GLU A 657 CG CD OE1 OE2
REMARK 470 ARG A 661 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 663 CG CD CE NZ
REMARK 470 LYS A 697 CB CG CD CE NZ
REMARK 470 LYS A 699 CG CD CE NZ
REMARK 470 ARG A 715 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 716 CG CD CE NZ
REMARK 470 MET A 721 CG SD CE
REMARK 470 LYS A 722 CG CD CE NZ
REMARK 470 SER A 741 OG
REMARK 470 LYS A 752 CG CD CE NZ
REMARK 470 GLN A 756 CG CD OE1 NE2
REMARK 470 LYS A 761 CG CD CE NZ
REMARK 470 GLU A 772 CG CD OE1 OE2
REMARK 470 LYS A 776 CG CD CE NZ
REMARK 470 ASP A 777 CG OD1 OD2
REMARK 470 SER A 778 OG
REMARK 470 SER A 780 OG
REMARK 470 LYS A 781 CG CD CE NZ
REMARK 470 GLU A 782 CG CD OE1 OE2
REMARK 470 LYS A 783 CG CD CE NZ
REMARK 470 SER A 788 OG
REMARK 470 LEU A 789 CG CD1 CD2
REMARK 470 VAL A 792 CG1 CG2
REMARK 470 ARG B 18 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 77 CG CD CE NZ
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 ARG B 139 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 153 CG CD OE1 OE2
REMARK 470 LYS B 154 CG CD CE NZ
REMARK 470 GLN B 157 CG CD OE1 NE2
REMARK 470 ILE B 166 CG1 CG2 CD1
REMARK 470 ASN B 167 CG OD1 ND2
REMARK 470 ASP B 169 CG OD1 OD2
REMARK 470 LYS B 170 CG CD CE NZ
REMARK 470 LYS B 171 CG CD CE NZ
REMARK 470 ASP B 172 CG OD1 OD2
REMARK 470 LYS B 185 CG CD CE NZ
REMARK 470 LYS B 186 CG CD CE NZ
REMARK 470 ARG B 189 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 232 CG CD CE NZ
REMARK 470 GLU B 239 CG CD OE1 OE2
REMARK 470 ARG B 301 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 307 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 367 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 368 CG CD CE NZ
REMARK 470 TYR B 371 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 377 CG CD CE NZ
REMARK 470 VAL B 379 CG1 CG2
REMARK 470 THR B 381 OG1 CG2
REMARK 470 LEU B 382 CG CD1 CD2
REMARK 470 THR B 383 OG1 CG2
REMARK 470 GLU B 384 CG CD OE1 OE2
REMARK 470 ASP B 385 CG OD1 OD2
REMARK 470 LEU B 390 CG CD1 CD2
REMARK 470 GLU B 391 CG CD OE1 OE2
REMARK 470 GLN B 392 CG CD OE1 NE2
REMARK 470 VAL B 395 CG1 CG2
REMARK 470 VAL B 396 CG1 CG2
REMARK 470 LYS B 410 CB CG CD CE NZ
REMARK 470 MET B 414 CB CG SD CE
REMARK 470 GLU B 416 CB CG CD OE1 OE2
REMARK 470 GLU B 419 CG CD OE1 OE2
REMARK 470 LYS B 434 CG CD CE NZ
REMARK 470 LYS B 439 CB CG CD CE NZ
REMARK 470 LYS B 441 CG CD CE NZ
REMARK 470 LYS B 449 CG CD CE NZ
REMARK 470 LYS B 458 CB CG CD CE NZ
REMARK 470 ILE B 459 CG1 CG2 CD1
REMARK 470 ASN B 461 CG OD1 ND2
REMARK 470 LYS B 505 CG CD CE NZ
REMARK 470 GLN B 508 CG CD OE1 NE2
REMARK 470 LYS B 509 CG CD CE NZ
REMARK 470 SER B 510 OG
REMARK 470 LYS B 511 CG CD CE NZ
REMARK 470 SER B 516 OG
REMARK 470 LEU B 521 CG CD1 CD2
REMARK 470 TYR B 523 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 524 CG CD OE1 OE2
REMARK 470 ILE B 525 CG1 CG2 CD1
REMARK 470 MET B 527 CG SD CE
REMARK 470 TYR B 533 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 540 CG CD1 CD2
REMARK 470 ARG B 594 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 596 CG CD1 CD2
REMARK 470 ARG B 599 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 627 CG CD OE1 OE2
REMARK 470 ARG B 628 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 630 CG1 CG2
REMARK 470 SER B 631 OG
REMARK 470 ILE B 633 CG1 CG2 CD1
REMARK 470 GLU B 634 CG CD OE1 OE2
REMARK 470 SER B 635 OG
REMARK 470 GLU B 637 CG CD OE1 OE2
REMARK 470 ASP B 638 CG OD1 OD2
REMARK 470 LEU B 639 CG CD1 CD2
REMARK 470 LYS B 641 CG CD CE NZ
REMARK 470 THR B 643 CB OG1 CG2
REMARK 470 SER B 652 OG
REMARK 470 GLU B 657 CG CD OE1 OE2
REMARK 470 ARG B 661 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 697 CB CG CD CE NZ
REMARK 470 SER B 741 OG
REMARK 470 LYS B 761 CG CD CE NZ
REMARK 470 LYS B 776 CG CD CE NZ
REMARK 470 ASP B 777 CG OD1 OD2
REMARK 470 SER B 778 OG
REMARK 470 SER B 780 OG
REMARK 470 LYS B 781 CG CD CE NZ
REMARK 470 GLU B 782 CG CD OE1 OE2
REMARK 470 THR B 784 OG1 CG2
REMARK 470 SER B 785 OG
REMARK 470 LEU B 787 CG CD1 CD2
REMARK 470 SER B 788 OG
REMARK 470 LEU D 15 CG CD1 CD2
REMARK 470 ARG D 18 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 38 CG CD OE1 OE2
REMARK 470 PHE D 39 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 77 CG CD CE NZ
REMARK 470 LYS D 78 CG CD CE NZ
REMARK 470 LYS D 116 CG CD CE NZ
REMARK 470 LYS D 130 CG CD CE NZ
REMARK 470 LYS D 155 CG CD CE NZ
REMARK 470 ILE D 161 CG1 CG2 CD1
REMARK 470 ASP D 169 CG OD1 OD2
REMARK 470 LYS D 170 CG CD CE NZ
REMARK 470 LYS D 171 CG CD CE NZ
REMARK 470 GLU D 173 CG CD OE1 OE2
REMARK 470 GLN D 180 CG CD OE1 NE2
REMARK 470 ASP D 181 CG OD1 OD2
REMARK 470 LEU D 184 CG CD1 CD2
REMARK 470 LYS D 185 CG CD CE NZ
REMARK 470 LYS D 186 CG CD CE NZ
REMARK 470 GLU D 187 CG CD OE1 OE2
REMARK 470 ARG D 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 195 CG CD OE1 OE2
REMARK 470 ARG D 196 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 214 CG CD CE NZ
REMARK 470 LYS D 255 CG CD CE NZ
REMARK 470 ARG D 259 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 265 CG CD OE1 OE2
REMARK 470 LYS D 266 CG CD CE NZ
REMARK 470 LYS D 277 CG CD CE NZ
REMARK 470 GLU D 292 CG CD OE1 OE2
REMARK 470 ARG D 295 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 299 CG CD CE NZ
REMARK 470 GLN D 300 CG CD OE1 NE2
REMARK 470 ARG D 301 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 332 CG CD CE NZ
REMARK 470 LYS D 350 CG CD CE NZ
REMARK 470 LYS D 362 CG CD CE NZ
REMARK 470 LYS D 368 CG CD CE NZ
REMARK 470 TYR D 371 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 377 CG CD CE NZ
REMARK 470 VAL D 380 CG1 CG2
REMARK 470 THR D 381 OG1 CG2
REMARK 470 GLU D 384 CG CD OE1 OE2
REMARK 470 ASP D 385 CG OD1 OD2
REMARK 470 LEU D 390 CG CD1 CD2
REMARK 470 LYS D 393 CG CD CE NZ
REMARK 470 THR D 394 OG1 CG2
REMARK 470 LYS D 410 CB CG CD CE NZ
REMARK 470 GLU D 416 CB CG CD OE1 OE2
REMARK 470 GLU D 419 CG CD OE1 OE2
REMARK 470 LYS D 439 CB CG CD CE NZ
REMARK 470 LYS D 449 CG CD CE NZ
REMARK 470 LYS D 458 CB CG CD CE NZ
REMARK 470 ILE D 459 CG1 CG2 CD1
REMARK 470 LYS D 505 CG CD CE NZ
REMARK 470 LYS D 506 CG CD CE NZ
REMARK 470 LYS D 509 CG CD CE NZ
REMARK 470 SER D 510 OG
REMARK 470 LYS D 511 CG CD CE NZ
REMARK 470 SER D 516 OG
REMARK 470 ASP D 519 CG OD1 OD2
REMARK 470 LEU D 521 CG CD1 CD2
REMARK 470 ARG D 599 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 608 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN D 619 CG OD1 ND2
REMARK 470 PHE D 623 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 628 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 630 CG1 CG2
REMARK 470 GLU D 634 CG CD OE1 OE2
REMARK 470 THR D 643 CB OG1 CG2
REMARK 470 SER D 652 OG
REMARK 470 GLU D 657 CG CD OE1 OE2
REMARK 470 ARG D 661 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 663 CG CD CE NZ
REMARK 470 LYS D 669 CG CD CE NZ
REMARK 470 LYS D 695 CG CD CE NZ
REMARK 470 LYS D 697 CB CG CD CE NZ
REMARK 470 LYS D 699 CG CD CE NZ
REMARK 470 LYS D 752 CG CD CE NZ
REMARK 470 GLU D 755 CG CD OE1 OE2
REMARK 470 VAL D 758 CG1 CG2
REMARK 470 LYS D 761 CG CD CE NZ
REMARK 470 LYS D 776 CG CD CE NZ
REMARK 470 ASP D 777 CG OD1 OD2
REMARK 470 SER D 778 OG
REMARK 470 LYS D 781 CG CD CE NZ
REMARK 470 GLU D 782 CG CD OE1 OE2
REMARK 470 SER D 785 OG
REMARK 470 LEU D 787 CG CD1 CD2
REMARK 470 ASN D 791 CG OD1 ND2
REMARK 470 VAL D 792 CG1 CG2
REMARK 470 LEU D 808 CG CD1 CD2
REMARK 470 GLU C 49 CG CD OE1 OE2
REMARK 470 LYS C 77 CG CD CE NZ
REMARK 470 LYS C 130 CG CD CE NZ
REMARK 470 ASP C 138 CG OD1 OD2
REMARK 470 ARG C 139 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 153 CG CD OE1 OE2
REMARK 470 ASN C 167 CG OD1 ND2
REMARK 470 ASP C 169 CG OD1 OD2
REMARK 470 LYS C 170 CG CD CE NZ
REMARK 470 LYS C 171 CG CD CE NZ
REMARK 470 ASP C 172 CG OD1 OD2
REMARK 470 GLU C 173 CG CD OE1 OE2
REMARK 470 LYS C 185 CG CD CE NZ
REMARK 470 LYS C 186 CG CD CE NZ
REMARK 470 GLU C 195 CG CD OE1 OE2
REMARK 470 LEU C 223 CG CD1 CD2
REMARK 470 GLU C 239 CG CD OE1 OE2
REMARK 470 ARG C 295 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 303 CG CD OE1 OE2
REMARK 470 ILE C 304 CG1 CG2 CD1
REMARK 470 ARG C 306 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 307 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 326 CG CD OE1 OE2
REMARK 470 LYS C 344 CG CD CE NZ
REMARK 470 LEU C 382 CG CD1 CD2
REMARK 470 GLU C 384 CG CD OE1 OE2
REMARK 470 ASP C 385 CG OD1 OD2
REMARK 470 ASP C 386 CG OD1 OD2
REMARK 470 GLU C 391 CG CD OE1 OE2
REMARK 470 GLN C 392 CG CD OE1 NE2
REMARK 470 LYS C 393 CG CD CE NZ
REMARK 470 LYS C 409 CG CD CE NZ
REMARK 470 LYS C 410 CB CG CD CE NZ
REMARK 470 MET C 414 CB CG SD CE
REMARK 470 GLU C 416 CB CG CD OE1 OE2
REMARK 470 GLU C 419 CG CD OE1 OE2
REMARK 470 LYS C 439 CB CG CD CE NZ
REMARK 470 LYS C 458 CB CG CD CE NZ
REMARK 470 ILE C 459 CG1 CG2 CD1
REMARK 470 LYS C 505 CG CD CE NZ
REMARK 470 LYS C 506 CG CD CE NZ
REMARK 470 GLN C 508 CG CD OE1 NE2
REMARK 470 LYS C 509 CG CD CE NZ
REMARK 470 SER C 510 OG
REMARK 470 LYS C 511 CG CD CE NZ
REMARK 470 VAL C 514 CG1 CG2
REMARK 470 PHE C 515 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER C 516 OG
REMARK 470 LEU C 518 CG CD1 CD2
REMARK 470 ASP C 519 CG OD1 OD2
REMARK 470 LEU C 521 CG CD1 CD2
REMARK 470 TYR C 523 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 524 CG CD OE1 OE2
REMARK 470 ILE C 525 CG1 CG2 CD1
REMARK 470 LEU C 540 CG CD1 CD2
REMARK 470 LEU C 542 CG CD1 CD2
REMARK 470 ARG C 594 CG CD NE CZ NH1 NH2
REMARK 470 SER C 595 OG
REMARK 470 LEU C 596 CG CD1 CD2
REMARK 470 ARG C 599 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 623 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 624 CG CD1 CD2
REMARK 470 VAL C 626 CG1 CG2
REMARK 470 GLU C 627 CG CD OE1 OE2
REMARK 470 MET C 629 CG SD CE
REMARK 470 SER C 631 OG
REMARK 470 ILE C 633 CG1 CG2 CD1
REMARK 470 GLU C 634 CG CD OE1 OE2
REMARK 470 GLU C 637 CG CD OE1 OE2
REMARK 470 ASP C 638 CG OD1 OD2
REMARK 470 LYS C 641 CG CD CE NZ
REMARK 470 GLN C 642 CG CD OE1 NE2
REMARK 470 THR C 643 CB OG1 CG2
REMARK 470 TYR C 647 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER C 652 OG
REMARK 470 GLU C 657 CG CD OE1 OE2
REMARK 470 ARG C 661 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 663 CG CD CE NZ
REMARK 470 LYS C 695 CG CD CE NZ
REMARK 470 LYS C 697 CB CG CD CE NZ
REMARK 470 ARG C 715 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 716 CG CD CE NZ
REMARK 470 LEU C 727 CG CD1 CD2
REMARK 470 SER C 741 OG
REMARK 470 LYS C 770 CG CD CE NZ
REMARK 470 GLU C 772 CG CD OE1 OE2
REMARK 470 LYS C 776 CG CD CE NZ
REMARK 470 ASP C 777 CG OD1 OD2
REMARK 470 SER C 778 OG
REMARK 470 LYS C 781 CG CD CE NZ
REMARK 470 LYS C 783 CG CD CE NZ
REMARK 470 THR C 784 OG1 CG2
REMARK 470 SER C 785 OG
REMARK 470 LEU C 787 CG CD1 CD2
REMARK 470 VAL C 792 CG1 CG2
REMARK 470 VAL C 795 CG1 CG2
REMARK 470 PHE C 814 CG CD1 CD2 CE1 CE2 CZ
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 ND2 ASN C 353 C2 NAG C 1001 2.17
REMARK 500 SG CYS B 718 CB CYS B 773 2.17
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 GLN A 63 -33.76 63.67
REMARK 500 LYS A 186 -131.28 56.69
REMARK 500 ILE A 369 -61.84 -93.06
REMARK 500 LYS A 377 -116.49 50.40
REMARK 500 ASP A 386 -17.43 68.25
REMARK 500 PRO A 404 37.06 -97.24
REMARK 500 LYS A 410 -18.22 78.05
REMARK 500 TYR A 450 -74.05 -56.66
REMARK 500 LYS A 458 -1.00 74.59
REMARK 500 PRO A 478 77.68 -66.11
REMARK 500 LYS A 511 59.97 -141.37
REMARK 500 GLU A 634 -10.56 63.94
REMARK 500 PRO A 717 41.14 -91.11
REMARK 500 ASP B 21 -61.06 -107.00
REMARK 500 ARG B 139 -76.63 -103.30
REMARK 500 LEU B 192 -72.74 -94.55
REMARK 500 ASP B 193 79.24 55.39
REMARK 500 ASN B 353 70.34 50.13
REMARK 500 LYS B 377 -16.63 67.12
REMARK 500 THR B 383 -123.89 47.06
REMARK 500 PRO B 404 37.20 -97.51
REMARK 500 LYS B 458 1.52 81.00
REMARK 500 PRO B 478 77.67 -66.30
REMARK 500 PRO B 717 40.10 -91.26
REMARK 500 ALA B 775 -74.09 -84.33
REMARK 500 LYS B 783 -6.21 66.68
REMARK 500 ASP D 21 -60.14 -108.50
REMARK 500 ASN D 168 -14.81 65.86
REMARK 500 LYS D 170 -17.67 71.94
REMARK 500 LYS D 377 -116.06 53.41
REMARK 500 GLN D 392 -6.58 63.64
REMARK 500 PRO D 404 36.04 -98.61
REMARK 500 ASN D 411 -5.15 -57.43
REMARK 500 TYR D 450 -73.70 -55.77
REMARK 500 PRO D 478 78.38 -67.91
REMARK 500 ARG D 628 -12.01 65.17
REMARK 500 PRO D 717 39.25 -91.77
REMARK 500 ASP D 777 -119.14 56.62
REMARK 500 SER D 785 -128.12 49.45
REMARK 500 LEU D 789 -70.42 -131.57
REMARK 500 ASP C 21 -60.86 -106.21
REMARK 500 LEU C 192 -63.48 -91.64
REMARK 500 ASP C 193 76.63 53.15
REMARK 500 ILE C 369 -60.21 -92.60
REMARK 500 PRO C 404 37.96 -96.75
REMARK 500 LYS C 410 -15.52 82.37
REMARK 500 TYR C 450 -179.24 -64.07
REMARK 500 ALA C 452 160.18 179.35
REMARK 500 PRO C 478 77.72 -67.14
REMARK 500 LEU C 596 -16.50 67.40
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4U2P A 8 826 UNP P19491 GRIA2_RAT 25 847
DBREF 4U2P B 8 826 UNP P19491 GRIA2_RAT 25 847
DBREF 4U2P D 8 826 UNP P19491 GRIA2_RAT 25 847
DBREF 4U2P C 8 826 UNP P19491 GRIA2_RAT 25 847
SEQADV 4U2P GLU A 239 UNP P19491 ASN 256 CONFLICT
SEQADV 4U2P A UNP P19491 LEU 402 DELETION
SEQADV 4U2P A UNP P19491 PRO 403 DELETION
SEQADV 4U2P A UNP P19491 SER 404 DELETION
SEQADV 4U2P A UNP P19491 GLY 405 DELETION
SEQADV 4U2P ASP A 385 UNP P19491 ASN 406 CONFLICT
SEQADV 4U2P GLN A 392 UNP P19491 ASN 413 CONFLICT
SEQADV 4U2P ALA A 528 UNP P19491 CYS 549 CONFLICT
SEQADV 4U2P PHE A 585 UNP P19491 MET 606 CONFLICT
SEQADV 4U2P ALA A 589 UNP P19491 CYS 610 CONFLICT
SEQADV 4U2P ALA A 598 UNP P19491 GLY 619 CONFLICT
SEQADV 4U2P ALA A 602 UNP P19491 GLY 623 CONFLICT
SEQADV 4U2P ALA A 815 UNP P19491 CYS 836 CONFLICT
SEQADV 4U2P GLY A 827 UNP P19491 EXPRESSION TAG
SEQADV 4U2P LEU A 828 UNP P19491 EXPRESSION TAG
SEQADV 4U2P VAL A 829 UNP P19491 EXPRESSION TAG
SEQADV 4U2P PRO A 830 UNP P19491 EXPRESSION TAG
SEQADV 4U2P ARG A 831 UNP P19491 EXPRESSION TAG
SEQADV 4U2P GLU B 239 UNP P19491 ASN 256 CONFLICT
SEQADV 4U2P B UNP P19491 LEU 402 DELETION
SEQADV 4U2P B UNP P19491 PRO 403 DELETION
SEQADV 4U2P B UNP P19491 SER 404 DELETION
SEQADV 4U2P B UNP P19491 GLY 405 DELETION
SEQADV 4U2P ASP B 385 UNP P19491 ASN 406 CONFLICT
SEQADV 4U2P GLN B 392 UNP P19491 ASN 413 CONFLICT
SEQADV 4U2P ALA B 528 UNP P19491 CYS 549 CONFLICT
SEQADV 4U2P PHE B 585 UNP P19491 MET 606 CONFLICT
SEQADV 4U2P ALA B 589 UNP P19491 CYS 610 CONFLICT
SEQADV 4U2P ALA B 598 UNP P19491 GLY 619 CONFLICT
SEQADV 4U2P ALA B 602 UNP P19491 GLY 623 CONFLICT
SEQADV 4U2P ALA B 815 UNP P19491 CYS 836 CONFLICT
SEQADV 4U2P GLY B 827 UNP P19491 EXPRESSION TAG
SEQADV 4U2P LEU B 828 UNP P19491 EXPRESSION TAG
SEQADV 4U2P VAL B 829 UNP P19491 EXPRESSION TAG
SEQADV 4U2P PRO B 830 UNP P19491 EXPRESSION TAG
SEQADV 4U2P ARG B 831 UNP P19491 EXPRESSION TAG
SEQADV 4U2P GLU D 239 UNP P19491 ASN 256 CONFLICT
SEQADV 4U2P D UNP P19491 LEU 402 DELETION
SEQADV 4U2P D UNP P19491 PRO 403 DELETION
SEQADV 4U2P D UNP P19491 SER 404 DELETION
SEQADV 4U2P D UNP P19491 GLY 405 DELETION
SEQADV 4U2P ASP D 385 UNP P19491 ASN 406 CONFLICT
SEQADV 4U2P GLN D 392 UNP P19491 ASN 413 CONFLICT
SEQADV 4U2P ALA D 528 UNP P19491 CYS 549 CONFLICT
SEQADV 4U2P PHE D 585 UNP P19491 MET 606 CONFLICT
SEQADV 4U2P ALA D 589 UNP P19491 CYS 610 CONFLICT
SEQADV 4U2P ALA D 598 UNP P19491 GLY 619 CONFLICT
SEQADV 4U2P ALA D 602 UNP P19491 GLY 623 CONFLICT
SEQADV 4U2P ALA D 815 UNP P19491 CYS 836 CONFLICT
SEQADV 4U2P GLY D 827 UNP P19491 EXPRESSION TAG
SEQADV 4U2P LEU D 828 UNP P19491 EXPRESSION TAG
SEQADV 4U2P VAL D 829 UNP P19491 EXPRESSION TAG
SEQADV 4U2P PRO D 830 UNP P19491 EXPRESSION TAG
SEQADV 4U2P ARG D 831 UNP P19491 EXPRESSION TAG
SEQADV 4U2P GLU C 239 UNP P19491 ASN 256 CONFLICT
SEQADV 4U2P C UNP P19491 LEU 402 DELETION
SEQADV 4U2P C UNP P19491 PRO 403 DELETION
SEQADV 4U2P C UNP P19491 SER 404 DELETION
SEQADV 4U2P C UNP P19491 GLY 405 DELETION
SEQADV 4U2P ASP C 385 UNP P19491 ASN 406 CONFLICT
SEQADV 4U2P GLN C 392 UNP P19491 ASN 413 CONFLICT
SEQADV 4U2P ALA C 528 UNP P19491 CYS 549 CONFLICT
SEQADV 4U2P PHE C 585 UNP P19491 MET 606 CONFLICT
SEQADV 4U2P ALA C 589 UNP P19491 CYS 610 CONFLICT
SEQADV 4U2P ALA C 598 UNP P19491 GLY 619 CONFLICT
SEQADV 4U2P ALA C 602 UNP P19491 GLY 623 CONFLICT
SEQADV 4U2P ALA C 815 UNP P19491 CYS 836 CONFLICT
SEQADV 4U2P GLY C 827 UNP P19491 EXPRESSION TAG
SEQADV 4U2P LEU C 828 UNP P19491 EXPRESSION TAG
SEQADV 4U2P VAL C 829 UNP P19491 EXPRESSION TAG
SEQADV 4U2P PRO C 830 UNP P19491 EXPRESSION TAG
SEQADV 4U2P ARG C 831 UNP P19491 EXPRESSION TAG
SEQRES 1 A 824 ASN SER ILE GLN ILE GLY GLY LEU PHE PRO ARG GLY ALA
SEQRES 2 A 824 ASP GLN GLU TYR SER ALA PHE ARG VAL GLY MET VAL GLN
SEQRES 3 A 824 PHE SER THR SER GLU PHE ARG LEU THR PRO HIS ILE ASP
SEQRES 4 A 824 ASN LEU GLU VAL ALA ASN SER PHE ALA VAL THR ASN ALA
SEQRES 5 A 824 PHE CYS SER GLN PHE SER ARG GLY VAL TYR ALA ILE PHE
SEQRES 6 A 824 GLY PHE TYR ASP LYS LYS SER VAL ASN THR ILE THR SER
SEQRES 7 A 824 PHE CYS GLY THR LEU HIS VAL SER PHE ILE THR PRO SER
SEQRES 8 A 824 PHE PRO THR ASP GLY THR HIS PRO PHE VAL ILE GLN MET
SEQRES 9 A 824 ARG PRO ASP LEU LYS GLY ALA LEU LEU SER LEU ILE GLU
SEQRES 10 A 824 TYR TYR GLN TRP ASP LYS PHE ALA TYR LEU TYR ASP SER
SEQRES 11 A 824 ASP ARG GLY LEU SER THR LEU GLN ALA VAL LEU ASP SER
SEQRES 12 A 824 ALA ALA GLU LYS LYS TRP GLN VAL THR ALA ILE ASN VAL
SEQRES 13 A 824 GLY ASN ILE ASN ASN ASP LYS LYS ASP GLU THR TYR ARG
SEQRES 14 A 824 SER LEU PHE GLN ASP LEU GLU LEU LYS LYS GLU ARG ARG
SEQRES 15 A 824 VAL ILE LEU ASP CYS GLU ARG ASP LYS VAL ASN ASP ILE
SEQRES 16 A 824 VAL ASP GLN VAL ILE THR ILE GLY LYS HIS VAL LYS GLY
SEQRES 17 A 824 TYR HIS TYR ILE ILE ALA ASN LEU GLY PHE THR ASP GLY
SEQRES 18 A 824 ASP LEU LEU LYS ILE GLN PHE GLY GLY ALA GLU VAL SER
SEQRES 19 A 824 GLY PHE GLN ILE VAL ASP TYR ASP ASP SER LEU VAL SER
SEQRES 20 A 824 LYS PHE ILE GLU ARG TRP SER THR LEU GLU GLU LYS GLU
SEQRES 21 A 824 TYR PRO GLY ALA HIS THR ALA THR ILE LYS TYR THR SER
SEQRES 22 A 824 ALA LEU THR TYR ASP ALA VAL GLN VAL MET THR GLU ALA
SEQRES 23 A 824 PHE ARG ASN LEU ARG LYS GLN ARG ILE GLU ILE SER ARG
SEQRES 24 A 824 ARG GLY ASN ALA GLY ASP CYS LEU ALA ASN PRO ALA VAL
SEQRES 25 A 824 PRO TRP GLY GLN GLY VAL GLU ILE GLU ARG ALA LEU LYS
SEQRES 26 A 824 GLN VAL GLN VAL GLU GLY LEU SER GLY ASN ILE LYS PHE
SEQRES 27 A 824 ASP GLN ASN GLY LYS ARG ILE ASN TYR THR ILE ASN ILE
SEQRES 28 A 824 MET GLU LEU LYS THR ASN GLY PRO ARG LYS ILE GLY TYR
SEQRES 29 A 824 TRP SER GLU VAL ASP LYS MET VAL VAL THR LEU THR GLU
SEQRES 30 A 824 ASP ASP THR SER GLY LEU GLU GLN LYS THR VAL VAL VAL
SEQRES 31 A 824 THR THR ILE LEU GLU SER PRO TYR VAL MET MET LYS LYS
SEQRES 32 A 824 ASN HIS GLU MET LEU GLU GLY ASN GLU ARG TYR GLU GLY
SEQRES 33 A 824 TYR CYS VAL ASP LEU ALA ALA GLU ILE ALA LYS HIS CYS
SEQRES 34 A 824 GLY PHE LYS TYR LYS LEU THR ILE VAL GLY ASP GLY LYS
SEQRES 35 A 824 TYR GLY ALA ARG ASP ALA ASP THR LYS ILE TRP ASN GLY
SEQRES 36 A 824 MET VAL GLY GLU LEU VAL TYR GLY LYS ALA ASP ILE ALA
SEQRES 37 A 824 ILE ALA PRO LEU THR ILE THR LEU VAL ARG GLU GLU VAL
SEQRES 38 A 824 ILE ASP PHE SER LYS PRO PHE MET SER LEU GLY ILE SER
SEQRES 39 A 824 ILE MET ILE LYS LYS PRO GLN LYS SER LYS PRO GLY VAL
SEQRES 40 A 824 PHE SER PHE LEU ASP PRO LEU ALA TYR GLU ILE TRP MET
SEQRES 41 A 824 ALA ILE VAL PHE ALA TYR ILE GLY VAL SER VAL VAL LEU
SEQRES 42 A 824 PHE LEU VAL SER ARG PHE SER PRO TYR GLU TRP HIS THR
SEQRES 43 A 824 GLU GLU PHE GLU ASP GLY ARG GLU THR GLN SER SER GLU
SEQRES 44 A 824 SER THR ASN GLU PHE GLY ILE PHE ASN SER LEU TRP PHE
SEQRES 45 A 824 SER LEU GLY ALA PHE PHE GLN GLN GLY ALA ASP ILE SER
SEQRES 46 A 824 PRO ARG SER LEU SER ALA ARG ILE VAL ALA GLY VAL TRP
SEQRES 47 A 824 TRP PHE PHE THR LEU ILE ILE ILE SER SER TYR THR ALA
SEQRES 48 A 824 ASN LEU ALA ALA PHE LEU THR VAL GLU ARG MET VAL SER
SEQRES 49 A 824 PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU
SEQRES 50 A 824 ILE ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU
SEQRES 51 A 824 PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET
SEQRES 52 A 824 TRP THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL
SEQRES 53 A 824 ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER
SEQRES 54 A 824 LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN
SEQRES 55 A 824 GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS
SEQRES 56 A 824 VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA
SEQRES 57 A 824 THR PRO LYS GLY SER SER LEU GLY THR PRO VAL ASN LEU
SEQRES 58 A 824 ALA VAL LEU LYS LEU SER GLU GLN GLY VAL LEU ASP LYS
SEQRES 59 A 824 LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS GLY
SEQRES 60 A 824 ALA LYS ASP SER GLY SER LYS GLU LYS THR SER ALA LEU
SEQRES 61 A 824 SER LEU SER ASN VAL ALA GLY VAL PHE TYR ILE LEU VAL
SEQRES 62 A 824 GLY GLY LEU GLY LEU ALA MET LEU VAL ALA LEU ILE GLU
SEQRES 63 A 824 PHE ALA TYR LYS SER ARG ALA GLU ALA LYS ARG MET LYS
SEQRES 64 A 824 GLY LEU VAL PRO ARG
SEQRES 1 B 824 ASN SER ILE GLN ILE GLY GLY LEU PHE PRO ARG GLY ALA
SEQRES 2 B 824 ASP GLN GLU TYR SER ALA PHE ARG VAL GLY MET VAL GLN
SEQRES 3 B 824 PHE SER THR SER GLU PHE ARG LEU THR PRO HIS ILE ASP
SEQRES 4 B 824 ASN LEU GLU VAL ALA ASN SER PHE ALA VAL THR ASN ALA
SEQRES 5 B 824 PHE CYS SER GLN PHE SER ARG GLY VAL TYR ALA ILE PHE
SEQRES 6 B 824 GLY PHE TYR ASP LYS LYS SER VAL ASN THR ILE THR SER
SEQRES 7 B 824 PHE CYS GLY THR LEU HIS VAL SER PHE ILE THR PRO SER
SEQRES 8 B 824 PHE PRO THR ASP GLY THR HIS PRO PHE VAL ILE GLN MET
SEQRES 9 B 824 ARG PRO ASP LEU LYS GLY ALA LEU LEU SER LEU ILE GLU
SEQRES 10 B 824 TYR TYR GLN TRP ASP LYS PHE ALA TYR LEU TYR ASP SER
SEQRES 11 B 824 ASP ARG GLY LEU SER THR LEU GLN ALA VAL LEU ASP SER
SEQRES 12 B 824 ALA ALA GLU LYS LYS TRP GLN VAL THR ALA ILE ASN VAL
SEQRES 13 B 824 GLY ASN ILE ASN ASN ASP LYS LYS ASP GLU THR TYR ARG
SEQRES 14 B 824 SER LEU PHE GLN ASP LEU GLU LEU LYS LYS GLU ARG ARG
SEQRES 15 B 824 VAL ILE LEU ASP CYS GLU ARG ASP LYS VAL ASN ASP ILE
SEQRES 16 B 824 VAL ASP GLN VAL ILE THR ILE GLY LYS HIS VAL LYS GLY
SEQRES 17 B 824 TYR HIS TYR ILE ILE ALA ASN LEU GLY PHE THR ASP GLY
SEQRES 18 B 824 ASP LEU LEU LYS ILE GLN PHE GLY GLY ALA GLU VAL SER
SEQRES 19 B 824 GLY PHE GLN ILE VAL ASP TYR ASP ASP SER LEU VAL SER
SEQRES 20 B 824 LYS PHE ILE GLU ARG TRP SER THR LEU GLU GLU LYS GLU
SEQRES 21 B 824 TYR PRO GLY ALA HIS THR ALA THR ILE LYS TYR THR SER
SEQRES 22 B 824 ALA LEU THR TYR ASP ALA VAL GLN VAL MET THR GLU ALA
SEQRES 23 B 824 PHE ARG ASN LEU ARG LYS GLN ARG ILE GLU ILE SER ARG
SEQRES 24 B 824 ARG GLY ASN ALA GLY ASP CYS LEU ALA ASN PRO ALA VAL
SEQRES 25 B 824 PRO TRP GLY GLN GLY VAL GLU ILE GLU ARG ALA LEU LYS
SEQRES 26 B 824 GLN VAL GLN VAL GLU GLY LEU SER GLY ASN ILE LYS PHE
SEQRES 27 B 824 ASP GLN ASN GLY LYS ARG ILE ASN TYR THR ILE ASN ILE
SEQRES 28 B 824 MET GLU LEU LYS THR ASN GLY PRO ARG LYS ILE GLY TYR
SEQRES 29 B 824 TRP SER GLU VAL ASP LYS MET VAL VAL THR LEU THR GLU
SEQRES 30 B 824 ASP ASP THR SER GLY LEU GLU GLN LYS THR VAL VAL VAL
SEQRES 31 B 824 THR THR ILE LEU GLU SER PRO TYR VAL MET MET LYS LYS
SEQRES 32 B 824 ASN HIS GLU MET LEU GLU GLY ASN GLU ARG TYR GLU GLY
SEQRES 33 B 824 TYR CYS VAL ASP LEU ALA ALA GLU ILE ALA LYS HIS CYS
SEQRES 34 B 824 GLY PHE LYS TYR LYS LEU THR ILE VAL GLY ASP GLY LYS
SEQRES 35 B 824 TYR GLY ALA ARG ASP ALA ASP THR LYS ILE TRP ASN GLY
SEQRES 36 B 824 MET VAL GLY GLU LEU VAL TYR GLY LYS ALA ASP ILE ALA
SEQRES 37 B 824 ILE ALA PRO LEU THR ILE THR LEU VAL ARG GLU GLU VAL
SEQRES 38 B 824 ILE ASP PHE SER LYS PRO PHE MET SER LEU GLY ILE SER
SEQRES 39 B 824 ILE MET ILE LYS LYS PRO GLN LYS SER LYS PRO GLY VAL
SEQRES 40 B 824 PHE SER PHE LEU ASP PRO LEU ALA TYR GLU ILE TRP MET
SEQRES 41 B 824 ALA ILE VAL PHE ALA TYR ILE GLY VAL SER VAL VAL LEU
SEQRES 42 B 824 PHE LEU VAL SER ARG PHE SER PRO TYR GLU TRP HIS THR
SEQRES 43 B 824 GLU GLU PHE GLU ASP GLY ARG GLU THR GLN SER SER GLU
SEQRES 44 B 824 SER THR ASN GLU PHE GLY ILE PHE ASN SER LEU TRP PHE
SEQRES 45 B 824 SER LEU GLY ALA PHE PHE GLN GLN GLY ALA ASP ILE SER
SEQRES 46 B 824 PRO ARG SER LEU SER ALA ARG ILE VAL ALA GLY VAL TRP
SEQRES 47 B 824 TRP PHE PHE THR LEU ILE ILE ILE SER SER TYR THR ALA
SEQRES 48 B 824 ASN LEU ALA ALA PHE LEU THR VAL GLU ARG MET VAL SER
SEQRES 49 B 824 PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU
SEQRES 50 B 824 ILE ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU
SEQRES 51 B 824 PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET
SEQRES 52 B 824 TRP THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL
SEQRES 53 B 824 ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER
SEQRES 54 B 824 LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN
SEQRES 55 B 824 GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS
SEQRES 56 B 824 VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA
SEQRES 57 B 824 THR PRO LYS GLY SER SER LEU GLY THR PRO VAL ASN LEU
SEQRES 58 B 824 ALA VAL LEU LYS LEU SER GLU GLN GLY VAL LEU ASP LYS
SEQRES 59 B 824 LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS GLY
SEQRES 60 B 824 ALA LYS ASP SER GLY SER LYS GLU LYS THR SER ALA LEU
SEQRES 61 B 824 SER LEU SER ASN VAL ALA GLY VAL PHE TYR ILE LEU VAL
SEQRES 62 B 824 GLY GLY LEU GLY LEU ALA MET LEU VAL ALA LEU ILE GLU
SEQRES 63 B 824 PHE ALA TYR LYS SER ARG ALA GLU ALA LYS ARG MET LYS
SEQRES 64 B 824 GLY LEU VAL PRO ARG
SEQRES 1 D 824 ASN SER ILE GLN ILE GLY GLY LEU PHE PRO ARG GLY ALA
SEQRES 2 D 824 ASP GLN GLU TYR SER ALA PHE ARG VAL GLY MET VAL GLN
SEQRES 3 D 824 PHE SER THR SER GLU PHE ARG LEU THR PRO HIS ILE ASP
SEQRES 4 D 824 ASN LEU GLU VAL ALA ASN SER PHE ALA VAL THR ASN ALA
SEQRES 5 D 824 PHE CYS SER GLN PHE SER ARG GLY VAL TYR ALA ILE PHE
SEQRES 6 D 824 GLY PHE TYR ASP LYS LYS SER VAL ASN THR ILE THR SER
SEQRES 7 D 824 PHE CYS GLY THR LEU HIS VAL SER PHE ILE THR PRO SER
SEQRES 8 D 824 PHE PRO THR ASP GLY THR HIS PRO PHE VAL ILE GLN MET
SEQRES 9 D 824 ARG PRO ASP LEU LYS GLY ALA LEU LEU SER LEU ILE GLU
SEQRES 10 D 824 TYR TYR GLN TRP ASP LYS PHE ALA TYR LEU TYR ASP SER
SEQRES 11 D 824 ASP ARG GLY LEU SER THR LEU GLN ALA VAL LEU ASP SER
SEQRES 12 D 824 ALA ALA GLU LYS LYS TRP GLN VAL THR ALA ILE ASN VAL
SEQRES 13 D 824 GLY ASN ILE ASN ASN ASP LYS LYS ASP GLU THR TYR ARG
SEQRES 14 D 824 SER LEU PHE GLN ASP LEU GLU LEU LYS LYS GLU ARG ARG
SEQRES 15 D 824 VAL ILE LEU ASP CYS GLU ARG ASP LYS VAL ASN ASP ILE
SEQRES 16 D 824 VAL ASP GLN VAL ILE THR ILE GLY LYS HIS VAL LYS GLY
SEQRES 17 D 824 TYR HIS TYR ILE ILE ALA ASN LEU GLY PHE THR ASP GLY
SEQRES 18 D 824 ASP LEU LEU LYS ILE GLN PHE GLY GLY ALA GLU VAL SER
SEQRES 19 D 824 GLY PHE GLN ILE VAL ASP TYR ASP ASP SER LEU VAL SER
SEQRES 20 D 824 LYS PHE ILE GLU ARG TRP SER THR LEU GLU GLU LYS GLU
SEQRES 21 D 824 TYR PRO GLY ALA HIS THR ALA THR ILE LYS TYR THR SER
SEQRES 22 D 824 ALA LEU THR TYR ASP ALA VAL GLN VAL MET THR GLU ALA
SEQRES 23 D 824 PHE ARG ASN LEU ARG LYS GLN ARG ILE GLU ILE SER ARG
SEQRES 24 D 824 ARG GLY ASN ALA GLY ASP CYS LEU ALA ASN PRO ALA VAL
SEQRES 25 D 824 PRO TRP GLY GLN GLY VAL GLU ILE GLU ARG ALA LEU LYS
SEQRES 26 D 824 GLN VAL GLN VAL GLU GLY LEU SER GLY ASN ILE LYS PHE
SEQRES 27 D 824 ASP GLN ASN GLY LYS ARG ILE ASN TYR THR ILE ASN ILE
SEQRES 28 D 824 MET GLU LEU LYS THR ASN GLY PRO ARG LYS ILE GLY TYR
SEQRES 29 D 824 TRP SER GLU VAL ASP LYS MET VAL VAL THR LEU THR GLU
SEQRES 30 D 824 ASP ASP THR SER GLY LEU GLU GLN LYS THR VAL VAL VAL
SEQRES 31 D 824 THR THR ILE LEU GLU SER PRO TYR VAL MET MET LYS LYS
SEQRES 32 D 824 ASN HIS GLU MET LEU GLU GLY ASN GLU ARG TYR GLU GLY
SEQRES 33 D 824 TYR CYS VAL ASP LEU ALA ALA GLU ILE ALA LYS HIS CYS
SEQRES 34 D 824 GLY PHE LYS TYR LYS LEU THR ILE VAL GLY ASP GLY LYS
SEQRES 35 D 824 TYR GLY ALA ARG ASP ALA ASP THR LYS ILE TRP ASN GLY
SEQRES 36 D 824 MET VAL GLY GLU LEU VAL TYR GLY LYS ALA ASP ILE ALA
SEQRES 37 D 824 ILE ALA PRO LEU THR ILE THR LEU VAL ARG GLU GLU VAL
SEQRES 38 D 824 ILE ASP PHE SER LYS PRO PHE MET SER LEU GLY ILE SER
SEQRES 39 D 824 ILE MET ILE LYS LYS PRO GLN LYS SER LYS PRO GLY VAL
SEQRES 40 D 824 PHE SER PHE LEU ASP PRO LEU ALA TYR GLU ILE TRP MET
SEQRES 41 D 824 ALA ILE VAL PHE ALA TYR ILE GLY VAL SER VAL VAL LEU
SEQRES 42 D 824 PHE LEU VAL SER ARG PHE SER PRO TYR GLU TRP HIS THR
SEQRES 43 D 824 GLU GLU PHE GLU ASP GLY ARG GLU THR GLN SER SER GLU
SEQRES 44 D 824 SER THR ASN GLU PHE GLY ILE PHE ASN SER LEU TRP PHE
SEQRES 45 D 824 SER LEU GLY ALA PHE PHE GLN GLN GLY ALA ASP ILE SER
SEQRES 46 D 824 PRO ARG SER LEU SER ALA ARG ILE VAL ALA GLY VAL TRP
SEQRES 47 D 824 TRP PHE PHE THR LEU ILE ILE ILE SER SER TYR THR ALA
SEQRES 48 D 824 ASN LEU ALA ALA PHE LEU THR VAL GLU ARG MET VAL SER
SEQRES 49 D 824 PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU
SEQRES 50 D 824 ILE ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU
SEQRES 51 D 824 PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET
SEQRES 52 D 824 TRP THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL
SEQRES 53 D 824 ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER
SEQRES 54 D 824 LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN
SEQRES 55 D 824 GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS
SEQRES 56 D 824 VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA
SEQRES 57 D 824 THR PRO LYS GLY SER SER LEU GLY THR PRO VAL ASN LEU
SEQRES 58 D 824 ALA VAL LEU LYS LEU SER GLU GLN GLY VAL LEU ASP LYS
SEQRES 59 D 824 LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS GLY
SEQRES 60 D 824 ALA LYS ASP SER GLY SER LYS GLU LYS THR SER ALA LEU
SEQRES 61 D 824 SER LEU SER ASN VAL ALA GLY VAL PHE TYR ILE LEU VAL
SEQRES 62 D 824 GLY GLY LEU GLY LEU ALA MET LEU VAL ALA LEU ILE GLU
SEQRES 63 D 824 PHE ALA TYR LYS SER ARG ALA GLU ALA LYS ARG MET LYS
SEQRES 64 D 824 GLY LEU VAL PRO ARG
SEQRES 1 C 824 ASN SER ILE GLN ILE GLY GLY LEU PHE PRO ARG GLY ALA
SEQRES 2 C 824 ASP GLN GLU TYR SER ALA PHE ARG VAL GLY MET VAL GLN
SEQRES 3 C 824 PHE SER THR SER GLU PHE ARG LEU THR PRO HIS ILE ASP
SEQRES 4 C 824 ASN LEU GLU VAL ALA ASN SER PHE ALA VAL THR ASN ALA
SEQRES 5 C 824 PHE CYS SER GLN PHE SER ARG GLY VAL TYR ALA ILE PHE
SEQRES 6 C 824 GLY PHE TYR ASP LYS LYS SER VAL ASN THR ILE THR SER
SEQRES 7 C 824 PHE CYS GLY THR LEU HIS VAL SER PHE ILE THR PRO SER
SEQRES 8 C 824 PHE PRO THR ASP GLY THR HIS PRO PHE VAL ILE GLN MET
SEQRES 9 C 824 ARG PRO ASP LEU LYS GLY ALA LEU LEU SER LEU ILE GLU
SEQRES 10 C 824 TYR TYR GLN TRP ASP LYS PHE ALA TYR LEU TYR ASP SER
SEQRES 11 C 824 ASP ARG GLY LEU SER THR LEU GLN ALA VAL LEU ASP SER
SEQRES 12 C 824 ALA ALA GLU LYS LYS TRP GLN VAL THR ALA ILE ASN VAL
SEQRES 13 C 824 GLY ASN ILE ASN ASN ASP LYS LYS ASP GLU THR TYR ARG
SEQRES 14 C 824 SER LEU PHE GLN ASP LEU GLU LEU LYS LYS GLU ARG ARG
SEQRES 15 C 824 VAL ILE LEU ASP CYS GLU ARG ASP LYS VAL ASN ASP ILE
SEQRES 16 C 824 VAL ASP GLN VAL ILE THR ILE GLY LYS HIS VAL LYS GLY
SEQRES 17 C 824 TYR HIS TYR ILE ILE ALA ASN LEU GLY PHE THR ASP GLY
SEQRES 18 C 824 ASP LEU LEU LYS ILE GLN PHE GLY GLY ALA GLU VAL SER
SEQRES 19 C 824 GLY PHE GLN ILE VAL ASP TYR ASP ASP SER LEU VAL SER
SEQRES 20 C 824 LYS PHE ILE GLU ARG TRP SER THR LEU GLU GLU LYS GLU
SEQRES 21 C 824 TYR PRO GLY ALA HIS THR ALA THR ILE LYS TYR THR SER
SEQRES 22 C 824 ALA LEU THR TYR ASP ALA VAL GLN VAL MET THR GLU ALA
SEQRES 23 C 824 PHE ARG ASN LEU ARG LYS GLN ARG ILE GLU ILE SER ARG
SEQRES 24 C 824 ARG GLY ASN ALA GLY ASP CYS LEU ALA ASN PRO ALA VAL
SEQRES 25 C 824 PRO TRP GLY GLN GLY VAL GLU ILE GLU ARG ALA LEU LYS
SEQRES 26 C 824 GLN VAL GLN VAL GLU GLY LEU SER GLY ASN ILE LYS PHE
SEQRES 27 C 824 ASP GLN ASN GLY LYS ARG ILE ASN TYR THR ILE ASN ILE
SEQRES 28 C 824 MET GLU LEU LYS THR ASN GLY PRO ARG LYS ILE GLY TYR
SEQRES 29 C 824 TRP SER GLU VAL ASP LYS MET VAL VAL THR LEU THR GLU
SEQRES 30 C 824 ASP ASP THR SER GLY LEU GLU GLN LYS THR VAL VAL VAL
SEQRES 31 C 824 THR THR ILE LEU GLU SER PRO TYR VAL MET MET LYS LYS
SEQRES 32 C 824 ASN HIS GLU MET LEU GLU GLY ASN GLU ARG TYR GLU GLY
SEQRES 33 C 824 TYR CYS VAL ASP LEU ALA ALA GLU ILE ALA LYS HIS CYS
SEQRES 34 C 824 GLY PHE LYS TYR LYS LEU THR ILE VAL GLY ASP GLY LYS
SEQRES 35 C 824 TYR GLY ALA ARG ASP ALA ASP THR LYS ILE TRP ASN GLY
SEQRES 36 C 824 MET VAL GLY GLU LEU VAL TYR GLY LYS ALA ASP ILE ALA
SEQRES 37 C 824 ILE ALA PRO LEU THR ILE THR LEU VAL ARG GLU GLU VAL
SEQRES 38 C 824 ILE ASP PHE SER LYS PRO PHE MET SER LEU GLY ILE SER
SEQRES 39 C 824 ILE MET ILE LYS LYS PRO GLN LYS SER LYS PRO GLY VAL
SEQRES 40 C 824 PHE SER PHE LEU ASP PRO LEU ALA TYR GLU ILE TRP MET
SEQRES 41 C 824 ALA ILE VAL PHE ALA TYR ILE GLY VAL SER VAL VAL LEU
SEQRES 42 C 824 PHE LEU VAL SER ARG PHE SER PRO TYR GLU TRP HIS THR
SEQRES 43 C 824 GLU GLU PHE GLU ASP GLY ARG GLU THR GLN SER SER GLU
SEQRES 44 C 824 SER THR ASN GLU PHE GLY ILE PHE ASN SER LEU TRP PHE
SEQRES 45 C 824 SER LEU GLY ALA PHE PHE GLN GLN GLY ALA ASP ILE SER
SEQRES 46 C 824 PRO ARG SER LEU SER ALA ARG ILE VAL ALA GLY VAL TRP
SEQRES 47 C 824 TRP PHE PHE THR LEU ILE ILE ILE SER SER TYR THR ALA
SEQRES 48 C 824 ASN LEU ALA ALA PHE LEU THR VAL GLU ARG MET VAL SER
SEQRES 49 C 824 PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU
SEQRES 50 C 824 ILE ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU
SEQRES 51 C 824 PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET
SEQRES 52 C 824 TRP THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL
SEQRES 53 C 824 ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER
SEQRES 54 C 824 LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN
SEQRES 55 C 824 GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS
SEQRES 56 C 824 VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA
SEQRES 57 C 824 THR PRO LYS GLY SER SER LEU GLY THR PRO VAL ASN LEU
SEQRES 58 C 824 ALA VAL LEU LYS LEU SER GLU GLN GLY VAL LEU ASP LYS
SEQRES 59 C 824 LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS GLY
SEQRES 60 C 824 ALA LYS ASP SER GLY SER LYS GLU LYS THR SER ALA LEU
SEQRES 61 C 824 SER LEU SER ASN VAL ALA GLY VAL PHE TYR ILE LEU VAL
SEQRES 62 C 824 GLY GLY LEU GLY LEU ALA MET LEU VAL ALA LEU ILE GLU
SEQRES 63 C 824 PHE ALA TYR LYS SER ARG ALA GLU ALA LYS ARG MET LYS
SEQRES 64 C 824 GLY LEU VAL PRO ARG
HET NAG A1001 14
HET MES A1002 12
HET NAG B1001 14
HET MES B1002 12
HET NAG D1001 14
HET MES D1002 12
HET NAG C1001 14
HET MES C1002 12
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
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
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 6 MES 4(C6 H13 N O4 S)
HELIX 1 AA1 ASP A 21 PHE A 34 1 14
HELIX 2 AA2 ASN A 52 SER A 65 1 14
HELIX 3 AA3 SER A 79 HIS A 91 1 13
HELIX 4 AA4 LEU A 115 TYR A 126 1 12
HELIX 5 AA5 LEU A 141 LYS A 155 1 15
HELIX 6 AA6 GLY A 164 ASN A 167 5 4
HELIX 7 AA7 ASN A 168 GLU A 173 1 6
HELIX 8 AA8 TYR A 175 LYS A 185 1 11
HELIX 9 AA9 GLU A 195 GLY A 210 1 16
HELIX 10 AB1 ASP A 250 THR A 262 1 13
HELIX 11 AB2 LYS A 277 GLN A 300 1 24
HELIX 12 AB3 GLY A 322 GLN A 333 1 12
HELIX 13 AB4 ASN A 411 LEU A 415 5 5
HELIX 14 AB5 GLU A 416 GLU A 419 5 4
HELIX 15 AB6 GLY A 423 GLY A 437 1 15
HELIX 16 AB7 MET A 463 TYR A 469 1 7
HELIX 17 AB8 THR A 482 GLU A 487 1 6
HELIX 18 AB9 ALA A 522 ARG A 545 1 24
HELIX 19 AC1 SER A 595 VAL A 630 1 36
HELIX 20 AC2 SER A 635 LYS A 641 1 7
HELIX 21 AC3 GLY A 653 SER A 662 1 10
HELIX 22 AC4 ILE A 664 SER A 676 1 13
HELIX 23 AC5 THR A 685 LYS A 695 1 11
HELIX 24 AC6 SER A 706 GLN A 714 1 9
HELIX 25 AC7 LEU A 742 GLN A 756 1 15
HELIX 26 AC8 GLY A 757 TYR A 768 1 12
HELIX 27 AC9 SER A 788 ALA A 793 1 6
HELIX 28 AD1 ALA A 793 LEU A 811 1 19
HELIX 29 AD2 ASP B 21 PHE B 34 1 14
HELIX 30 AD3 ASN B 52 GLY B 67 1 16
HELIX 31 AD4 SER B 79 HIS B 91 1 13
HELIX 32 AD5 LEU B 115 GLN B 127 1 13
HELIX 33 AD6 LEU B 141 LYS B 155 1 15
HELIX 34 AD7 ASP B 172 LYS B 186 1 15
HELIX 35 AD8 GLU B 195 GLY B 210 1 16
HELIX 36 AD9 LEU B 230 GLN B 234 5 5
HELIX 37 AE1 ASP B 250 SER B 261 1 12
HELIX 38 AE2 LYS B 277 GLN B 300 1 24
HELIX 39 AE3 GLY B 322 GLN B 333 1 12
HELIX 40 AE4 ASN B 411 LEU B 415 5 5
HELIX 41 AE5 GLU B 416 GLU B 419 5 4
HELIX 42 AE6 GLY B 423 GLY B 437 1 15
HELIX 43 AE7 MET B 463 TYR B 469 1 7
HELIX 44 AE8 THR B 482 GLU B 487 1 6
HELIX 45 AE9 ALA B 522 LEU B 542 1 21
HELIX 46 AF1 SER B 595 VAL B 626 1 32
HELIX 47 AF2 GLU B 637 GLN B 642 5 6
HELIX 48 AF3 GLY B 653 SER B 662 1 10
HELIX 49 AF4 ILE B 664 SER B 676 1 13
HELIX 50 AF5 THR B 685 LYS B 695 1 11
HELIX 51 AF6 SER B 706 GLN B 714 1 9
HELIX 52 AF7 LEU B 742 GLN B 756 1 15
HELIX 53 AF8 GLY B 757 TYR B 768 1 12
HELIX 54 AF9 LEU B 789 TYR B 816 1 28
HELIX 55 AG1 ASP D 21 PHE D 34 1 14
HELIX 56 AG2 ASN D 52 GLY D 67 1 16
HELIX 57 AG3 SER D 79 HIS D 91 1 13
HELIX 58 AG4 LEU D 115 GLN D 127 1 13
HELIX 59 AG5 SER D 137 GLY D 140 5 4
HELIX 60 AG6 LEU D 141 LYS D 154 1 14
HELIX 61 AG7 THR D 174 LYS D 186 1 13
HELIX 62 AG8 GLU D 195 GLY D 210 1 16
HELIX 63 AG9 LEU D 230 PHE D 235 1 6
HELIX 64 AH1 ASP D 250 SER D 261 1 12
HELIX 65 AH2 LYS D 277 GLN D 300 1 24
HELIX 66 AH3 GLY D 322 GLN D 333 1 12
HELIX 67 AH4 LYS D 410 LEU D 415 5 6
HELIX 68 AH5 GLY D 417 GLU D 419 5 3
HELIX 69 AH6 GLY D 423 GLY D 437 1 15
HELIX 70 AH7 MET D 463 TYR D 469 1 7
HELIX 71 AH8 THR D 482 VAL D 488 1 7
HELIX 72 AH9 ALA D 522 LEU D 542 1 21
HELIX 73 AI1 SER D 597 GLU D 627 1 31
HELIX 74 AI2 SER D 635 LYS D 641 1 7
HELIX 75 AI3 GLY D 653 SER D 662 1 10
HELIX 76 AI4 ILE D 664 SER D 676 1 13
HELIX 77 AI5 THR D 685 LYS D 695 1 11
HELIX 78 AI6 SER D 706 GLN D 714 1 9
HELIX 79 AI7 LEU D 742 GLN D 756 1 15
HELIX 80 AI8 GLY D 757 TYR D 768 1 12
HELIX 81 AI9 LYS D 776 LYS D 781 5 6
HELIX 82 AJ1 LEU D 789 LEU D 811 1 23
HELIX 83 AJ2 ASP C 21 PHE C 34 1 14
HELIX 84 AJ3 ASN C 52 GLY C 67 1 16
HELIX 85 AJ4 SER C 79 HIS C 91 1 13
HELIX 86 AJ5 LEU C 115 TYR C 126 1 12
HELIX 87 AJ6 LEU C 141 LYS C 155 1 15
HELIX 88 AJ7 THR C 174 LYS C 185 1 12
HELIX 89 AJ8 GLU C 195 GLY C 210 1 16
HELIX 90 AJ9 LEU C 230 PHE C 235 1 6
HELIX 91 AK1 ASP C 250 SER C 261 1 12
HELIX 92 AK2 LYS C 277 GLN C 300 1 24
HELIX 93 AK3 GLY C 322 GLN C 333 1 12
HELIX 94 AK4 GLU C 416 GLU C 419 5 4
HELIX 95 AK5 GLY C 423 GLY C 437 1 15
HELIX 96 AK6 GLY C 462 TYR C 469 1 8
HELIX 97 AK7 THR C 482 ILE C 489 1 8
HELIX 98 AK8 ALA C 522 VAL C 543 1 22
HELIX 99 AK9 LEU C 596 MET C 629 1 34
HELIX 100 AL1 SER C 635 LYS C 641 1 7
HELIX 101 AL2 GLY C 653 SER C 662 1 10
HELIX 102 AL3 ILE C 664 ALA C 677 1 14
HELIX 103 AL4 THR C 685 LYS C 695 1 11
HELIX 104 AL5 SER C 706 GLN C 714 1 9
HELIX 105 AL6 LEU C 742 GLN C 756 1 15
HELIX 106 AL7 GLY C 757 TYR C 768 1 12
HELIX 107 AL8 ALA C 775 GLU C 782 1 8
HELIX 108 AL9 LEU C 789 TYR C 797 1 9
HELIX 109 AM1 TYR C 797 PHE C 814 1 18
SHEET 1 AA1 5 THR A 42 LEU A 48 0
SHEET 2 AA1 5 GLN A 11 PRO A 17 1 N PHE A 16 O LEU A 48
SHEET 3 AA1 5 ALA A 70 GLY A 73 1 O ALA A 70 N GLY A 13
SHEET 4 AA1 5 SER A 93 THR A 96 1 O SER A 93 N ILE A 71
SHEET 5 AA1 5 VAL A 108 GLN A 110 1 O ILE A 109 N PHE A 94
SHEET 1 AA2 8 GLN A 157 ASN A 162 0
SHEET 2 AA2 8 LYS A 130 TYR A 135 1 N TYR A 133 O ILE A 161
SHEET 3 AA2 8 ARG A 189 ASP A 193 1 O ARG A 189 N ALA A 132
SHEET 4 AA2 8 HIS A 217 ILE A 220 1 O HIS A 217 N VAL A 190
SHEET 5 AA2 8 GLU A 239 GLN A 244 1 O GLU A 239 N TYR A 218
SHEET 6 AA2 8 ILE A 356 LYS A 362 -1 O MET A 359 N GLY A 242
SHEET 7 AA2 8 GLY A 365 SER A 373 -1 O ARG A 367 N GLU A 360
SHEET 8 AA2 8 LYS A 377 VAL A 380 -1 O LYS A 377 N SER A 373
SHEET 1 AA3 2 VAL A 336 GLY A 338 0
SHEET 2 AA3 2 GLY A 341 ILE A 343 -1 O ILE A 343 N VAL A 336
SHEET 1 AA4 3 LYS A 439 ILE A 444 0
SHEET 2 AA4 3 THR A 394 THR A 399 1 N VAL A 397 O THR A 443
SHEET 3 AA4 3 ILE A 474 ALA A 475 1 O ILE A 474 N THR A 398
SHEET 1 AA5 2 MET A 407 MET A 408 0
SHEET 2 AA5 2 TYR A 421 GLU A 422 -1 O GLU A 422 N MET A 407
SHEET 1 AA6 2 GLY A 451 ARG A 453 0
SHEET 2 AA6 2 TRP A 460 GLY A 462 -1 O ASN A 461 N ALA A 452
SHEET 1 AA7 2 ASP A 490 LEU A 498 0
SHEET 2 AA7 2 LYS A 730 THR A 736 -1 O LYS A 730 N LEU A 498
SHEET 1 AA8 4 ALA A 646 GLY A 648 0
SHEET 2 AA8 4 TYR A 700 GLU A 705 1 O LEU A 703 N GLY A 648
SHEET 3 AA8 4 ILE A 500 LYS A 505 -1 N SER A 501 O LEU A 704
SHEET 4 AA8 4 THR A 720 VAL A 723 -1 O MET A 721 N ILE A 504
SHEET 1 AA9 5 ARG B 40 LEU B 48 0
SHEET 2 AA9 5 SER B 9 PRO B 17 1 N ILE B 10 O ARG B 40
SHEET 3 AA9 5 ALA B 70 GLY B 73 1 O ALA B 70 N GLY B 13
SHEET 4 AA9 5 SER B 93 THR B 96 1 O SER B 93 N ILE B 71
SHEET 5 AA9 5 VAL B 108 GLN B 110 1 O ILE B 109 N PHE B 94
SHEET 1 AB1 7 GLN B 157 ASN B 162 0
SHEET 2 AB1 7 LYS B 130 TYR B 135 1 N TYR B 135 O ILE B 161
SHEET 3 AB1 7 ARG B 189 ILE B 191 1 O ILE B 191 N LEU B 134
SHEET 4 AB1 7 HIS B 217 ILE B 220 1 O HIS B 217 N VAL B 190
SHEET 5 AB1 7 GLU B 239 GLN B 244 1 O GLU B 239 N TYR B 218
SHEET 6 AB1 7 ILE B 356 LYS B 362 -1 O ASN B 357 N GLN B 244
SHEET 7 AB1 7 GLY B 365 TRP B 372 -1 O ARG B 367 N GLU B 360
SHEET 1 AB2 2 VAL B 336 GLY B 338 0
SHEET 2 AB2 2 GLY B 341 ILE B 343 -1 O ILE B 343 N VAL B 336
SHEET 1 AB3 5 TYR B 440 ILE B 444 0
SHEET 2 AB3 5 VAL B 395 THR B 399 1 N VAL B 397 O THR B 443
SHEET 3 AB3 5 ILE B 474 THR B 480 1 O ILE B 474 N THR B 398
SHEET 4 AB3 5 LYS B 730 PRO B 737 -1 O ALA B 735 N ALA B 475
SHEET 5 AB3 5 ILE B 489 PHE B 491 -1 N ASP B 490 O THR B 736
SHEET 1 AB4 5 TYR B 440 ILE B 444 0
SHEET 2 AB4 5 VAL B 395 THR B 399 1 N VAL B 397 O THR B 443
SHEET 3 AB4 5 ILE B 474 THR B 480 1 O ILE B 474 N THR B 398
SHEET 4 AB4 5 LYS B 730 PRO B 737 -1 O ALA B 735 N ALA B 475
SHEET 5 AB4 5 MET B 496 LEU B 498 -1 N LEU B 498 O LYS B 730
SHEET 1 AB5 2 MET B 407 MET B 408 0
SHEET 2 AB5 2 TYR B 421 GLU B 422 -1 O GLU B 422 N MET B 407
SHEET 1 AB6 2 GLY B 451 ARG B 453 0
SHEET 2 AB6 2 TRP B 460 GLY B 462 -1 O ASN B 461 N ALA B 452
SHEET 1 AB7 4 ALA B 646 GLY B 648 0
SHEET 2 AB7 4 TYR B 700 GLU B 705 1 O LEU B 703 N GLY B 648
SHEET 3 AB7 4 ILE B 500 LYS B 505 -1 N SER B 501 O LEU B 704
SHEET 4 AB7 4 THR B 720 VAL B 723 -1 O MET B 721 N ILE B 504
SHEET 1 AB8 5 ARG D 40 LEU D 48 0
SHEET 2 AB8 5 SER D 9 PRO D 17 1 N ILE D 10 O THR D 42
SHEET 3 AB8 5 ALA D 70 PHE D 72 1 O ALA D 70 N GLY D 13
SHEET 4 AB8 5 SER D 93 THR D 96 1 O SER D 93 N ILE D 71
SHEET 5 AB8 5 VAL D 108 GLN D 110 1 O ILE D 109 N PHE D 94
SHEET 1 AB9 8 GLN D 157 ASN D 162 0
SHEET 2 AB9 8 LYS D 130 TYR D 135 1 N TYR D 133 O THR D 159
SHEET 3 AB9 8 VAL D 190 ASP D 193 1 O ILE D 191 N LEU D 134
SHEET 4 AB9 8 HIS D 217 ILE D 220 1 O ILE D 219 N LEU D 192
SHEET 5 AB9 8 GLU D 239 GLN D 244 1 O GLU D 239 N TYR D 218
SHEET 6 AB9 8 ILE D 356 LYS D 362 -1 O ASN D 357 N GLN D 244
SHEET 7 AB9 8 GLY D 365 SER D 373 -1 O ARG D 367 N GLU D 360
SHEET 8 AB9 8 LYS D 377 VAL D 380 -1 O LYS D 377 N SER D 373
SHEET 1 AC1 2 GLN D 335 GLY D 338 0
SHEET 2 AC1 2 GLY D 341 LYS D 344 -1 O ILE D 343 N VAL D 336
SHEET 1 AC2 5 TYR D 440 ILE D 444 0
SHEET 2 AC2 5 VAL D 395 THR D 399 1 N VAL D 397 O THR D 443
SHEET 3 AC2 5 ILE D 474 THR D 480 1 O ILE D 474 N THR D 398
SHEET 4 AC2 5 LYS D 730 PRO D 737 -1 O ALA D 735 N ALA D 475
SHEET 5 AC2 5 ILE D 489 LEU D 498 -1 N LEU D 498 O LYS D 730
SHEET 1 AC3 2 MET D 407 MET D 408 0
SHEET 2 AC3 2 TYR D 421 GLU D 422 -1 O GLU D 422 N MET D 407
SHEET 1 AC4 2 GLY D 451 ARG D 453 0
SHEET 2 AC4 2 TRP D 460 GLY D 462 -1 O ASN D 461 N ALA D 452
SHEET 1 AC5 4 ALA D 646 GLY D 648 0
SHEET 2 AC5 4 TYR D 700 GLU D 705 1 O LEU D 703 N GLY D 648
SHEET 3 AC5 4 ILE D 500 LYS D 505 -1 N SER D 501 O LEU D 704
SHEET 4 AC5 4 THR D 720 VAL D 723 -1 O MET D 721 N ILE D 504
SHEET 1 AC6 5 ARG C 40 LEU C 48 0
SHEET 2 AC6 5 SER C 9 PRO C 17 1 N ILE C 10 O THR C 42
SHEET 3 AC6 5 ALA C 70 GLY C 73 1 O ALA C 70 N GLY C 13
SHEET 4 AC6 5 SER C 93 THR C 96 1 O SER C 93 N ILE C 71
SHEET 5 AC6 5 VAL C 108 GLN C 110 1 O ILE C 109 N PHE C 94
SHEET 1 AC7 8 GLN C 157 ASN C 162 0
SHEET 2 AC7 8 LYS C 130 TYR C 135 1 N PHE C 131 O GLN C 157
SHEET 3 AC7 8 ARG C 189 ILE C 191 1 O ILE C 191 N LEU C 134
SHEET 4 AC7 8 HIS C 217 ILE C 220 1 O HIS C 217 N VAL C 190
SHEET 5 AC7 8 GLU C 239 GLN C 244 1 O SER C 241 N TYR C 218
SHEET 6 AC7 8 ILE C 356 LYS C 362 -1 O MET C 359 N GLY C 242
SHEET 7 AC7 8 GLY C 365 TRP C 372 -1 O TRP C 372 N ILE C 356
SHEET 8 AC7 8 VAL C 379 VAL C 380 -1 O VAL C 379 N TYR C 371
SHEET 1 AC8 2 VAL C 336 GLY C 338 0
SHEET 2 AC8 2 GLY C 341 ILE C 343 -1 O ILE C 343 N VAL C 336
SHEET 1 AC9 3 TYR C 440 ILE C 444 0
SHEET 2 AC9 3 VAL C 395 THR C 399 1 N VAL C 397 O THR C 443
SHEET 3 AC9 3 ILE C 474 ALA C 475 1 O ILE C 474 N THR C 398
SHEET 1 AD1 2 MET C 407 MET C 408 0
SHEET 2 AD1 2 TYR C 421 GLU C 422 -1 O GLU C 422 N MET C 407
SHEET 1 AD2 2 ALA C 452 ARG C 453 0
SHEET 2 AD2 2 TRP C 460 ASN C 461 -1 O ASN C 461 N ALA C 452
SHEET 1 AD3 2 ASP C 490 LEU C 498 0
SHEET 2 AD3 2 LYS C 730 THR C 736 -1 O LYS C 730 N LEU C 498
SHEET 1 AD4 4 ALA C 646 GLY C 648 0
SHEET 2 AD4 4 TYR C 700 GLU C 705 1 O LEU C 703 N GLY C 648
SHEET 3 AD4 4 ILE C 500 LYS C 505 -1 N MET C 503 O TYR C 702
SHEET 4 AD4 4 THR C 720 VAL C 723 -1 O MET C 721 N ILE C 504
SSBOND 1 CYS A 61 CYS A 313 1555 1555 2.03
SSBOND 2 CYS A 718 CYS A 773 1555 1555 2.03
SSBOND 3 CYS B 61 CYS B 313 1555 1555 2.03
SSBOND 4 CYS B 718 CYS B 773 1555 1555 2.03
SSBOND 5 CYS D 61 CYS D 313 1555 1555 2.04
SSBOND 6 CYS D 718 CYS D 773 1555 1555 2.03
SSBOND 7 CYS C 61 CYS C 313 1555 1555 2.04
SSBOND 8 CYS C 718 CYS C 773 1555 1555 2.03
LINK ND2 ASN A 353 C1 NAG A1001 1555 1555 1.46
LINK ND2 ASN B 353 C1 NAG B1001 1555 1555 1.43
LINK ND2 ASN D 353 C1 NAG D1001 1555 1555 1.43
LINK ND2 ASN C 353 C1 NAG C1001 1555 1555 1.44
CISPEP 1 ASN A 316 PRO A 317 0 1.39
CISPEP 2 SER A 403 PRO A 404 0 -6.39
CISPEP 3 GLU A 678 PRO A 679 0 -3.11
CISPEP 4 LYS A 716 PRO A 717 0 -3.90
CISPEP 5 ASN B 316 PRO B 317 0 -0.55
CISPEP 6 SER B 403 PRO B 404 0 -7.23
CISPEP 7 GLU B 678 PRO B 679 0 -3.63
CISPEP 8 LYS B 716 PRO B 717 0 -3.82
CISPEP 9 ASN D 316 PRO D 317 0 1.74
CISPEP 10 SER D 403 PRO D 404 0 -6.71
CISPEP 11 GLU D 678 PRO D 679 0 -4.49
CISPEP 12 LYS D 716 PRO D 717 0 -3.65
CISPEP 13 ASN C 316 PRO C 317 0 -1.43
CISPEP 14 SER C 403 PRO C 404 0 -6.52
CISPEP 15 GLU C 678 PRO C 679 0 -4.29
CISPEP 16 LYS C 716 PRO C 717 0 -3.28
CRYST1 107.810 149.130 352.790 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009276 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002835 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
