HEADER TRANSPORT PROTEIN 11-AUG-25 9PZW TITLE GLUN1/GLUN2A IN COMPLEX WITH 3D2 FAB, GLYCINE AND GLUTAMATE-BOUND TITLE 2 STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF GLUN2A-SPECIFIC MONOCLONAL FAB FRAGMENT, COMPND 3 TERMED 3D2; COMPND 4 CHAIN: J, L; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LIGHT CHAIN OF GLUN2A-SPECIFIC MONOCLONAL FAB FRAGMENT, COMPND 8 TERMED 3D2; COMPND 9 CHAIN: K, M; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1; COMPND 13 CHAIN: A, C; COMPND 14 SYNONYM: GLUN1,GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1,N-METHYL-D- COMPND 15 ASPARTATE RECEPTOR SUBUNIT NR1,NMD-R1; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A; COMPND 19 CHAIN: B, D; COMPND 20 SYNONYM: GLUN2A,GLUTAMATE [NMDA] RECEPTOR SUBUNIT EPSILON-1,N-METHYL COMPND 21 D-ASPARTATE RECEPTOR SUBTYPE 2A,NMDAR2A,NR2A; COMPND 22 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 13 ORGANISM_COMMON: NORWAY RAT; SOURCE 14 ORGANISM_TAXID: 10116; SOURCE 15 GENE: GRIN1, NMDAR1; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 20 ORGANISM_COMMON: NORWAY RAT; SOURCE 21 ORGANISM_TAXID: 10116; SOURCE 22 GENE: GRIN2A; SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS LIGAND-GATED ION CHANNEL, NMDA, ANTIBODY, COMPLEX, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.KIM,E.GOUAUX REVDAT 1 17-DEC-25 9PZW 0 JRNL AUTH J.KIM,E.GOUAUX JRNL TITL GLUN1/GLUN2A IN COMPLEX WITH 3D2 FAB, GLYCINE AND JRNL TITL 2 GLUTAMATE-BOUND STATE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.43 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.430 REMARK 3 NUMBER OF PARTICLES : 183438 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9PZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298441. 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 : GLUN1/GLUN2A IN COMPLEX WITH REMARK 245 3D2 FAB, GLYCINE AND GLUTAMATE- REMARK 245 BOUND STATE REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.05 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 6721 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 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: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, A, B, C, D, L, M 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 J 0 REMARK 465 VAL J 1 REMARK 465 SER J 2 REMARK 465 ALA J 3 REMARK 465 ILE J 4 REMARK 465 VAL J 5 REMARK 465 LEU J 6 REMARK 465 TYR J 7 REMARK 465 VAL J 8 REMARK 465 LEU J 9 REMARK 465 LEU J 10 REMARK 465 ALA J 11 REMARK 465 ALA J 12 REMARK 465 ALA J 13 REMARK 465 ALA J 14 REMARK 465 HIS J 15 REMARK 465 SER J 16 REMARK 465 ALA J 17 REMARK 465 PHE J 18 REMARK 465 ALA J 19 REMARK 465 SER J 139 REMARK 465 ALA J 140 REMARK 465 MET K 1 REMARK 465 VAL K 2 REMARK 465 SER K 3 REMARK 465 ALA K 4 REMARK 465 ILE K 5 REMARK 465 VAL K 6 REMARK 465 LEU K 7 REMARK 465 TYR K 8 REMARK 465 VAL K 9 REMARK 465 LEU K 10 REMARK 465 LEU K 11 REMARK 465 ALA K 12 REMARK 465 ALA K 13 REMARK 465 ALA K 14 REMARK 465 ALA K 15 REMARK 465 HIS K 16 REMARK 465 SER K 17 REMARK 465 ALA K 18 REMARK 465 PHE K 19 REMARK 465 ALA K 20 REMARK 465 ILE K 130 REMARK 465 LYS K 131 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 SER A 617 REMARK 465 GLY A 618 REMARK 465 ILE A 619 REMARK 465 GLY A 620 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 ARG A 839 REMARK 465 HIS A 840 REMARK 465 LYS A 841 REMARK 465 ASP A 842 REMARK 465 ALA A 843 REMARK 465 ARG A 844 REMARK 465 ARG A 845 REMARK 465 LYS A 846 REMARK 465 GLN A 847 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 TRP B 55 REMARK 465 GLY B 56 REMARK 465 PRO B 57 REMARK 465 GLU B 58 REMARK 465 GLN B 59 REMARK 465 ALA B 60 REMARK 465 ALA B 324 REMARK 465 GLU B 325 REMARK 465 LYS B 326 REMARK 465 PRO B 327 REMARK 465 GLU B 328 REMARK 465 THR B 329 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 GLU B 838 REMARK 465 HIS B 839 REMARK 465 LEU B 840 REMARK 465 PHE B 841 REMARK 465 TYR B 842 REMARK 465 TRP B 843 REMARK 465 LYS B 844 REMARK 465 LEU B 845 REMARK 465 ARG B 846 REMARK 465 PHE B 847 REMARK 465 CYS B 848 REMARK 465 PHE B 849 REMARK 465 THR B 850 REMARK 465 GLY B 851 REMARK 465 VAL B 852 REMARK 465 CYS B 853 REMARK 465 SER B 854 REMARK 465 ASP B 855 REMARK 465 ARG B 856 REMARK 465 PRO B 857 REMARK 465 GLY B 858 REMARK 465 LEU B 859 REMARK 465 LEU B 860 REMARK 465 PHE B 861 REMARK 465 SER B 862 REMARK 465 ILE B 863 REMARK 465 SER B 864 REMARK 465 ARG B 865 REMARK 465 GLY B 866 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 LEU C 601 REMARK 465 THR C 602 REMARK 465 LEU C 603 REMARK 465 SER C 604 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 ARG C 839 REMARK 465 HIS C 840 REMARK 465 LYS C 841 REMARK 465 ASP C 842 REMARK 465 ALA C 843 REMARK 465 ARG C 844 REMARK 465 ARG C 845 REMARK 465 LYS C 846 REMARK 465 GLN C 847 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 ALA D 324 REMARK 465 GLU D 325 REMARK 465 LYS D 326 REMARK 465 PRO D 327 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 GLU D 838 REMARK 465 HIS D 839 REMARK 465 LEU D 840 REMARK 465 PHE D 841 REMARK 465 TYR D 842 REMARK 465 TRP D 843 REMARK 465 LYS D 844 REMARK 465 LEU D 845 REMARK 465 ARG D 846 REMARK 465 PHE D 847 REMARK 465 CYS D 848 REMARK 465 PHE D 849 REMARK 465 THR D 850 REMARK 465 GLY D 851 REMARK 465 VAL D 852 REMARK 465 CYS D 853 REMARK 465 SER D 854 REMARK 465 ASP D 855 REMARK 465 ARG D 856 REMARK 465 PRO D 857 REMARK 465 GLY D 858 REMARK 465 LEU D 859 REMARK 465 LEU D 860 REMARK 465 PHE D 861 REMARK 465 SER D 862 REMARK 465 ILE D 863 REMARK 465 SER D 864 REMARK 465 ARG D 865 REMARK 465 GLY D 866 REMARK 465 MET L 0 REMARK 465 VAL L 1 REMARK 465 SER L 2 REMARK 465 ALA L 3 REMARK 465 ILE L 4 REMARK 465 VAL L 5 REMARK 465 LEU L 6 REMARK 465 TYR L 7 REMARK 465 VAL L 8 REMARK 465 LEU L 9 REMARK 465 LEU L 10 REMARK 465 ALA L 11 REMARK 465 ALA L 12 REMARK 465 ALA L 13 REMARK 465 ALA L 14 REMARK 465 HIS L 15 REMARK 465 SER L 16 REMARK 465 ALA L 17 REMARK 465 PHE L 18 REMARK 465 ALA L 19 REMARK 465 SER L 139 REMARK 465 ALA L 140 REMARK 465 MET M 1 REMARK 465 VAL M 2 REMARK 465 SER M 3 REMARK 465 ALA M 4 REMARK 465 ILE M 5 REMARK 465 VAL M 6 REMARK 465 LEU M 7 REMARK 465 TYR M 8 REMARK 465 VAL M 9 REMARK 465 LEU M 10 REMARK 465 LEU M 11 REMARK 465 ALA M 12 REMARK 465 ALA M 13 REMARK 465 ALA M 14 REMARK 465 ALA M 15 REMARK 465 HIS M 16 REMARK 465 SER M 17 REMARK 465 ALA M 18 REMARK 465 PHE M 19 REMARK 465 ALA M 20 REMARK 465 ILE M 130 REMARK 465 LYS M 131 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 THR J 93 OG1 CG2 REMARK 470 ASP K 21 CG OD1 OD2 REMARK 470 VAL K 82 CG1 CG2 REMARK 470 LYS K 127 CG CD CE NZ REMARK 470 LYS A 25 CG CD CE NZ REMARK 470 ARG A 36 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 37 CG CD CE NZ REMARK 470 ARG A 43 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 44 CG CD OE1 OE2 REMARK 470 ARG A 52 CG CD NE CZ NH1 NH2 REMARK 470 TRP A 56 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 56 CZ3 CH2 REMARK 470 LYS A 57 CG CD CE NZ REMARK 470 ASN A 99 CG OD1 ND2 REMARK 470 LYS A 202 CG CD CE NZ REMARK 470 ASN A 257 CG OD1 ND2 REMARK 470 LYS A 316 CG CD CE NZ REMARK 470 LYS A 329 CG CD CE NZ REMARK 470 ARG A 337 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 378 CG CD CE NZ REMARK 470 GLU A 406 CG CD OE1 OE2 REMARK 470 LEU A 699 CG CD1 CD2 REMARK 470 ARG B 49 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 323 CG CD OE1 NE2 REMARK 470 LYS B 394 CG CD CE NZ REMARK 470 GLU B 400 CG CD OE1 OE2 REMARK 470 ARG B 431 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 668 CG CD CE NZ REMARK 470 LYS B 669 CG CD CE NZ REMARK 470 GLN B 671 CG CD OE1 NE2 REMARK 470 ARG B 672 CG CD NE CZ NH1 NH2 REMARK 470 HIS B 674 CG ND1 CD2 CE1 NE2 REMARK 470 TYR B 676 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG B 681 CG CD NE CZ NH1 NH2 REMARK 470 TYR B 700 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR B 754 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE B 755 CG1 CG2 CD1 REMARK 470 PHE B 835 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP C 100 CG OD1 OD2 REMARK 470 LYS C 316 CG CD CE NZ REMARK 470 ARG C 323 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 630 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 49 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 207 CG OD1 OD2 REMARK 470 LYS D 214 CG CD CE NZ REMARK 470 GLN D 323 CG CD OE1 NE2 REMARK 470 GLU D 328 CG CD OE1 OE2 REMARK 470 GLU D 352 CG CD OE1 OE2 REMARK 470 GLU D 353 CG CD OE1 OE2 REMARK 470 LEU D 665 CG CD1 CD2 REMARK 470 LYS D 668 CG CD CE NZ REMARK 470 LYS D 669 CG CD CE NZ REMARK 470 TYR D 676 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG D 681 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 707 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 711 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 724 CG CD CE NZ REMARK 470 TYR D 754 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE D 755 CG1 CG2 CD1 REMARK 470 LYS M 127 CG CD CE NZ 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 ARG J 49 34.15 -91.35 REMARK 500 PRO J 60 76.47 -66.26 REMARK 500 ILE J 67 -62.24 -104.70 REMARK 500 ALA K 75 -5.79 69.28 REMARK 500 ASP K 106 59.24 -91.31 REMARK 500 HIS A 94 76.08 61.64 REMARK 500 ASN A 99 0.72 -69.37 REMARK 500 ASP A 100 -146.59 61.56 REMARK 500 SER A 136 52.89 -140.06 REMARK 500 ASP A 169 -6.66 73.03 REMARK 500 GLU A 299 -169.44 -118.60 REMARK 500 THR A 302 -167.91 -101.23 REMARK 500 ASN A 341 -164.54 -79.70 REMARK 500 ASP A 345 -167.87 -122.22 REMARK 500 THR A 370 12.33 -142.51 REMARK 500 ASP A 481 -168.85 -101.35 REMARK 500 SER A 493 -6.10 69.22 REMARK 500 LYS A 678 -62.54 -92.94 REMARK 500 GLN A 686 62.26 61.97 REMARK 500 ARG A 763 -162.91 -78.45 REMARK 500 LYS A 764 -162.00 -73.94 REMARK 500 ASN A 782 -158.42 -88.10 REMARK 500 THR B 104 -168.47 -76.54 REMARK 500 ILE B 127 -61.63 -123.28 REMARK 500 THR B 143 44.69 -109.50 REMARK 500 SER B 171 -168.88 -124.43 REMARK 500 SER B 209 33.78 -99.33 REMARK 500 ASP B 212 -3.80 66.59 REMARK 500 SER B 224 -167.68 -77.17 REMARK 500 GLU B 379 -160.11 -75.07 REMARK 500 PHE B 396 -126.44 54.23 REMARK 500 ASP B 398 55.28 38.77 REMARK 500 LYS B 472 70.27 62.36 REMARK 500 LEU B 512 114.96 -166.76 REMARK 500 THR B 600 34.88 -97.59 REMARK 500 THR B 749 -173.04 -68.23 REMARK 500 ALA B 757 43.19 34.93 REMARK 500 THR B 758 108.04 -50.79 REMARK 500 SER C 55 35.71 -94.30 REMARK 500 CYS C 79 -6.82 -58.16 REMARK 500 PRO C 143 -166.53 -74.21 REMARK 500 SER C 168 -62.35 -95.20 REMARK 500 GLU C 188 61.63 64.24 REMARK 500 GLU C 297 30.85 -142.19 REMARK 500 ASP C 345 -162.87 -77.65 REMARK 500 ASN C 375 -169.22 -104.53 REMARK 500 PRO C 516 76.04 -69.84 REMARK 500 GLU C 707 5.84 -69.80 REMARK 500 THR C 749 -156.97 -85.31 REMARK 500 ARG C 763 -162.81 -77.81 REMARK 500 REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-72084 RELATED DB: EMDB REMARK 900 GLUN1/GLUN2A IN COMPLEX WITH 3D2 FAB, GLYCINE AND GLUTAMATE-BOUND REMARK 900 STATE DBREF 9PZW J 0 140 PDB 9PZW 9PZW 0 140 DBREF 9PZW K 1 131 PDB 9PZW 9PZW 1 131 DBREF 9PZW A 1 847 UNP P35439 NMDZ1_RAT 1 847 DBREF 9PZW B 1 866 UNP Q00959 NMDE1_RAT 1 866 DBREF 9PZW C 1 847 UNP P35439 NMDZ1_RAT 1 847 DBREF 9PZW D 1 866 UNP Q00959 NMDE1_RAT 1 866 DBREF 9PZW L 0 140 PDB 9PZW 9PZW 0 140 DBREF 9PZW M 1 131 PDB 9PZW 9PZW 1 131 SEQADV 9PZW THR B 758 UNP Q00959 SER 758 CONFLICT SEQADV 9PZW THR D 758 UNP Q00959 SER 758 CONFLICT SEQRES 1 J 141 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 J 141 ALA ALA HIS SER ALA PHE ALA GLN VAL GLN LEU GLN GLN SEQRES 3 J 141 SER GLY ALA GLU LEU MET LYS PRO GLY ALA SER VAL LYS SEQRES 4 J 141 ILE SER CYS LYS ALA THR GLY TYR THR PHE ARG SER TYR SEQRES 5 J 141 TRP ILE GLU TRP LEU LYS GLN ARG PRO GLY HIS GLY LEU SEQRES 6 J 141 GLU TRP ILE GLY GLU ILE LEU PRO GLY SER GLY ARG THR SEQRES 7 J 141 ASN TYR ASN GLU LYS PHE LYS GLY LYS ALA THR ILE THR SEQRES 8 J 141 ALA ASP THR SER SER ASN THR ALA TYR MET GLN LEU SER SEQRES 9 J 141 SER LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS THR SEQRES 10 J 141 ARG SER ARG GLY THR MET ILE THR ARG GLU PHE THR TYR SEQRES 11 J 141 TRP GLY GLN GLY ALA LEU VAL THR VAL SER ALA SEQRES 1 K 131 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 K 131 ALA ALA HIS SER ALA PHE ALA ASP ILE VAL LEU THR GLN SEQRES 3 K 131 SER PRO ALA SER LEU ALA VAL SER LEU GLY GLN ARG ALA SEQRES 4 K 131 THR ILE SER CYS ARG ALA SER GLU SER VAL GLU TYR TYR SEQRES 5 K 131 GLY THR THR LEU MET GLN TRP TYR GLN GLN LYS PRO GLY SEQRES 6 K 131 GLN PRO PRO LYS LEU LEU ILE TYR ALA ALA SER ASN VAL SEQRES 7 K 131 ASP SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SER SEQRES 8 K 131 GLY THR ASP PHE SER LEU ASN ILE HIS PRO VAL GLU GLU SEQRES 9 K 131 ASP ASP ILE ALA MET TYR PHE CYS GLN GLN SER ARG LYS SEQRES 10 K 131 VAL PRO SER THR PHE GLY GLY GLY THR LYS LEU GLU ILE SEQRES 11 K 131 LYS SEQRES 1 A 847 MET SER THR MET HIS LEU LEU THR PHE ALA LEU LEU PHE SEQRES 2 A 847 SER CYS SER PHE ALA ARG ALA ALA CYS ASP PRO LYS ILE SEQRES 3 A 847 VAL ASN ILE GLY ALA VAL LEU SER THR ARG LYS HIS GLU SEQRES 4 A 847 GLN MET PHE ARG GLU ALA VAL ASN GLN ALA ASN LYS ARG SEQRES 5 A 847 HIS GLY SER TRP LYS ILE GLN LEU ASN ALA THR SER VAL SEQRES 6 A 847 THR HIS LYS PRO ASN ALA ILE GLN MET ALA LEU SER VAL SEQRES 7 A 847 CYS GLU ASP LEU ILE SER SER GLN VAL TYR ALA ILE LEU SEQRES 8 A 847 VAL SER HIS PRO PRO THR PRO ASN ASP HIS PHE THR PRO SEQRES 9 A 847 THR PRO VAL SER TYR THR ALA GLY PHE TYR ARG ILE PRO SEQRES 10 A 847 VAL LEU GLY LEU THR THR ARG MET SER ILE TYR SER ASP SEQRES 11 A 847 LYS SER ILE HIS LEU SER PHE LEU ARG THR VAL PRO PRO SEQRES 12 A 847 TYR SER HIS GLN SER SER VAL TRP PHE GLU MET MET ARG SEQRES 13 A 847 VAL TYR ASN TRP ASN HIS ILE ILE LEU LEU VAL SER ASP SEQRES 14 A 847 ASP HIS GLU GLY ARG ALA ALA GLN LYS ARG LEU GLU THR SEQRES 15 A 847 LEU LEU GLU GLU ARG GLU SER LYS ALA GLU LYS VAL LEU SEQRES 16 A 847 GLN PHE ASP PRO GLY THR LYS ASN VAL THR ALA LEU LEU SEQRES 17 A 847 MET GLU ALA ARG GLU LEU GLU ALA ARG VAL ILE ILE LEU SEQRES 18 A 847 SER ALA SER GLU ASP ASP ALA ALA THR VAL TYR ARG ALA SEQRES 19 A 847 ALA ALA MET LEU ASN MET THR GLY SER GLY TYR VAL TRP SEQRES 20 A 847 LEU VAL GLY GLU ARG GLU ILE SER GLY ASN ALA LEU ARG SEQRES 21 A 847 TYR ALA PRO ASP GLY ILE ILE GLY LEU GLN LEU ILE ASN SEQRES 22 A 847 GLY LYS ASN GLU SER ALA HIS ILE SER ASP ALA VAL GLY SEQRES 23 A 847 VAL VAL ALA GLN ALA VAL HIS GLU LEU LEU GLU LYS GLU SEQRES 24 A 847 ASN ILE THR ASP PRO PRO ARG GLY CYS VAL GLY ASN THR SEQRES 25 A 847 ASN ILE TRP LYS THR GLY PRO LEU PHE LYS ARG VAL LEU SEQRES 26 A 847 MET SER SER LYS TYR ALA ASP GLY VAL THR GLY ARG VAL SEQRES 27 A 847 GLU PHE ASN GLU ASP GLY ASP ARG LYS PHE ALA ASN TYR SEQRES 28 A 847 SER ILE MET ASN LEU GLN ASN ARG LYS LEU VAL GLN VAL SEQRES 29 A 847 GLY ILE TYR ASN GLY THR HIS VAL ILE PRO ASN ASP ARG SEQRES 30 A 847 LYS ILE ILE TRP PRO GLY GLY GLU THR GLU LYS PRO ARG SEQRES 31 A 847 GLY TYR GLN MET SER THR ARG LEU LYS ILE VAL THR ILE SEQRES 32 A 847 HIS GLN GLU PRO PHE VAL TYR VAL LYS PRO THR MET SER SEQRES 33 A 847 ASP GLY THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP SEQRES 34 A 847 PRO VAL LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR SEQRES 35 A 847 SER PRO GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS SEQRES 36 A 847 TYR GLY PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG SEQRES 37 A 847 THR MET ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP SEQRES 38 A 847 GLY LYS PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN SEQRES 39 A 847 LYS LYS GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER SEQRES 40 A 847 GLY GLN ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN SEQRES 41 A 847 ASN GLU ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE SEQRES 42 A 847 LYS TYR GLN GLY LEU THR ILE LEU VAL LYS LYS GLU ILE SEQRES 43 A 847 PRO ARG SER THR LEU ASP SER PHE MET GLN PRO PHE GLN SEQRES 44 A 847 SER THR LEU TRP LEU LEU VAL GLY LEU SER VAL HIS VAL SEQRES 45 A 847 VAL ALA VAL MET LEU TYR LEU LEU ASP ARG PHE SER PRO SEQRES 46 A 847 PHE GLY ARG PHE LYS VAL ASN SER GLU GLU GLU GLU GLU SEQRES 47 A 847 ASP ALA LEU THR LEU SER SER ALA MET TRP PHE SER TRP SEQRES 48 A 847 GLY VAL LEU LEU ASN SER GLY ILE GLY GLU GLY ALA PRO SEQRES 49 A 847 ARG SER PHE SER ALA ARG ILE LEU GLY MET VAL TRP ALA SEQRES 50 A 847 GLY PHE ALA MET ILE ILE VAL ALA SER TYR THR ALA ASN SEQRES 51 A 847 LEU ALA ALA PHE LEU VAL LEU ASP ARG PRO GLU GLU ARG SEQRES 52 A 847 ILE THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER SEQRES 53 A 847 ASP LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL SEQRES 54 A 847 ASP ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET SEQRES 55 A 847 TYR ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA SEQRES 56 A 847 GLU ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA SEQRES 57 A 847 PHE ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER SEQRES 58 A 847 GLN LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE SEQRES 59 A 847 ARG SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO SEQRES 60 A 847 TRP LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS SEQRES 61 A 847 GLU ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL SEQRES 62 A 847 ARG TYR GLN GLU CYS ASP SER ARG SER ASN ALA PRO ALA SEQRES 63 A 847 THR LEU THR PHE GLU ASN MET ALA GLY VAL PHE MET LEU SEQRES 64 A 847 VAL ALA GLY GLY ILE VAL ALA GLY ILE PHE LEU ILE PHE SEQRES 65 A 847 ILE GLU ILE ALA TYR LYS ARG HIS LYS ASP ALA ARG ARG SEQRES 66 A 847 LYS GLN SEQRES 1 B 866 MET GLY ARG LEU GLY TYR TRP THR LEU LEU VAL LEU PRO SEQRES 2 B 866 ALA LEU LEU VAL TRP ARG ASP PRO ALA GLN ASN ALA ALA SEQRES 3 B 866 ALA GLU LYS GLY PRO PRO ALA LEU ASN ILE ALA VAL LEU SEQRES 4 B 866 LEU GLY HIS SER HIS ASP VAL THR GLU ARG GLU LEU ARG SEQRES 5 B 866 ASN LEU TRP GLY PRO GLU GLN ALA THR GLY LEU PRO LEU SEQRES 6 B 866 ASP VAL ASN VAL VAL ALA LEU LEU MET ASN ARG THR ASP SEQRES 7 B 866 PRO LYS SER LEU ILE THR HIS VAL CYS ASP LEU MET SER SEQRES 8 B 866 GLY ALA ARG ILE HIS GLY LEU VAL PHE GLY ASP ASP THR SEQRES 9 B 866 ASP GLN GLU ALA VAL ALA GLN MET LEU ASP PHE ILE SER SEQRES 10 B 866 SER GLN THR PHE ILE PRO ILE LEU GLY ILE HIS GLY GLY SEQRES 11 B 866 ALA SER MET ILE MET ALA ASP LYS ASP PRO THR SER THR SEQRES 12 B 866 PHE PHE GLN PHE GLY ALA SER ILE GLN GLN GLN ALA THR SEQRES 13 B 866 VAL MET LEU LYS ILE MET GLN ASP TYR ASP TRP HIS VAL SEQRES 14 B 866 PHE SER LEU VAL THR THR ILE PHE PRO GLY TYR ARG ASP SEQRES 15 B 866 PHE ILE SER PHE ILE LYS THR THR VAL ASP ASN SER PHE SEQRES 16 B 866 VAL GLY TRP ASP MET GLN ASN VAL ILE THR LEU ASP THR SEQRES 17 B 866 SER PHE GLU ASP ALA LYS THR GLN VAL GLN LEU LYS LYS SEQRES 18 B 866 ILE HIS SER SER VAL ILE LEU LEU TYR CYS SER LYS ASP SEQRES 19 B 866 GLU ALA VAL LEU ILE LEU SER GLU ALA ARG SER LEU GLY SEQRES 20 B 866 LEU THR GLY TYR ASP PHE PHE TRP ILE VAL PRO SER LEU SEQRES 21 B 866 VAL SER GLY ASN THR GLU LEU ILE PRO LYS GLU PHE PRO SEQRES 22 B 866 SER GLY LEU ILE SER VAL SER TYR ASP ASP TRP ASP TYR SEQRES 23 B 866 SER LEU GLU ALA ARG VAL ARG ASP GLY LEU GLY ILE LEU SEQRES 24 B 866 THR THR ALA ALA SER SER MET LEU GLU LYS PHE SER TYR SEQRES 25 B 866 ILE PRO GLU ALA LYS ALA SER CYS TYR GLY GLN ALA GLU SEQRES 26 B 866 LYS PRO GLU THR PRO LEU HIS THR LEU HIS GLN PHE MET SEQRES 27 B 866 VAL ASN VAL THR TRP ASP GLY LYS ASP LEU SER PHE THR SEQRES 28 B 866 GLU GLU GLY TYR GLN VAL HIS PRO ARG LEU VAL VAL ILE SEQRES 29 B 866 VAL LEU ASN LYS ASP ARG GLU TRP GLU LYS VAL GLY LYS SEQRES 30 B 866 TRP GLU ASN GLN THR LEU SER LEU ARG HIS ALA VAL TRP SEQRES 31 B 866 PRO ARG TYR LYS SER PHE SER ASP CYS GLU PRO ASP ASP SEQRES 32 B 866 ASN HIS LEU SER ILE VAL THR LEU GLU GLU ALA PRO PHE SEQRES 33 B 866 VAL ILE VAL GLU ASP ILE ASP PRO LEU THR GLU THR CYS SEQRES 34 B 866 VAL ARG ASN THR VAL PRO CYS ARG LYS PHE VAL LYS ILE SEQRES 35 B 866 ASN ASN SER THR ASN GLU GLY MET ASN VAL LYS LYS CYS SEQRES 36 B 866 CYS LYS GLY PHE CYS ILE ASP ILE LEU LYS LYS LEU SER SEQRES 37 B 866 ARG THR VAL LYS PHE THR TYR ASP LEU TYR LEU VAL THR SEQRES 38 B 866 ASN GLY LYS HIS GLY LYS LYS VAL ASN ASN VAL TRP ASN SEQRES 39 B 866 GLY MET ILE GLY GLU VAL VAL TYR GLN ARG ALA VAL MET SEQRES 40 B 866 ALA VAL GLY SER LEU THR ILE ASN GLU GLU ARG SER GLU SEQRES 41 B 866 VAL VAL ASP PHE SER VAL PRO PHE VAL GLU THR GLY ILE SEQRES 42 B 866 SER VAL MET VAL SER ARG SER ASN GLY THR VAL SER PRO SEQRES 43 B 866 SER ALA PHE LEU GLU PRO PHE SER ALA SER VAL TRP VAL SEQRES 44 B 866 MET MET PHE VAL MET LEU LEU ILE VAL SER ALA ILE ALA SEQRES 45 B 866 VAL PHE VAL PHE GLU TYR PHE SER PRO VAL GLY TYR ASN SEQRES 46 B 866 ARG ASN LEU ALA LYS GLY LYS ALA PRO HIS GLY PRO SER SEQRES 47 B 866 PHE THR ILE GLY LYS ALA ILE TRP LEU LEU TRP GLY LEU SEQRES 48 B 866 VAL PHE ASN ASN SER VAL PRO VAL GLN ASN PRO LYS GLY SEQRES 49 B 866 THR THR SER LYS ILE MET VAL SER VAL TRP ALA PHE PHE SEQRES 50 B 866 ALA VAL ILE PHE LEU ALA SER TYR THR ALA ASN LEU ALA SEQRES 51 B 866 ALA PHE MET ILE GLN GLU GLU PHE VAL ASP GLN VAL THR SEQRES 52 B 866 GLY LEU SER ASP LYS LYS PHE GLN ARG PRO HIS ASP TYR SEQRES 53 B 866 SER PRO PRO PHE ARG PHE GLY THR VAL PRO ASN GLY SER SEQRES 54 B 866 THR GLU ARG ASN ILE ARG ASN ASN TYR PRO TYR MET HIS SEQRES 55 B 866 GLN TYR MET THR ARG PHE ASN GLN ARG GLY VAL GLU ASP SEQRES 56 B 866 ALA LEU VAL SER LEU LYS THR GLY LYS LEU ASP ALA PHE SEQRES 57 B 866 ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS ALA GLY ARG SEQRES 58 B 866 ASP GLU GLY CYS LYS LEU VAL THR ILE GLY SER GLY TYR SEQRES 59 B 866 ILE PHE ALA THR THR GLY TYR GLY ILE ALA LEU GLN LYS SEQRES 60 B 866 GLY SER PRO TRP LYS ARG GLN ILE ASP LEU ALA LEU LEU SEQRES 61 B 866 GLN PHE VAL GLY ASP GLY GLU MET GLU GLU LEU GLU THR SEQRES 62 B 866 LEU TRP LEU THR GLY ILE CYS HIS ASN GLU LYS ASN GLU SEQRES 63 B 866 VAL MET SER SER GLN LEU ASP ILE ASP ASN MET ALA GLY SEQRES 64 B 866 VAL PHE TYR MET LEU ALA ALA ALA MET ALA LEU SER LEU SEQRES 65 B 866 ILE THR PHE ILE TRP GLU HIS LEU PHE TYR TRP LYS LEU SEQRES 66 B 866 ARG PHE CYS PHE THR GLY VAL CYS SER ASP ARG PRO GLY SEQRES 67 B 866 LEU LEU PHE SER ILE SER ARG GLY SEQRES 1 C 847 MET SER THR MET HIS LEU LEU THR PHE ALA LEU LEU PHE SEQRES 2 C 847 SER CYS SER PHE ALA ARG ALA ALA CYS ASP PRO LYS ILE SEQRES 3 C 847 VAL ASN ILE GLY ALA VAL LEU SER THR ARG LYS HIS GLU SEQRES 4 C 847 GLN MET PHE ARG GLU ALA VAL ASN GLN ALA ASN LYS ARG SEQRES 5 C 847 HIS GLY SER TRP LYS ILE GLN LEU ASN ALA THR SER VAL SEQRES 6 C 847 THR HIS LYS PRO ASN ALA ILE GLN MET ALA LEU SER VAL SEQRES 7 C 847 CYS GLU ASP LEU ILE SER SER GLN VAL TYR ALA ILE LEU SEQRES 8 C 847 VAL SER HIS PRO PRO THR PRO ASN ASP HIS PHE THR PRO SEQRES 9 C 847 THR PRO VAL SER TYR THR ALA GLY PHE TYR ARG ILE PRO SEQRES 10 C 847 VAL LEU GLY LEU THR THR ARG MET SER ILE TYR SER ASP SEQRES 11 C 847 LYS SER ILE HIS LEU SER PHE LEU ARG THR VAL PRO PRO SEQRES 12 C 847 TYR SER HIS GLN SER SER VAL TRP PHE GLU MET MET ARG SEQRES 13 C 847 VAL TYR ASN TRP ASN HIS ILE ILE LEU LEU VAL SER ASP SEQRES 14 C 847 ASP HIS GLU GLY ARG ALA ALA GLN LYS ARG LEU GLU THR SEQRES 15 C 847 LEU LEU GLU GLU ARG GLU SER LYS ALA GLU LYS VAL LEU SEQRES 16 C 847 GLN PHE ASP PRO GLY THR LYS ASN VAL THR ALA LEU LEU SEQRES 17 C 847 MET GLU ALA ARG GLU LEU GLU ALA ARG VAL ILE ILE LEU SEQRES 18 C 847 SER ALA SER GLU ASP ASP ALA ALA THR VAL TYR ARG ALA SEQRES 19 C 847 ALA ALA MET LEU ASN MET THR GLY SER GLY TYR VAL TRP SEQRES 20 C 847 LEU VAL GLY GLU ARG GLU ILE SER GLY ASN ALA LEU ARG SEQRES 21 C 847 TYR ALA PRO ASP GLY ILE ILE GLY LEU GLN LEU ILE ASN SEQRES 22 C 847 GLY LYS ASN GLU SER ALA HIS ILE SER ASP ALA VAL GLY SEQRES 23 C 847 VAL VAL ALA GLN ALA VAL HIS GLU LEU LEU GLU LYS GLU SEQRES 24 C 847 ASN ILE THR ASP PRO PRO ARG GLY CYS VAL GLY ASN THR SEQRES 25 C 847 ASN ILE TRP LYS THR GLY PRO LEU PHE LYS ARG VAL LEU SEQRES 26 C 847 MET SER SER LYS TYR ALA ASP GLY VAL THR GLY ARG VAL SEQRES 27 C 847 GLU PHE ASN GLU ASP GLY ASP ARG LYS PHE ALA ASN TYR SEQRES 28 C 847 SER ILE MET ASN LEU GLN ASN ARG LYS LEU VAL GLN VAL SEQRES 29 C 847 GLY ILE TYR ASN GLY THR HIS VAL ILE PRO ASN ASP ARG SEQRES 30 C 847 LYS ILE ILE TRP PRO GLY GLY GLU THR GLU LYS PRO ARG SEQRES 31 C 847 GLY TYR GLN MET SER THR ARG LEU LYS ILE VAL THR ILE SEQRES 32 C 847 HIS GLN GLU PRO PHE VAL TYR VAL LYS PRO THR MET SER SEQRES 33 C 847 ASP GLY THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP SEQRES 34 C 847 PRO VAL LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR SEQRES 35 C 847 SER PRO GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS SEQRES 36 C 847 TYR GLY PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG SEQRES 37 C 847 THR MET ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP SEQRES 38 C 847 GLY LYS PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN SEQRES 39 C 847 LYS LYS GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER SEQRES 40 C 847 GLY GLN ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN SEQRES 41 C 847 ASN GLU ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE SEQRES 42 C 847 LYS TYR GLN GLY LEU THR ILE LEU VAL LYS LYS GLU ILE SEQRES 43 C 847 PRO ARG SER THR LEU ASP SER PHE MET GLN PRO PHE GLN SEQRES 44 C 847 SER THR LEU TRP LEU LEU VAL GLY LEU SER VAL HIS VAL SEQRES 45 C 847 VAL ALA VAL MET LEU TYR LEU LEU ASP ARG PHE SER PRO SEQRES 46 C 847 PHE GLY ARG PHE LYS VAL ASN SER GLU GLU GLU GLU GLU SEQRES 47 C 847 ASP ALA LEU THR LEU SER SER ALA MET TRP PHE SER TRP SEQRES 48 C 847 GLY VAL LEU LEU ASN SER GLY ILE GLY GLU GLY ALA PRO SEQRES 49 C 847 ARG SER PHE SER ALA ARG ILE LEU GLY MET VAL TRP ALA SEQRES 50 C 847 GLY PHE ALA MET ILE ILE VAL ALA SER TYR THR ALA ASN SEQRES 51 C 847 LEU ALA ALA PHE LEU VAL LEU ASP ARG PRO GLU GLU ARG SEQRES 52 C 847 ILE THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER SEQRES 53 C 847 ASP LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL SEQRES 54 C 847 ASP ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET SEQRES 55 C 847 TYR ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA SEQRES 56 C 847 GLU ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA SEQRES 57 C 847 PHE ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER SEQRES 58 C 847 GLN LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE SEQRES 59 C 847 ARG SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO SEQRES 60 C 847 TRP LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS SEQRES 61 C 847 GLU ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL SEQRES 62 C 847 ARG TYR GLN GLU CYS ASP SER ARG SER ASN ALA PRO ALA SEQRES 63 C 847 THR LEU THR PHE GLU ASN MET ALA GLY VAL PHE MET LEU SEQRES 64 C 847 VAL ALA GLY GLY ILE VAL ALA GLY ILE PHE LEU ILE PHE SEQRES 65 C 847 ILE GLU ILE ALA TYR LYS ARG HIS LYS ASP ALA ARG ARG SEQRES 66 C 847 LYS GLN SEQRES 1 D 866 MET GLY ARG LEU GLY TYR TRP THR LEU LEU VAL LEU PRO SEQRES 2 D 866 ALA LEU LEU VAL TRP ARG ASP PRO ALA GLN ASN ALA ALA SEQRES 3 D 866 ALA GLU LYS GLY PRO PRO ALA LEU ASN ILE ALA VAL LEU SEQRES 4 D 866 LEU GLY HIS SER HIS ASP VAL THR GLU ARG GLU LEU ARG SEQRES 5 D 866 ASN LEU TRP GLY PRO GLU GLN ALA THR GLY LEU PRO LEU SEQRES 6 D 866 ASP VAL ASN VAL VAL ALA LEU LEU MET ASN ARG THR ASP SEQRES 7 D 866 PRO LYS SER LEU ILE THR HIS VAL CYS ASP LEU MET SER SEQRES 8 D 866 GLY ALA ARG ILE HIS GLY LEU VAL PHE GLY ASP ASP THR SEQRES 9 D 866 ASP GLN GLU ALA VAL ALA GLN MET LEU ASP PHE ILE SER SEQRES 10 D 866 SER GLN THR PHE ILE PRO ILE LEU GLY ILE HIS GLY GLY SEQRES 11 D 866 ALA SER MET ILE MET ALA ASP LYS ASP PRO THR SER THR SEQRES 12 D 866 PHE PHE GLN PHE GLY ALA SER ILE GLN GLN GLN ALA THR SEQRES 13 D 866 VAL MET LEU LYS ILE MET GLN ASP TYR ASP TRP HIS VAL SEQRES 14 D 866 PHE SER LEU VAL THR THR ILE PHE PRO GLY TYR ARG ASP SEQRES 15 D 866 PHE ILE SER PHE ILE LYS THR THR VAL ASP ASN SER PHE SEQRES 16 D 866 VAL GLY TRP ASP MET GLN ASN VAL ILE THR LEU ASP THR SEQRES 17 D 866 SER PHE GLU ASP ALA LYS THR GLN VAL GLN LEU LYS LYS SEQRES 18 D 866 ILE HIS SER SER VAL ILE LEU LEU TYR CYS SER LYS ASP SEQRES 19 D 866 GLU ALA VAL LEU ILE LEU SER GLU ALA ARG SER LEU GLY SEQRES 20 D 866 LEU THR GLY TYR ASP PHE PHE TRP ILE VAL PRO SER LEU SEQRES 21 D 866 VAL SER GLY ASN THR GLU LEU ILE PRO LYS GLU PHE PRO SEQRES 22 D 866 SER GLY LEU ILE SER VAL SER TYR ASP ASP TRP ASP TYR SEQRES 23 D 866 SER LEU GLU ALA ARG VAL ARG ASP GLY LEU GLY ILE LEU SEQRES 24 D 866 THR THR ALA ALA SER SER MET LEU GLU LYS PHE SER TYR SEQRES 25 D 866 ILE PRO GLU ALA LYS ALA SER CYS TYR GLY GLN ALA GLU SEQRES 26 D 866 LYS PRO GLU THR PRO LEU HIS THR LEU HIS GLN PHE MET SEQRES 27 D 866 VAL ASN VAL THR TRP ASP GLY LYS ASP LEU SER PHE THR SEQRES 28 D 866 GLU GLU GLY TYR GLN VAL HIS PRO ARG LEU VAL VAL ILE SEQRES 29 D 866 VAL LEU ASN LYS ASP ARG GLU TRP GLU LYS VAL GLY LYS SEQRES 30 D 866 TRP GLU ASN GLN THR LEU SER LEU ARG HIS ALA VAL TRP SEQRES 31 D 866 PRO ARG TYR LYS SER PHE SER ASP CYS GLU PRO ASP ASP SEQRES 32 D 866 ASN HIS LEU SER ILE VAL THR LEU GLU GLU ALA PRO PHE SEQRES 33 D 866 VAL ILE VAL GLU ASP ILE ASP PRO LEU THR GLU THR CYS SEQRES 34 D 866 VAL ARG ASN THR VAL PRO CYS ARG LYS PHE VAL LYS ILE SEQRES 35 D 866 ASN ASN SER THR ASN GLU GLY MET ASN VAL LYS LYS CYS SEQRES 36 D 866 CYS LYS GLY PHE CYS ILE ASP ILE LEU LYS LYS LEU SER SEQRES 37 D 866 ARG THR VAL LYS PHE THR TYR ASP LEU TYR LEU VAL THR SEQRES 38 D 866 ASN GLY LYS HIS GLY LYS LYS VAL ASN ASN VAL TRP ASN SEQRES 39 D 866 GLY MET ILE GLY GLU VAL VAL TYR GLN ARG ALA VAL MET SEQRES 40 D 866 ALA VAL GLY SER LEU THR ILE ASN GLU GLU ARG SER GLU SEQRES 41 D 866 VAL VAL ASP PHE SER VAL PRO PHE VAL GLU THR GLY ILE SEQRES 42 D 866 SER VAL MET VAL SER ARG SER ASN GLY THR VAL SER PRO SEQRES 43 D 866 SER ALA PHE LEU GLU PRO PHE SER ALA SER VAL TRP VAL SEQRES 44 D 866 MET MET PHE VAL MET LEU LEU ILE VAL SER ALA ILE ALA SEQRES 45 D 866 VAL PHE VAL PHE GLU TYR PHE SER PRO VAL GLY TYR ASN SEQRES 46 D 866 ARG ASN LEU ALA LYS GLY LYS ALA PRO HIS GLY PRO SER SEQRES 47 D 866 PHE THR ILE GLY LYS ALA ILE TRP LEU LEU TRP GLY LEU SEQRES 48 D 866 VAL PHE ASN ASN SER VAL PRO VAL GLN ASN PRO LYS GLY SEQRES 49 D 866 THR THR SER LYS ILE MET VAL SER VAL TRP ALA PHE PHE SEQRES 50 D 866 ALA VAL ILE PHE LEU ALA SER TYR THR ALA ASN LEU ALA SEQRES 51 D 866 ALA PHE MET ILE GLN GLU GLU PHE VAL ASP GLN VAL THR SEQRES 52 D 866 GLY LEU SER ASP LYS LYS PHE GLN ARG PRO HIS ASP TYR SEQRES 53 D 866 SER PRO PRO PHE ARG PHE GLY THR VAL PRO ASN GLY SER SEQRES 54 D 866 THR GLU ARG ASN ILE ARG ASN ASN TYR PRO TYR MET HIS SEQRES 55 D 866 GLN TYR MET THR ARG PHE ASN GLN ARG GLY VAL GLU ASP SEQRES 56 D 866 ALA LEU VAL SER LEU LYS THR GLY LYS LEU ASP ALA PHE SEQRES 57 D 866 ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS ALA GLY ARG SEQRES 58 D 866 ASP GLU GLY CYS LYS LEU VAL THR ILE GLY SER GLY TYR SEQRES 59 D 866 ILE PHE ALA THR THR GLY TYR GLY ILE ALA LEU GLN LYS SEQRES 60 D 866 GLY SER PRO TRP LYS ARG GLN ILE ASP LEU ALA LEU LEU SEQRES 61 D 866 GLN PHE VAL GLY ASP GLY GLU MET GLU GLU LEU GLU THR SEQRES 62 D 866 LEU TRP LEU THR GLY ILE CYS HIS ASN GLU LYS ASN GLU SEQRES 63 D 866 VAL MET SER SER GLN LEU ASP ILE ASP ASN MET ALA GLY SEQRES 64 D 866 VAL PHE TYR MET LEU ALA ALA ALA MET ALA LEU SER LEU SEQRES 65 D 866 ILE THR PHE ILE TRP GLU HIS LEU PHE TYR TRP LYS LEU SEQRES 66 D 866 ARG PHE CYS PHE THR GLY VAL CYS SER ASP ARG PRO GLY SEQRES 67 D 866 LEU LEU PHE SER ILE SER ARG GLY SEQRES 1 L 141 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 L 141 ALA ALA HIS SER ALA PHE ALA GLN VAL GLN LEU GLN GLN SEQRES 3 L 141 SER GLY ALA GLU LEU MET LYS PRO GLY ALA SER VAL LYS SEQRES 4 L 141 ILE SER CYS LYS ALA THR GLY TYR THR PHE ARG SER TYR SEQRES 5 L 141 TRP ILE GLU TRP LEU LYS GLN ARG PRO GLY HIS GLY LEU SEQRES 6 L 141 GLU TRP ILE GLY GLU ILE LEU PRO GLY SER GLY ARG THR SEQRES 7 L 141 ASN TYR ASN GLU LYS PHE LYS GLY LYS ALA THR ILE THR SEQRES 8 L 141 ALA ASP THR SER SER ASN THR ALA TYR MET GLN LEU SER SEQRES 9 L 141 SER LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS THR SEQRES 10 L 141 ARG SER ARG GLY THR MET ILE THR ARG GLU PHE THR TYR SEQRES 11 L 141 TRP GLY GLN GLY ALA LEU VAL THR VAL SER ALA SEQRES 1 M 131 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 M 131 ALA ALA HIS SER ALA PHE ALA ASP ILE VAL LEU THR GLN SEQRES 3 M 131 SER PRO ALA SER LEU ALA VAL SER LEU GLY GLN ARG ALA SEQRES 4 M 131 THR ILE SER CYS ARG ALA SER GLU SER VAL GLU TYR TYR SEQRES 5 M 131 GLY THR THR LEU MET GLN TRP TYR GLN GLN LYS PRO GLY SEQRES 6 M 131 GLN PRO PRO LYS LEU LEU ILE TYR ALA ALA SER ASN VAL SEQRES 7 M 131 ASP SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SER SEQRES 8 M 131 GLY THR ASP PHE SER LEU ASN ILE HIS PRO VAL GLU GLU SEQRES 9 M 131 ASP ASP ILE ALA MET TYR PHE CYS GLN GLN SER ARG LYS SEQRES 10 M 131 VAL PRO SER THR PHE GLY GLY GLY THR LYS LEU GLU ILE SEQRES 11 M 131 LYS HET GLY A 901 5 HET NAG A 902 14 HET NAG A 903 14 HET NAG A 904 14 HET NAG A 905 14 HET GLU B 901 10 HET NAG B 902 14 HET NAG B 903 14 HET NAG B 904 14 HET NAG B 905 14 HET GLY C 901 5 HET NAG C 902 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 GLU D 901 10 HET NAG D 902 14 HET NAG D 903 14 HETNAM GLY GLYCINE HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM GLU GLUTAMIC 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 9 GLY 2(C2 H5 N O2) FORMUL 10 NAG 16(C8 H15 N O6) FORMUL 14 GLU 2(C5 H9 N O4) HELIX 1 AA1 THR J 47 TYR J 51 5 5 HELIX 2 AA2 THR A 35 HIS A 53 1 19 HELIX 3 AA3 ASN A 70 SER A 84 1 15 HELIX 4 AA4 PRO A 104 TYR A 114 1 11 HELIX 5 AA5 SER A 126 ASP A 130 5 5 HELIX 6 AA6 HIS A 146 TYR A 158 1 13 HELIX 7 AA7 ASP A 170 GLU A 186 1 17 HELIX 8 AA8 VAL A 204 GLU A 213 1 10 HELIX 9 AA9 SER A 224 ASN A 239 1 16 HELIX 10 AB1 GLU A 251 ILE A 254 5 4 HELIX 11 AB2 SER A 255 TYR A 261 1 7 HELIX 12 AB3 ASN A 276 GLU A 297 1 22 HELIX 13 AB4 THR A 317 SER A 327 1 11 HELIX 14 AB5 PHE A 458 ASN A 471 1 14 HELIX 15 AB6 ASN A 499 SER A 507 1 9 HELIX 16 AB7 ASN A 520 GLN A 525 1 6 HELIX 17 AB8 THR A 561 SER A 584 1 24 HELIX 18 AB9 LEU A 603 ASN A 616 1 14 HELIX 19 AC1 SER A 628 LEU A 657 1 30 HELIX 20 AC2 THR A 665 ASN A 668 5 4 HELIX 21 AC3 ASP A 669 ASN A 674 1 6 HELIX 22 AC4 SER A 687 GLN A 696 1 10 HELIX 23 AC5 LEU A 699 GLU A 707 1 9 HELIX 24 AC6 SER A 713 ASP A 723 1 11 HELIX 25 AC7 SER A 733 LYS A 743 1 11 HELIX 26 AC8 LYS A 769 ASN A 782 1 14 HELIX 27 AC9 GLY A 783 VAL A 793 1 11 HELIX 28 AD1 ASN A 812 LYS A 838 1 27 HELIX 29 AD2 THR B 47 LEU B 54 1 8 HELIX 30 AD3 LYS B 80 MET B 90 1 11 HELIX 31 AD4 ALA B 108 PHE B 121 1 14 HELIX 32 AD5 SER B 150 TYR B 165 1 16 HELIX 33 AD6 GLY B 179 ASN B 193 1 15 HELIX 34 AD7 LYS B 214 LYS B 221 1 8 HELIX 35 AD8 SER B 232 GLY B 247 1 16 HELIX 36 AD9 SER B 287 PHE B 310 1 24 HELIX 37 AE1 LEU B 334 MET B 338 5 5 HELIX 38 AE2 GLY B 458 LYS B 472 1 15 HELIX 39 AE3 ASN B 494 TYR B 502 1 9 HELIX 40 AE4 ASN B 515 VAL B 522 1 8 HELIX 41 AE5 SER B 556 PHE B 579 1 24 HELIX 42 AE6 LYS B 603 PHE B 613 1 11 HELIX 43 AE7 GLY B 624 GLN B 655 1 32 HELIX 44 AE8 ASP B 667 ARG B 672 1 6 HELIX 45 AE9 GLY B 688 TYR B 698 1 11 HELIX 46 AF1 TYR B 698 THR B 706 1 9 HELIX 47 AF2 ARG B 707 ASN B 709 5 3 HELIX 48 AF3 GLY B 712 GLY B 723 1 12 HELIX 49 AF4 ALA B 732 ARG B 741 1 10 HELIX 50 AF5 TRP B 771 GLY B 784 1 14 HELIX 51 AF6 GLY B 786 LEU B 796 1 11 HELIX 52 AF7 ASP B 813 ILE B 836 1 24 HELIX 53 AF8 THR C 35 ASN C 50 1 16 HELIX 54 AF9 ASN C 70 LEU C 82 1 13 HELIX 55 AG1 ILE C 83 SER C 85 5 3 HELIX 56 AG2 PRO C 104 PHE C 113 1 10 HELIX 57 AG3 SER C 126 ASP C 130 5 5 HELIX 58 AG4 HIS C 146 ASN C 159 1 14 HELIX 59 AG5 GLU C 172 GLU C 188 1 17 HELIX 60 AG6 VAL C 204 GLU C 213 1 10 HELIX 61 AG7 SER C 224 LEU C 238 1 15 HELIX 62 AG8 GLU C 251 SER C 255 5 5 HELIX 63 AG9 GLY C 256 TYR C 261 1 6 HELIX 64 AH1 GLU C 277 LEU C 296 1 20 HELIX 65 AH2 THR C 317 SER C 327 1 11 HELIX 66 AH3 PHE C 458 MET C 470 1 13 HELIX 67 AH4 ASN C 499 SER C 507 1 9 HELIX 68 AH5 ASN C 520 ILE C 527 1 8 HELIX 69 AH6 THR C 561 SER C 584 1 24 HELIX 70 AH7 ALA C 606 ASN C 616 1 11 HELIX 71 AH8 SER C 628 LEU C 657 1 30 HELIX 72 AH9 ASP C 669 ASN C 674 1 6 HELIX 73 AI1 SER C 687 GLN C 696 1 10 HELIX 74 AI2 LEU C 699 GLU C 707 1 9 HELIX 75 AI3 SER C 713 ASP C 723 1 11 HELIX 76 AI4 SER C 733 LYS C 743 1 11 HELIX 77 AI5 LYS C 769 ASN C 782 1 14 HELIX 78 AI6 GLY C 783 VAL C 793 1 11 HELIX 79 AI7 MET C 813 LYS C 838 1 26 HELIX 80 AI8 SER D 43 ASP D 45 5 3 HELIX 81 AI9 THR D 47 ASN D 53 1 7 HELIX 82 AJ1 LEU D 54 GLN D 59 1 6 HELIX 83 AJ2 LYS D 80 MET D 90 1 11 HELIX 84 AJ3 ALA D 108 PHE D 121 1 14 HELIX 85 AJ4 HIS D 128 MET D 133 5 6 HELIX 86 AJ5 SER D 150 ASP D 166 1 17 HELIX 87 AJ6 GLY D 179 ASN D 193 1 15 HELIX 88 AJ7 LYS D 214 LYS D 220 1 7 HELIX 89 AJ8 SER D 232 LEU D 246 1 15 HELIX 90 AJ9 SER D 287 PHE D 310 1 24 HELIX 91 AK1 HIS D 335 VAL D 339 5 5 HELIX 92 AK2 GLY D 458 LYS D 472 1 15 HELIX 93 AK3 GLY D 495 TYR D 502 1 8 HELIX 94 AK4 GLU D 516 VAL D 522 1 7 HELIX 95 AK5 SER D 556 PHE D 579 1 24 HELIX 96 AK6 LYS D 603 ASN D 614 1 12 HELIX 97 AK7 GLY D 624 GLN D 655 1 32 HELIX 98 AK8 ASP D 667 ARG D 672 1 6 HELIX 99 AK9 SER D 689 TYR D 698 1 10 HELIX 100 AL1 TYR D 698 PHE D 708 1 11 HELIX 101 AL2 GLY D 712 GLY D 723 1 12 HELIX 102 AL3 ALA D 732 ARG D 741 1 10 HELIX 103 AL4 TRP D 771 GLY D 784 1 14 HELIX 104 AL5 GLY D 786 LEU D 796 1 11 HELIX 105 AL6 ASP D 813 TRP D 837 1 25 HELIX 106 AL7 THR L 47 TYR L 51 5 5 SHEET 1 AA1 4 LEU J 23 GLN J 24 0 SHEET 2 AA1 4 LYS J 38 ALA J 43 -1 O LYS J 42 N GLN J 24 SHEET 3 AA1 4 THR J 97 LEU J 102 -1 O ALA J 98 N CYS J 41 SHEET 4 AA1 4 ALA J 87 ASP J 92 -1 N THR J 90 O TYR J 99 SHEET 1 AA2 6 GLU J 29 LEU J 30 0 SHEET 2 AA2 6 ALA J 134 THR J 137 1 O LEU J 135 N GLU J 29 SHEET 3 AA2 6 VAL J 112 ARG J 117 -1 N TYR J 113 O ALA J 134 SHEET 4 AA2 6 ILE J 53 GLN J 58 -1 N GLU J 54 O THR J 116 SHEET 5 AA2 6 GLY J 68 ILE J 70 -1 O GLY J 68 N TRP J 55 SHEET 6 AA2 6 THR J 77 TYR J 79 -1 O ASN J 78 N GLU J 69 SHEET 1 AA3 4 GLU J 29 LEU J 30 0 SHEET 2 AA3 4 ALA J 134 THR J 137 1 O LEU J 135 N GLU J 29 SHEET 3 AA3 4 VAL J 112 ARG J 117 -1 N TYR J 113 O ALA J 134 SHEET 4 AA3 4 TYR J 129 TRP J 130 -1 O TYR J 129 N ARG J 117 SHEET 1 AA4 4 LEU K 24 SER K 27 0 SHEET 2 AA4 4 ALA K 39 ALA K 45 -1 O ARG K 44 N THR K 25 SHEET 3 AA4 4 ASP K 94 ILE K 99 -1 O LEU K 97 N ILE K 41 SHEET 4 AA4 4 PHE K 86 SER K 91 -1 N SER K 89 O SER K 96 SHEET 1 AA5 2 SER K 30 LEU K 31 0 SHEET 2 AA5 2 LYS K 127 LEU K 128 1 O LYS K 127 N LEU K 31 SHEET 1 AA6 2 GLU K 50 TYR K 51 0 SHEET 2 AA6 2 THR K 54 THR K 55 -1 O THR K 54 N TYR K 51 SHEET 1 AA7 4 ASN K 77 VAL K 78 0 SHEET 2 AA7 4 LYS K 69 TYR K 73 -1 N TYR K 73 O ASN K 77 SHEET 3 AA7 4 GLN K 58 GLN K 62 -1 N GLN K 61 O LYS K 69 SHEET 4 AA7 4 MET K 109 GLN K 113 -1 O PHE K 111 N TYR K 60 SHEET 1 AA8 5 GLN A 59 VAL A 65 0 SHEET 2 AA8 5 ILE A 26 VAL A 32 1 N VAL A 27 O ASN A 61 SHEET 3 AA8 5 VAL A 87 VAL A 92 1 O LEU A 91 N VAL A 32 SHEET 4 AA8 5 VAL A 118 GLY A 120 1 O LEU A 119 N ILE A 90 SHEET 5 AA8 5 PHE A 137 ARG A 139 1 O LEU A 138 N GLY A 120 SHEET 1 AA9 4 LYS A 193 GLN A 196 0 SHEET 2 AA9 4 ILE A 163 VAL A 167 1 N VAL A 167 O LEU A 195 SHEET 3 AA9 4 VAL A 218 ILE A 220 1 O VAL A 218 N ILE A 164 SHEET 4 AA9 4 VAL A 246 LEU A 248 1 O VAL A 246 N ILE A 219 SHEET 1 AB1 4 ILE A 267 LEU A 271 0 SHEET 2 AB1 4 TYR A 351 LEU A 356 -1 O SER A 352 N GLN A 270 SHEET 3 AB1 4 LEU A 361 TYR A 367 -1 O VAL A 362 N ASN A 355 SHEET 4 AB1 4 VAL A 372 PRO A 374 -1 O ILE A 373 N ILE A 366 SHEET 1 AB2 7 VAL A 476 LEU A 478 0 SHEET 2 AB2 7 ILE A 400 THR A 402 1 N THR A 402 O HIS A 477 SHEET 3 AB2 7 MET A 512 THR A 518 1 O MET A 512 N VAL A 401 SHEET 4 AB2 7 PHE A 753 GLY A 761 -1 O GLY A 759 N LEU A 517 SHEET 5 AB2 7 TYR A 535 LYS A 543 -1 N LEU A 538 O PHE A 753 SHEET 6 AB2 7 ALA A 728 ASP A 732 -1 O PHE A 729 N LEU A 541 SHEET 7 AB2 7 TYR A 681 ALA A 682 1 N ALA A 682 O ILE A 730 SHEET 1 AB3 6 VAL A 476 LEU A 478 0 SHEET 2 AB3 6 ILE A 400 THR A 402 1 N THR A 402 O HIS A 477 SHEET 3 AB3 6 MET A 512 THR A 518 1 O MET A 512 N VAL A 401 SHEET 4 AB3 6 PHE A 753 GLY A 761 -1 O GLY A 759 N LEU A 517 SHEET 5 AB3 6 TYR A 535 LYS A 543 -1 N LEU A 538 O PHE A 753 SHEET 6 AB3 6 LEU A 746 THR A 748 -1 O VAL A 747 N VAL A 542 SHEET 1 AB4 3 VAL A 409 PRO A 413 0 SHEET 2 AB4 3 THR A 450 GLY A 457 -1 O CYS A 454 N LYS A 412 SHEET 3 AB4 3 VAL A 434 PRO A 439 -1 N VAL A 434 O CYS A 455 SHEET 1 AB5 2 GLN A 487 ARG A 489 0 SHEET 2 AB5 2 LYS A 496 TRP A 498 -1 O GLU A 497 N GLU A 488 SHEET 1 AB6 5 VAL B 70 MET B 74 0 SHEET 2 AB6 5 ALA B 37 GLY B 41 1 N LEU B 40 O MET B 74 SHEET 3 AB6 5 LEU B 98 PHE B 100 1 O VAL B 99 N LEU B 39 SHEET 4 AB6 5 ILE B 124 GLY B 126 1 O LEU B 125 N PHE B 100 SHEET 5 AB6 5 PHE B 144 PHE B 145 1 O PHE B 145 N ILE B 124 SHEET 1 AB7 3 ASP B 199 MET B 200 0 SHEET 2 AB7 3 VAL B 169 THR B 174 1 N PHE B 170 O ASP B 199 SHEET 3 AB7 3 ILE B 204 THR B 205 1 O ILE B 204 N LEU B 172 SHEET 1 AB8 7 ASP B 199 MET B 200 0 SHEET 2 AB8 7 VAL B 169 THR B 174 1 N PHE B 170 O ASP B 199 SHEET 3 AB8 7 VAL B 226 TYR B 230 1 O LEU B 228 N VAL B 173 SHEET 4 AB8 7 PHE B 254 VAL B 257 1 O PHE B 254 N ILE B 227 SHEET 5 AB8 7 ILE B 277 TYR B 281 1 O ILE B 277 N VAL B 257 SHEET 6 AB8 7 LEU B 361 LEU B 366 -1 O VAL B 362 N SER B 280 SHEET 7 AB8 7 TRP B 372 LYS B 377 -1 O VAL B 375 N VAL B 363 SHEET 1 AB9 2 THR B 342 TRP B 343 0 SHEET 2 AB9 2 LYS B 346 ASP B 347 -1 O LYS B 346 N TRP B 343 SHEET 1 AC1 5 THR B 474 LEU B 479 0 SHEET 2 AC1 5 HIS B 405 THR B 410 1 N LEU B 406 O THR B 474 SHEET 3 AC1 5 MET B 507 ALA B 508 1 O MET B 507 N VAL B 409 SHEET 4 AC1 5 ALA B 764 LEU B 765 -1 O ALA B 764 N ALA B 508 SHEET 5 AC1 5 ASP B 523 PHE B 524 -1 N ASP B 523 O LEU B 765 SHEET 1 AC2 3 ILE B 418 GLU B 420 0 SHEET 2 AC2 3 CYS B 455 LYS B 457 -1 O CYS B 455 N GLU B 420 SHEET 3 AC2 3 VAL B 434 PRO B 435 -1 N VAL B 434 O CYS B 456 SHEET 1 AC3 2 LYS B 438 LYS B 441 0 SHEET 2 AC3 2 GLY B 449 VAL B 452 -1 O VAL B 452 N LYS B 438 SHEET 1 AC4 2 GLU B 530 THR B 531 0 SHEET 2 AC4 2 THR B 759 GLY B 760 -1 O THR B 759 N THR B 531 SHEET 1 AC5 4 PHE B 682 GLY B 683 0 SHEET 2 AC5 4 ALA B 727 ASP B 731 1 O ALA B 727 N GLY B 683 SHEET 3 AC5 4 ILE B 533 VAL B 537 -1 N MET B 536 O PHE B 728 SHEET 4 AC5 4 VAL B 748 THR B 749 -1 O VAL B 748 N VAL B 537 SHEET 1 AC6 5 LEU C 60 THR C 66 0 SHEET 2 AC6 5 VAL C 27 LEU C 33 1 N ILE C 29 O ASN C 61 SHEET 3 AC6 5 VAL C 87 VAL C 92 1 O LEU C 91 N VAL C 32 SHEET 4 AC6 5 VAL C 118 GLY C 120 1 O LEU C 119 N ILE C 90 SHEET 5 AC6 5 PHE C 137 ARG C 139 1 O LEU C 138 N GLY C 120 SHEET 1 AC7 4 LYS C 193 LEU C 195 0 SHEET 2 AC7 4 ILE C 164 VAL C 167 1 N LEU C 165 O LEU C 195 SHEET 3 AC7 4 VAL C 218 SER C 222 1 O ILE C 220 N LEU C 166 SHEET 4 AC7 4 VAL C 246 LEU C 248 1 O LEU C 248 N ILE C 219 SHEET 1 AC8 3 ILE C 267 LEU C 271 0 SHEET 2 AC8 3 TYR C 351 LEU C 356 -1 O MET C 354 N GLY C 268 SHEET 3 AC8 3 LEU C 361 GLN C 363 -1 O VAL C 362 N ASN C 355 SHEET 1 AC9 2 GLY C 365 ASN C 368 0 SHEET 2 AC9 2 HIS C 371 PRO C 374 -1 O ILE C 373 N ILE C 366 SHEET 1 AD1 7 HIS C 477 LEU C 478 0 SHEET 2 AD1 7 ILE C 400 THR C 402 1 N THR C 402 O HIS C 477 SHEET 3 AD1 7 MET C 512 THR C 518 1 O VAL C 514 N VAL C 401 SHEET 4 AD1 7 PHE C 753 GLY C 761 -1 O GLY C 759 N LEU C 517 SHEET 5 AD1 7 TYR C 535 LYS C 543 -1 N GLN C 536 O SER C 756 SHEET 6 AD1 7 ALA C 728 ASP C 732 -1 O PHE C 729 N LEU C 541 SHEET 7 AD1 7 TYR C 681 ALA C 682 1 N ALA C 682 O ILE C 730 SHEET 1 AD2 6 HIS C 477 LEU C 478 0 SHEET 2 AD2 6 ILE C 400 THR C 402 1 N THR C 402 O HIS C 477 SHEET 3 AD2 6 MET C 512 THR C 518 1 O VAL C 514 N VAL C 401 SHEET 4 AD2 6 PHE C 753 GLY C 761 -1 O GLY C 759 N LEU C 517 SHEET 5 AD2 6 TYR C 535 LYS C 543 -1 N GLN C 536 O SER C 756 SHEET 6 AD2 6 LEU C 746 THR C 748 -1 O VAL C 747 N VAL C 542 SHEET 1 AD3 3 VAL C 409 PRO C 413 0 SHEET 2 AD3 3 THR C 450 GLY C 457 -1 O TYR C 456 N TYR C 410 SHEET 3 AD3 3 THR C 437 PRO C 439 -1 N GLY C 438 O VAL C 451 SHEET 1 AD4 2 GLU C 488 ARG C 489 0 SHEET 2 AD4 2 LYS C 496 GLU C 497 -1 O GLU C 497 N GLU C 488 SHEET 1 AD5 5 VAL D 67 MET D 74 0 SHEET 2 AD5 5 LEU D 34 GLY D 41 1 N LEU D 40 O LEU D 72 SHEET 3 AD5 5 GLY D 97 GLY D 101 1 O GLY D 101 N LEU D 39 SHEET 4 AD5 5 ILE D 124 GLY D 126 1 O LEU D 125 N PHE D 100 SHEET 5 AD5 5 PHE D 144 GLN D 146 1 O PHE D 145 N ILE D 124 SHEET 1 AD6 8 ILE D 204 THR D 205 0 SHEET 2 AD6 8 PHE D 170 THR D 174 1 N LEU D 172 O ILE D 204 SHEET 3 AD6 8 VAL D 226 TYR D 230 1 O LEU D 228 N VAL D 173 SHEET 4 AD6 8 PHE D 254 VAL D 257 1 O PHE D 254 N ILE D 227 SHEET 5 AD6 8 ILE D 277 TYR D 281 1 O ILE D 277 N VAL D 257 SHEET 6 AD6 8 LEU D 361 LEU D 366 -1 O ILE D 364 N SER D 278 SHEET 7 AD6 8 TRP D 372 GLU D 379 -1 O GLY D 376 N VAL D 363 SHEET 8 AD6 8 THR D 382 LEU D 383 -1 O THR D 382 N GLU D 379 SHEET 1 AD7 2 THR D 342 TRP D 343 0 SHEET 2 AD7 2 LYS D 346 ASP D 347 -1 O LYS D 346 N TRP D 343 SHEET 1 AD8 4 THR D 474 LEU D 479 0 SHEET 2 AD8 4 HIS D 405 THR D 410 1 N LEU D 406 O THR D 474 SHEET 3 AD8 4 MET D 507 ALA D 508 1 O MET D 507 N VAL D 409 SHEET 4 AD8 4 ALA D 764 LEU D 765 -1 O ALA D 764 N ALA D 508 SHEET 1 AD9 3 ILE D 418 GLU D 420 0 SHEET 2 AD9 3 GLY D 449 LYS D 457 -1 O LYS D 457 N ILE D 418 SHEET 3 AD9 3 VAL D 434 LYS D 441 -1 N VAL D 440 O MET D 450 SHEET 1 AE1 3 PHE D 728 ASP D 731 0 SHEET 2 AE1 3 ILE D 533 VAL D 537 -1 N MET D 536 O PHE D 728 SHEET 3 AE1 3 VAL D 748 THR D 749 -1 O VAL D 748 N VAL D 537 SHEET 1 AE2 4 LEU L 23 GLN L 24 0 SHEET 2 AE2 4 VAL L 37 ALA L 43 -1 O LYS L 42 N GLN L 24 SHEET 3 AE2 4 THR L 97 LEU L 102 -1 O ALA L 98 N CYS L 41 SHEET 4 AE2 4 ALA L 87 ASP L 92 -1 N THR L 90 O TYR L 99 SHEET 1 AE3 6 GLU L 29 LEU L 30 0 SHEET 2 AE3 6 ALA L 134 THR L 137 1 O LEU L 135 N GLU L 29 SHEET 3 AE3 6 VAL L 112 ARG L 117 -1 N TYR L 113 O ALA L 134 SHEET 4 AE3 6 ILE L 53 GLN L 58 -1 N GLU L 54 O THR L 116 SHEET 5 AE3 6 GLY L 68 ILE L 70 -1 O ILE L 70 N ILE L 53 SHEET 6 AE3 6 THR L 77 TYR L 79 -1 O ASN L 78 N GLU L 69 SHEET 1 AE4 4 GLU L 29 LEU L 30 0 SHEET 2 AE4 4 ALA L 134 THR L 137 1 O LEU L 135 N GLU L 29 SHEET 3 AE4 4 VAL L 112 ARG L 117 -1 N TYR L 113 O ALA L 134 SHEET 4 AE4 4 TYR L 129 TRP L 130 -1 O TYR L 129 N ARG L 117 SHEET 1 AE5 4 GLN M 26 SER M 27 0 SHEET 2 AE5 4 ALA M 39 ARG M 44 -1 O SER M 42 N SER M 27 SHEET 3 AE5 4 ASP M 94 ILE M 99 -1 O PHE M 95 N CYS M 43 SHEET 4 AE5 4 PHE M 86 SER M 91 -1 N SER M 87 O ASN M 98 SHEET 1 AE6 2 SER M 30 ALA M 32 0 SHEET 2 AE6 2 LYS M 127 GLU M 129 1 O LYS M 127 N LEU M 31 SHEET 1 AE7 2 GLU M 50 TYR M 51 0 SHEET 2 AE7 2 THR M 54 THR M 55 -1 O THR M 54 N TYR M 51 SHEET 1 AE8 5 ASN M 77 VAL M 78 0 SHEET 2 AE8 5 LYS M 69 TYR M 73 -1 N TYR M 73 O ASN M 77 SHEET 3 AE8 5 GLN M 58 GLN M 62 -1 N GLN M 61 O LYS M 69 SHEET 4 AE8 5 MET M 109 GLN M 114 -1 O GLN M 113 N GLN M 58 SHEET 5 AE8 5 THR M 121 PHE M 122 -1 O THR M 121 N GLN M 114 SSBOND 1 CYS J 41 CYS J 115 1555 1555 2.03 SSBOND 2 CYS K 43 CYS K 112 1555 1555 2.04 SSBOND 3 CYS A 79 CYS A 308 1555 1555 2.02 SSBOND 4 CYS A 420 CYS A 454 1555 1555 2.03 SSBOND 5 CYS A 436 CYS A 455 1555 1555 2.03 SSBOND 6 CYS B 87 CYS B 320 1555 1555 2.03 SSBOND 7 CYS B 429 CYS B 455 1555 1555 2.03 SSBOND 8 CYS C 79 CYS C 308 1555 1555 2.03 SSBOND 9 CYS C 420 CYS C 454 1555 1555 2.03 SSBOND 10 CYS C 436 CYS C 455 1555 1555 2.03 SSBOND 11 CYS D 87 CYS D 320 1555 1555 2.03 SSBOND 12 CYS D 429 CYS D 455 1555 1555 2.03 SSBOND 13 CYS D 745 CYS D 800 1555 1555 2.03 SSBOND 14 CYS L 41 CYS L 115 1555 1555 2.04 SSBOND 15 CYS M 43 CYS M 112 1555 1555 2.03 LINK ND2 ASN A 61 C1 NAG A 902 1555 1555 1.45 LINK ND2 ASN A 239 C1 NAG A 903 1555 1555 1.45 LINK ND2 ASN A 350 C1 NAG A 904 1555 1555 1.45 LINK ND2 ASN A 771 C1 NAG A 905 1555 1555 1.45 LINK ND2 ASN B 75 C1 NAG B 902 1555 1555 1.44 LINK ND2 ASN B 340 C1 NAG B 903 1555 1555 1.44 LINK ND2 ASN B 380 C1 NAG B 904 1555 1555 1.44 LINK ND2 ASN B 687 C1 NAG B 905 1555 1555 1.45 LINK ND2 ASN C 61 C1 NAG C 902 1555 1555 1.44 LINK ND2 ASN C 203 C1 NAG C 903 1555 1555 1.45 LINK ND2 ASN C 239 C1 NAG C 904 1555 1555 1.47 LINK ND2 ASN C 276 C1 NAG C 905 1555 1555 1.44 LINK ND2 ASN C 350 C1 NAG C 906 1555 1555 1.44 LINK ND2 ASN C 771 C1 NAG C 907 1555 1555 1.44 LINK ND2 ASN D 75 C1 NAG D 902 1555 1555 1.44 LINK ND2 ASN D 687 C1 NAG D 903 1555 1555 1.44 CISPEP 1 SER K 27 PRO K 28 0 -1.90 CISPEP 2 HIS K 100 PRO K 101 0 -1.27 CISPEP 3 VAL K 118 PRO K 119 0 2.81 CISPEP 4 ALA B 414 PRO B 415 0 3.16 CISPEP 5 ALA D 414 PRO D 415 0 1.36 CISPEP 6 SER M 27 PRO M 28 0 -1.00 CISPEP 7 HIS M 100 PRO M 101 0 0.17 CISPEP 8 VAL M 118 PRO M 119 0 -0.15 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000