HEADER CHAPERONE 06-DEC-11 4AB3
TITLE ATP-TRIGGERED MOLECULAR MECHANICS OF THE CHAPERONIN GROEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 60 KDA CHAPERONIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;
COMPND 4 SYNONYM: HSP60, GROEL PROTEIN, PROTEIN CPN60;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: ATPASE MUTANT, CHAINS A-G ARE IN THE RDOPEN ATP BOUND
COMPND 8 CONFORMATION. CHAINS H-N ARE IN THE RD5 ATP BOUND CONFORMATION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHAPERONE
EXPDTA ELECTRON MICROSCOPY
AUTHOR D.K.CLARE,D.VASISHTAN,S.STAGG,J.QUISPE,G.W.FARR,M.TOPF,A.L.HORWICH,
AUTHOR 2 H.R.SAIBIL
REVDAT 3 23-AUG-17 4AB3 1 REMARK
REVDAT 2 25-SEP-13 4AB3 1 REMARK MASTER
REVDAT 1 12-DEC-12 4AB3 0
JRNL AUTH D.K.CLARE,D.VASISHTAN,S.STAGG,J.QUISPE,G.W.FARR,M.TOPF,
JRNL AUTH 2 A.L.HORWICH,H.R.SAIBIL
JRNL TITL ATP-TRIGGERED CONFORMATIONAL CHANGES DELINEATE
JRNL TITL 2 SUBSTRATE-BINDING AND -FOLDING MECHANICS OF THE GROEL
JRNL TITL 3 CHAPERONIN.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 149 113 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22445172
JRNL DOI 10.1016/J.CELL.2012.02.047
REMARK 2
REMARK 2 RESOLUTION. 8.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : FLEX-EM, NAMD, UCSF CHIMERA, IMAGIC,
REMARK 3 SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1OEL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--FLEXIBLE FITTING REFINEMENT PROTOCOL-
REMARK 3 -X-RAY
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 2.020
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 8.500
REMARK 3 NUMBER OF PARTICLES : 15000
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD
REMARK 3 -2003.(DEPOSITION ID: 10412).
REMARK 4
REMARK 4 4AB3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290050602.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : CRYO EM
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : GROEL-ATP14 RD5-RDOPEN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 4.00
REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : VITRIFIED WITH A VITROBOT AT
REMARK 245 100 PERCENT HUMIDITY WITH 2-3
REMARK 245 SECONDS BLOTTING TIME
REMARK 245 SAMPLE BUFFER : 50 MM TRIS-HCL PH 7.4, 50 MM
REMARK 245 KCL AND 10 MM MGCL2, 200 UM ATP
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 95.00
REMARK 245 MICROSCOPE MODEL : FEI TECNAI F20
REMARK 245 DETECTOR TYPE : GATAN ULTRASCAN 4000 (4K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 700.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.00
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 15.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : 148500
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 120
REMARK 245 IMAGING DETAILS : THE DATA WERE COLLECTED WITH
REMARK 245 LEGINON AT SCRIPPS
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: TETRADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 526
REMARK 465 ASN A 527
REMARK 465 ASP A 528
REMARK 465 ALA A 529
REMARK 465 ALA A 530
REMARK 465 ASP A 531
REMARK 465 LEU A 532
REMARK 465 GLY A 533
REMARK 465 ALA A 534
REMARK 465 ALA A 535
REMARK 465 GLY A 536
REMARK 465 GLY A 537
REMARK 465 MET A 538
REMARK 465 GLY A 539
REMARK 465 GLY A 540
REMARK 465 MET A 541
REMARK 465 GLY A 542
REMARK 465 GLY A 543
REMARK 465 MET A 544
REMARK 465 GLY A 545
REMARK 465 GLY A 546
REMARK 465 MET A 547
REMARK 465 MET A 548
REMARK 465 MET B 1
REMARK 465 LYS B 526
REMARK 465 ASN B 527
REMARK 465 ASP B 528
REMARK 465 ALA B 529
REMARK 465 ALA B 530
REMARK 465 ASP B 531
REMARK 465 LEU B 532
REMARK 465 GLY B 533
REMARK 465 ALA B 534
REMARK 465 ALA B 535
REMARK 465 GLY B 536
REMARK 465 GLY B 537
REMARK 465 MET B 538
REMARK 465 GLY B 539
REMARK 465 GLY B 540
REMARK 465 MET B 541
REMARK 465 GLY B 542
REMARK 465 GLY B 543
REMARK 465 MET B 544
REMARK 465 GLY B 545
REMARK 465 GLY B 546
REMARK 465 MET B 547
REMARK 465 MET B 548
REMARK 465 MET C 1
REMARK 465 LYS C 526
REMARK 465 ASN C 527
REMARK 465 ASP C 528
REMARK 465 ALA C 529
REMARK 465 ALA C 530
REMARK 465 ASP C 531
REMARK 465 LEU C 532
REMARK 465 GLY C 533
REMARK 465 ALA C 534
REMARK 465 ALA C 535
REMARK 465 GLY C 536
REMARK 465 GLY C 537
REMARK 465 MET C 538
REMARK 465 GLY C 539
REMARK 465 GLY C 540
REMARK 465 MET C 541
REMARK 465 GLY C 542
REMARK 465 GLY C 543
REMARK 465 MET C 544
REMARK 465 GLY C 545
REMARK 465 GLY C 546
REMARK 465 MET C 547
REMARK 465 MET C 548
REMARK 465 MET D 1
REMARK 465 LYS D 526
REMARK 465 ASN D 527
REMARK 465 ASP D 528
REMARK 465 ALA D 529
REMARK 465 ALA D 530
REMARK 465 ASP D 531
REMARK 465 LEU D 532
REMARK 465 GLY D 533
REMARK 465 ALA D 534
REMARK 465 ALA D 535
REMARK 465 GLY D 536
REMARK 465 GLY D 537
REMARK 465 MET D 538
REMARK 465 GLY D 539
REMARK 465 GLY D 540
REMARK 465 MET D 541
REMARK 465 GLY D 542
REMARK 465 GLY D 543
REMARK 465 MET D 544
REMARK 465 GLY D 545
REMARK 465 GLY D 546
REMARK 465 MET D 547
REMARK 465 MET D 548
REMARK 465 MET E 1
REMARK 465 LYS E 526
REMARK 465 ASN E 527
REMARK 465 ASP E 528
REMARK 465 ALA E 529
REMARK 465 ALA E 530
REMARK 465 ASP E 531
REMARK 465 LEU E 532
REMARK 465 GLY E 533
REMARK 465 ALA E 534
REMARK 465 ALA E 535
REMARK 465 GLY E 536
REMARK 465 GLY E 537
REMARK 465 MET E 538
REMARK 465 GLY E 539
REMARK 465 GLY E 540
REMARK 465 MET E 541
REMARK 465 GLY E 542
REMARK 465 GLY E 543
REMARK 465 MET E 544
REMARK 465 GLY E 545
REMARK 465 GLY E 546
REMARK 465 MET E 547
REMARK 465 MET E 548
REMARK 465 MET F 1
REMARK 465 LYS F 526
REMARK 465 ASN F 527
REMARK 465 ASP F 528
REMARK 465 ALA F 529
REMARK 465 ALA F 530
REMARK 465 ASP F 531
REMARK 465 LEU F 532
REMARK 465 GLY F 533
REMARK 465 ALA F 534
REMARK 465 ALA F 535
REMARK 465 GLY F 536
REMARK 465 GLY F 537
REMARK 465 MET F 538
REMARK 465 GLY F 539
REMARK 465 GLY F 540
REMARK 465 MET F 541
REMARK 465 GLY F 542
REMARK 465 GLY F 543
REMARK 465 MET F 544
REMARK 465 GLY F 545
REMARK 465 GLY F 546
REMARK 465 MET F 547
REMARK 465 MET F 548
REMARK 465 MET G 1
REMARK 465 PRO G 524A
REMARK 465 LYS G 524B
REMARK 465 ASN G 524C
REMARK 465 ASP G 524D
REMARK 465 ALA G 530
REMARK 465 ALA G 524F
REMARK 465 ASP G 524G
REMARK 465 GLY G 533
REMARK 465 ALA G 534
REMARK 465 ALA G 535
REMARK 465 GLY G 536
REMARK 465 GLY G 537
REMARK 465 MET G 538
REMARK 465 GLY G 539
REMARK 465 GLY G 540
REMARK 465 MET G 541
REMARK 465 GLY G 542
REMARK 465 GLY G 543
REMARK 465 MET G 544
REMARK 465 GLY G 545
REMARK 465 GLY G 546
REMARK 465 MET G 547
REMARK 465 MET G 548
REMARK 465 MET H 1
REMARK 465 LYS H 526
REMARK 465 ASN H 527
REMARK 465 ASP H 528
REMARK 465 ALA H 529
REMARK 465 ALA H 530
REMARK 465 ASP H 531
REMARK 465 LEU H 532
REMARK 465 GLY H 533
REMARK 465 ALA H 534
REMARK 465 ALA H 535
REMARK 465 GLY H 536
REMARK 465 GLY H 537
REMARK 465 MET H 538
REMARK 465 GLY H 539
REMARK 465 GLY H 540
REMARK 465 MET H 541
REMARK 465 GLY H 542
REMARK 465 GLY H 543
REMARK 465 MET H 544
REMARK 465 GLY H 545
REMARK 465 GLY H 546
REMARK 465 MET H 547
REMARK 465 MET H 548
REMARK 465 MET I 1
REMARK 465 LYS I 526
REMARK 465 ASN I 527
REMARK 465 ASP I 528
REMARK 465 ALA I 529
REMARK 465 ALA I 530
REMARK 465 ASP I 531
REMARK 465 LEU I 532
REMARK 465 GLY I 533
REMARK 465 ALA I 534
REMARK 465 ALA I 535
REMARK 465 GLY I 536
REMARK 465 GLY I 537
REMARK 465 MET I 538
REMARK 465 GLY I 539
REMARK 465 GLY I 540
REMARK 465 MET I 541
REMARK 465 GLY I 542
REMARK 465 GLY I 543
REMARK 465 MET I 544
REMARK 465 GLY I 545
REMARK 465 GLY I 546
REMARK 465 MET I 547
REMARK 465 MET I 548
REMARK 465 MET J 1
REMARK 465 LYS J 526
REMARK 465 ASN J 527
REMARK 465 ASP J 528
REMARK 465 ALA J 529
REMARK 465 ALA J 530
REMARK 465 ASP J 531
REMARK 465 LEU J 532
REMARK 465 GLY J 533
REMARK 465 ALA J 534
REMARK 465 ALA J 535
REMARK 465 GLY J 536
REMARK 465 GLY J 537
REMARK 465 MET J 538
REMARK 465 GLY J 539
REMARK 465 GLY J 540
REMARK 465 MET J 541
REMARK 465 GLY J 542
REMARK 465 GLY J 543
REMARK 465 MET J 544
REMARK 465 GLY J 545
REMARK 465 GLY J 546
REMARK 465 MET J 547
REMARK 465 MET J 548
REMARK 465 MET K 1
REMARK 465 LYS K 526
REMARK 465 ASN K 527
REMARK 465 ASP K 528
REMARK 465 ALA K 529
REMARK 465 ALA K 530
REMARK 465 ASP K 531
REMARK 465 LEU K 532
REMARK 465 GLY K 533
REMARK 465 ALA K 534
REMARK 465 ALA K 535
REMARK 465 GLY K 536
REMARK 465 GLY K 537
REMARK 465 MET K 538
REMARK 465 GLY K 539
REMARK 465 GLY K 540
REMARK 465 MET K 541
REMARK 465 GLY K 542
REMARK 465 GLY K 543
REMARK 465 MET K 544
REMARK 465 GLY K 545
REMARK 465 GLY K 546
REMARK 465 MET K 547
REMARK 465 MET K 548
REMARK 465 MET L 1
REMARK 465 LYS L 526
REMARK 465 ASN L 527
REMARK 465 ASP L 528
REMARK 465 ALA L 529
REMARK 465 ALA L 530
REMARK 465 ASP L 531
REMARK 465 LEU L 532
REMARK 465 GLY L 533
REMARK 465 ALA L 534
REMARK 465 ALA L 535
REMARK 465 GLY L 536
REMARK 465 GLY L 537
REMARK 465 MET L 538
REMARK 465 GLY L 539
REMARK 465 GLY L 540
REMARK 465 MET L 541
REMARK 465 GLY L 542
REMARK 465 GLY L 543
REMARK 465 MET L 544
REMARK 465 GLY L 545
REMARK 465 GLY L 546
REMARK 465 MET L 547
REMARK 465 MET L 548
REMARK 465 MET M 1
REMARK 465 LYS M 526
REMARK 465 ASN M 527
REMARK 465 ASP M 528
REMARK 465 ALA M 529
REMARK 465 ALA M 530
REMARK 465 ASP M 531
REMARK 465 LEU M 532
REMARK 465 GLY M 533
REMARK 465 ALA M 534
REMARK 465 ALA M 535
REMARK 465 GLY M 536
REMARK 465 GLY M 537
REMARK 465 MET M 538
REMARK 465 GLY M 539
REMARK 465 GLY M 540
REMARK 465 MET M 541
REMARK 465 GLY M 542
REMARK 465 GLY M 543
REMARK 465 MET M 544
REMARK 465 GLY M 545
REMARK 465 GLY M 546
REMARK 465 MET M 547
REMARK 465 MET M 548
REMARK 465 MET N 1
REMARK 465 PRO N 524A
REMARK 465 LYS N 524B
REMARK 465 ASN N 524C
REMARK 465 ASP N 524D
REMARK 465 ALA N 530
REMARK 465 ALA N 524F
REMARK 465 ASP N 524G
REMARK 465 GLY N 533
REMARK 465 ALA N 534
REMARK 465 ALA N 535
REMARK 465 GLY N 536
REMARK 465 GLY N 537
REMARK 465 MET N 538
REMARK 465 GLY N 539
REMARK 465 GLY N 540
REMARK 465 MET N 541
REMARK 465 GLY N 542
REMARK 465 GLY N 543
REMARK 465 MET N 544
REMARK 465 GLY N 545
REMARK 465 GLY N 546
REMARK 465 MET N 547
REMARK 465 MET N 548
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 PRO A 525 CA C O CB CG CD
REMARK 470 ALA B 2 N
REMARK 470 PRO B 525 CA C O CB CG CD
REMARK 470 ALA C 2 N
REMARK 470 PRO C 525 CA C O CB CG CD
REMARK 470 ALA D 2 N
REMARK 470 PRO D 525 CA C O CB CG CD
REMARK 470 ALA E 2 N
REMARK 470 PRO E 525 CA C O CB CG CD
REMARK 470 ALA F 2 N
REMARK 470 PRO F 525 CA C O CB CG CD
REMARK 470 ALA G 2 N
REMARK 470 LEU G 525 CA C O CB CG CD1 CD2
REMARK 470 ALA H 2 N
REMARK 470 PRO H 525 CA C O CB CG CD
REMARK 470 ALA I 2 N
REMARK 470 PRO I 525 CA C O CB CG CD
REMARK 470 ALA J 2 N
REMARK 470 PRO J 525 CA C O CB CG CD
REMARK 470 ALA K 2 N
REMARK 470 PRO K 525 CA C O CB CG CD
REMARK 470 ALA L 2 N
REMARK 470 PRO L 525 CA C O CB CG CD
REMARK 470 ALA M 2 N
REMARK 470 PRO M 525 CA C O CB CG CD
REMARK 470 ALA N 2 N
REMARK 470 LEU N 525 CA C O CB CG CD1 CD2
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 O ASN M 37 N GLU N 518 0.83
REMARK 500 O ASN J 37 N GLU K 518 0.84
REMARK 500 N GLU H 518 O ASN N 37 0.84
REMARK 500 O ASN L 37 N GLU M 518 0.84
REMARK 500 O ASN H 37 N GLU I 518 0.84
REMARK 500 O ASN I 37 N GLU J 518 0.84
REMARK 500 O ASN K 37 N GLU L 518 0.84
REMARK 500 CD1 LEU B 200 CG1 VAL B 254 0.87
REMARK 500 CD1 LEU C 200 CG1 VAL C 254 0.87
REMARK 500 CD1 LEU D 200 CG1 VAL D 254 0.87
REMARK 500 CD1 LEU A 200 CG1 VAL A 254 0.87
REMARK 500 CD1 LEU E 200 CG1 VAL E 254 0.87
REMARK 500 CD1 LEU F 200 CG1 VAL F 254 0.87
REMARK 500 O ASN J 37 CA GLU K 518 1.09
REMARK 500 O ASN K 37 CA GLU L 518 1.09
REMARK 500 O ASN L 37 CA GLU M 518 1.09
REMARK 500 CA GLU H 518 O ASN N 37 1.09
REMARK 500 O ASN H 37 CA GLU I 518 1.09
REMARK 500 O ASN M 37 CA GLU N 518 1.09
REMARK 500 O ASN I 37 CA GLU J 518 1.09
REMARK 500 C ASN L 37 N GLU M 518 1.19
REMARK 500 C ASN H 37 N GLU I 518 1.19
REMARK 500 N GLU H 518 C ASN N 37 1.19
REMARK 500 C ASN I 37 N GLU J 518 1.19
REMARK 500 C ASN M 37 N GLU N 518 1.19
REMARK 500 C ASN J 37 N GLU K 518 1.19
REMARK 500 C ASN K 37 N GLU L 518 1.19
REMARK 500 CG LEU B 200 CG1 VAL B 254 1.64
REMARK 500 CG LEU A 200 CG1 VAL A 254 1.64
REMARK 500 CG LEU D 200 CG1 VAL D 254 1.64
REMARK 500 CG LEU C 200 CG1 VAL C 254 1.64
REMARK 500 CG LEU E 200 CG1 VAL E 254 1.64
REMARK 500 CG LEU F 200 CG1 VAL F 254 1.64
REMARK 500 O ASN I 37 C GLU J 518 1.72
REMARK 500 O ASN K 37 C GLU L 518 1.73
REMARK 500 O ASN H 37 C GLU I 518 1.73
REMARK 500 C GLU H 518 O ASN N 37 1.73
REMARK 500 O ASN L 37 C GLU M 518 1.73
REMARK 500 O ASN J 37 C GLU K 518 1.73
REMARK 500 O ASN M 37 C GLU N 518 1.73
REMARK 500 CD2 LEU A 200 CG2 VAL A 254 1.87
REMARK 500 CD2 LEU C 200 CG2 VAL C 254 1.87
REMARK 500 CD2 LEU D 200 CG2 VAL D 254 1.87
REMARK 500 CD2 LEU F 200 CG2 VAL F 254 1.87
REMARK 500 CD2 LEU B 200 CG2 VAL B 254 1.87
REMARK 500 CD2 LEU E 200 CG2 VAL E 254 1.87
REMARK 500 CA ASN H 37 N GLU I 518 1.89
REMARK 500 CA ASN L 37 N GLU M 518 1.89
REMARK 500 CA ASN M 37 N GLU N 518 1.89
REMARK 500 N GLU H 518 CA ASN N 37 1.89
REMARK 500
REMARK 500 THIS ENTRY HAS 92 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 7 C PHE A 8 N -0.268
REMARK 500 ASP A 11 C ALA A 12 N 0.182
REMARK 500 ASP A 52 C GLY A 53 N -0.139
REMARK 500 ILE A 230 C ARG A 231 N 0.165
REMARK 500 LEU A 513 C MET A 514 N -0.151
REMARK 500 GLU A 518 C CYS A 519 N -0.144
REMARK 500 LYS B 7 C PHE B 8 N -0.268
REMARK 500 ASP B 11 C ALA B 12 N 0.182
REMARK 500 ASP B 52 C GLY B 53 N -0.140
REMARK 500 VAL B 213 C GLU B 214 N -0.258
REMARK 500 ILE B 230 C ARG B 231 N 0.165
REMARK 500 LEU B 513 C MET B 514 N -0.152
REMARK 500 GLU B 518 C CYS B 519 N -0.144
REMARK 500 LYS C 7 C PHE C 8 N -0.268
REMARK 500 ASP C 11 C ALA C 12 N 0.182
REMARK 500 ASP C 52 C GLY C 53 N -0.139
REMARK 500 VAL C 213 C GLU C 214 N -0.259
REMARK 500 ILE C 230 C ARG C 231 N 0.165
REMARK 500 LEU C 513 C MET C 514 N -0.151
REMARK 500 GLU C 518 C CYS C 519 N -0.144
REMARK 500 LYS D 7 C PHE D 8 N -0.268
REMARK 500 ASP D 11 C ALA D 12 N 0.182
REMARK 500 ASP D 52 C GLY D 53 N -0.139
REMARK 500 VAL D 213 C GLU D 214 N -0.258
REMARK 500 ILE D 230 C ARG D 231 N 0.165
REMARK 500 LEU D 513 C MET D 514 N -0.151
REMARK 500 GLU D 518 C CYS D 519 N -0.143
REMARK 500 LYS E 7 C PHE E 8 N -0.268
REMARK 500 ASP E 11 C ALA E 12 N 0.182
REMARK 500 ASP E 52 C GLY E 53 N -0.139
REMARK 500 VAL E 213 C GLU E 214 N -0.258
REMARK 500 ILE E 230 C ARG E 231 N 0.165
REMARK 500 LEU E 513 C MET E 514 N -0.152
REMARK 500 GLU E 518 C CYS E 519 N -0.144
REMARK 500 LYS F 7 C PHE F 8 N -0.268
REMARK 500 ASP F 11 C ALA F 12 N 0.182
REMARK 500 ASP F 52 C GLY F 53 N -0.139
REMARK 500 VAL F 213 C GLU F 214 N -0.258
REMARK 500 ILE F 230 C ARG F 231 N 0.165
REMARK 500 LEU F 513 C MET F 514 N -0.151
REMARK 500 GLU F 518 C CYS F 519 N -0.144
REMARK 500 LYS G 7 C PHE G 8 N -0.268
REMARK 500 ASP G 11 C ALA G 12 N 0.182
REMARK 500 ASP G 52 C GLY G 53 N -0.139
REMARK 500 VAL G 213 C GLU G 214 N -0.258
REMARK 500 ILE G 230 C ARG G 231 N 0.165
REMARK 500 LEU G 513 C MET G 514 N -0.151
REMARK 500 GLU G 518 C CYS G 519 N -0.144
REMARK 500 LYS H 242 CA LYS H 242 CB 0.135
REMARK 500 ALA H 243 CA ALA H 243 CB 0.155
REMARK 500
REMARK 500 THIS ENTRY HAS 70 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 7 CA - C - N ANGL. DEV. = -20.7 DEGREES
REMARK 500 LYS A 7 O - C - N ANGL. DEV. = 16.4 DEGREES
REMARK 500 PHE A 8 C - N - CA ANGL. DEV. = -25.7 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 VAL A 29 CA - C - N ANGL. DEV. = -24.1 DEGREES
REMARK 500 VAL A 29 O - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 THR A 30 C - N - CA ANGL. DEV. = -20.6 DEGREES
REMARK 500 LYS A 34 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 VAL A 39 N - CA - CB ANGL. DEV. = 15.1 DEGREES
REMARK 500 VAL A 39 CA - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 VAL A 39 O - C - N ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP A 41 N - CA - CB ANGL. DEV. = 17.3 DEGREES
REMARK 500 GLY A 53 C - N - CA ANGL. DEV. = -18.9 DEGREES
REMARK 500 VAL A 56 CB - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 GLU A 59 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 ASP A 87 N - CA - CB ANGL. DEV. = 12.2 DEGREES
REMARK 500 ASN A 153 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 GLU A 214 CB - CA - C ANGL. DEV. = -19.7 DEGREES
REMARK 500 LYS A 225 N - CA - CB ANGL. DEV. = 15.4 DEGREES
REMARK 500 ILE A 230 O - C - N ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 LEU A 247 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 ALA A 251 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 GLU A 252 N - CA - CB ANGL. DEV. = 11.7 DEGREES
REMARK 500 ASP A 253 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ALA A 258 N - CA - CB ANGL. DEV. = 10.8 DEGREES
REMARK 500 VAL A 273 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 LEU A 289 CB - CG - CD1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 LYS A 311 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 ALA A 312 CB - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 ASP A 316 N - CA - CB ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLU A 367 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG A 452 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 SER A 463 N - CA - CB ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 501 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 GLU A 518 N - CA - CB ANGL. DEV. = 14.6 DEGREES
REMARK 500 GLU A 518 CA - C - N ANGL. DEV. = 17.8 DEGREES
REMARK 500 GLU A 518 O - C - N ANGL. DEV. = -18.4 DEGREES
REMARK 500 CYS A 519 C - N - CA ANGL. DEV. = 28.3 DEGREES
REMARK 500 LYS B 7 CA - C - N ANGL. DEV. = -20.7 DEGREES
REMARK 500 LYS B 7 O - C - N ANGL. DEV. = 16.4 DEGREES
REMARK 500 PHE B 8 C - N - CA ANGL. DEV. = -25.7 DEGREES
REMARK 500 ARG B 18 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 18 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 VAL B 29 CA - C - N ANGL. DEV. = -24.0 DEGREES
REMARK 500 VAL B 29 O - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 THR B 30 C - N - CA ANGL. DEV. = -20.6 DEGREES
REMARK 500 LYS B 34 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 621 ANGLE DEVIATIONS.
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 ASN A 37 173.75 59.80
REMARK 500 ASN A 153 79.20 55.47
REMARK 500 TYR A 199 144.53 -35.29
REMARK 500 ASN A 206 -140.23 -98.81
REMARK 500 PRO A 208 104.80 -55.89
REMARK 500 THR A 210 5.92 -65.04
REMARK 500 ILE A 250 77.08 -115.23
REMARK 500 VAL A 271 89.02 52.62
REMARK 500 THR A 313 -157.32 -141.29
REMARK 500 ASN A 326 -158.17 -143.19
REMARK 500 THR A 329 -167.03 -172.80
REMARK 500 ASP A 334 168.76 72.79
REMARK 500 ALA A 384 94.44 46.78
REMARK 500 ASN B 37 173.72 59.77
REMARK 500 ASN B 153 79.17 55.50
REMARK 500 ASN B 206 -154.43 -94.62
REMARK 500 ILE B 250 77.05 -115.24
REMARK 500 VAL B 271 89.01 52.62
REMARK 500 THR B 313 -157.27 -141.25
REMARK 500 ASN B 326 -158.19 -143.24
REMARK 500 THR B 329 -167.04 -172.77
REMARK 500 ASP B 334 168.77 72.79
REMARK 500 ALA B 384 94.40 46.77
REMARK 500 ASN C 37 173.72 59.80
REMARK 500 ASN C 153 79.19 55.48
REMARK 500 TYR C 199 144.52 -29.42
REMARK 500 ASN C 206 -152.31 -100.90
REMARK 500 PRO C 208 107.15 -51.91
REMARK 500 THR C 210 5.91 -65.62
REMARK 500 ILE C 250 77.08 -115.24
REMARK 500 VAL C 271 89.01 52.63
REMARK 500 THR C 313 -157.34 -141.30
REMARK 500 ASN C 326 -158.16 -143.19
REMARK 500 THR C 329 -167.05 -172.81
REMARK 500 ASP C 334 168.74 72.82
REMARK 500 ALA C 384 94.41 46.81
REMARK 500 ASN D 37 173.78 59.83
REMARK 500 ASN D 153 79.20 55.44
REMARK 500 GLU D 191 95.00 -67.12
REMARK 500 ASN D 206 -136.19 -91.73
REMARK 500 PRO D 208 96.86 -47.47
REMARK 500 THR D 210 5.96 -65.14
REMARK 500 ILE D 250 77.09 -115.22
REMARK 500 VAL D 271 89.03 52.62
REMARK 500 THR D 313 -157.32 -141.30
REMARK 500 ASN D 326 -158.18 -143.17
REMARK 500 THR D 329 -167.05 -172.83
REMARK 500 ASP D 334 168.77 72.83
REMARK 500 ALA D 384 94.45 46.74
REMARK 500 ASN E 37 173.75 59.75
REMARK 500
REMARK 500 THIS ENTRY HAS 124 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 190 GLU A 191 -149.87
REMARK 500 ASP A 196 ARG A 197 143.67
REMARK 500 ARG A 197 GLY A 198 122.73
REMARK 500 GLU A 255 GLY A 256 122.72
REMARK 500 PHE A 281 GLY A 282 146.20
REMARK 500 THR A 296 GLY A 297 148.83
REMARK 500 ILE A 325 ASN A 326 -145.70
REMARK 500 THR A 329 THR A 330 148.23
REMARK 500 VAL B 190 GLU B 191 -149.82
REMARK 500 ASP B 196 ARG B 197 136.79
REMARK 500 ARG B 197 GLY B 198 121.79
REMARK 500 GLU B 255 GLY B 256 122.72
REMARK 500 PHE B 281 GLY B 282 146.22
REMARK 500 THR B 296 GLY B 297 148.81
REMARK 500 ILE B 325 ASN B 326 -145.67
REMARK 500 THR B 329 THR B 330 148.23
REMARK 500 VAL C 190 GLU C 191 -149.84
REMARK 500 ASP C 196 ARG C 197 149.88
REMARK 500 ARG C 197 GLY C 198 127.55
REMARK 500 GLU C 255 GLY C 256 122.69
REMARK 500 PHE C 281 GLY C 282 146.23
REMARK 500 THR C 296 GLY C 297 148.83
REMARK 500 ILE C 325 ASN C 326 -145.74
REMARK 500 THR C 329 THR C 330 148.24
REMARK 500 ASP D 196 ARG D 197 148.04
REMARK 500 ARG D 197 GLY D 198 125.86
REMARK 500 GLU D 255 GLY D 256 122.71
REMARK 500 PHE D 281 GLY D 282 146.22
REMARK 500 THR D 296 GLY D 297 148.86
REMARK 500 ILE D 325 ASN D 326 -145.72
REMARK 500 THR D 329 THR D 330 148.23
REMARK 500 VAL E 190 GLU E 191 -149.85
REMARK 500 ASP E 196 ARG E 197 149.81
REMARK 500 ARG E 197 GLY E 198 125.96
REMARK 500 GLU E 255 GLY E 256 122.70
REMARK 500 PHE E 281 GLY E 282 146.22
REMARK 500 THR E 296 GLY E 297 148.83
REMARK 500 ILE E 325 ASN E 326 -145.70
REMARK 500 THR E 329 THR E 330 148.23
REMARK 500 VAL F 190 GLU F 191 -149.87
REMARK 500 ASP F 196 ARG F 197 137.75
REMARK 500 ARG F 197 GLY F 198 124.39
REMARK 500 GLU F 255 GLY F 256 122.75
REMARK 500 PHE F 281 GLY F 282 146.18
REMARK 500 THR F 296 GLY F 297 148.82
REMARK 500 ILE F 325 ASN F 326 -145.68
REMARK 500 THR F 329 THR F 330 148.22
REMARK 500 VAL G 190 GLU G 191 -149.85
REMARK 500 ARG G 197 GLY G 198 125.51
REMARK 500 GLU G 255 GLY G 256 122.72
REMARK 500
REMARK 500 THIS ENTRY HAS 65 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 13 0.12 SIDE CHAIN
REMARK 500 ARG A 18 0.13 SIDE CHAIN
REMARK 500 ARG A 231 0.10 SIDE CHAIN
REMARK 500 ARG A 284 0.10 SIDE CHAIN
REMARK 500 ARG A 285 0.27 SIDE CHAIN
REMARK 500 ARG A 368 0.13 SIDE CHAIN
REMARK 500 ARG A 404 0.22 SIDE CHAIN
REMARK 500 ARG B 13 0.12 SIDE CHAIN
REMARK 500 ARG B 18 0.13 SIDE CHAIN
REMARK 500 ARG B 231 0.10 SIDE CHAIN
REMARK 500 ARG B 284 0.10 SIDE CHAIN
REMARK 500 ARG B 285 0.27 SIDE CHAIN
REMARK 500 ARG B 368 0.13 SIDE CHAIN
REMARK 500 ARG B 404 0.22 SIDE CHAIN
REMARK 500 ARG C 13 0.12 SIDE CHAIN
REMARK 500 ARG C 18 0.13 SIDE CHAIN
REMARK 500 ARG C 231 0.10 SIDE CHAIN
REMARK 500 ARG C 284 0.10 SIDE CHAIN
REMARK 500 ARG C 285 0.27 SIDE CHAIN
REMARK 500 ARG C 368 0.13 SIDE CHAIN
REMARK 500 ARG C 404 0.22 SIDE CHAIN
REMARK 500 ARG D 13 0.12 SIDE CHAIN
REMARK 500 ARG D 18 0.13 SIDE CHAIN
REMARK 500 ARG D 231 0.10 SIDE CHAIN
REMARK 500 ARG D 284 0.10 SIDE CHAIN
REMARK 500 ARG D 285 0.27 SIDE CHAIN
REMARK 500 ARG D 368 0.13 SIDE CHAIN
REMARK 500 ARG D 404 0.22 SIDE CHAIN
REMARK 500 ARG E 13 0.12 SIDE CHAIN
REMARK 500 ARG E 18 0.13 SIDE CHAIN
REMARK 500 ARG E 231 0.10 SIDE CHAIN
REMARK 500 ARG E 284 0.10 SIDE CHAIN
REMARK 500 ARG E 285 0.27 SIDE CHAIN
REMARK 500 ARG E 368 0.13 SIDE CHAIN
REMARK 500 ARG E 404 0.22 SIDE CHAIN
REMARK 500 ARG F 13 0.12 SIDE CHAIN
REMARK 500 ARG F 18 0.13 SIDE CHAIN
REMARK 500 ARG F 231 0.10 SIDE CHAIN
REMARK 500 ARG F 284 0.10 SIDE CHAIN
REMARK 500 ARG F 285 0.27 SIDE CHAIN
REMARK 500 ARG F 368 0.13 SIDE CHAIN
REMARK 500 ARG F 404 0.22 SIDE CHAIN
REMARK 500 ARG G 13 0.12 SIDE CHAIN
REMARK 500 ARG G 18 0.13 SIDE CHAIN
REMARK 500 ARG G 231 0.10 SIDE CHAIN
REMARK 500 ARG G 284 0.10 SIDE CHAIN
REMARK 500 ARG G 285 0.27 SIDE CHAIN
REMARK 500 ARG G 368 0.13 SIDE CHAIN
REMARK 500 ARG G 404 0.22 SIDE CHAIN
REMARK 500 ARG H 58 0.21 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 127 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 29 11.96
REMARK 500 ASP A 52 15.95
REMARK 500 MET A 193 12.00
REMARK 500 ARG A 197 -20.54
REMARK 500 VAL B 29 11.95
REMARK 500 ASP B 52 15.95
REMARK 500 ARG B 197 -20.58
REMARK 500 VAL C 29 11.96
REMARK 500 ASP C 52 15.94
REMARK 500 ARG C 197 -21.50
REMARK 500 VAL D 29 11.96
REMARK 500 ASP D 52 15.94
REMARK 500 MET D 193 12.01
REMARK 500 ARG D 197 -20.91
REMARK 500 VAL E 29 11.92
REMARK 500 ASP E 52 15.94
REMARK 500 MET E 193 12.01
REMARK 500 ARG E 197 -20.87
REMARK 500 VAL F 29 11.97
REMARK 500 ASP F 52 15.95
REMARK 500 MET F 193 12.01
REMARK 500 ARG F 197 -20.52
REMARK 500 VAL G 29 11.93
REMARK 500 ASP G 52 15.94
REMARK 500 ARG G 197 -20.59
REMARK 500 TYR G 199 -19.16
REMARK 500 VAL H 213 12.52
REMARK 500 ARG I 197 -11.50
REMARK 500 VAL I 213 12.53
REMARK 500 ARG J 197 -11.13
REMARK 500 VAL J 213 12.43
REMARK 500 ARG K 197 -11.02
REMARK 500 VAL K 213 12.52
REMARK 500 ARG L 197 -11.33
REMARK 500 VAL L 213 12.48
REMARK 500 ARG M 197 -11.71
REMARK 500 VAL M 213 12.50
REMARK 500 ARG N 197 -10.78
REMARK 500 VAL N 213 12.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PO4 A 1525
REMARK 610 PO4 B 1525
REMARK 610 PO4 C 1525
REMARK 610 PO4 D 1525
REMARK 610 PO4 E 1525
REMARK 610 PO4 F 1525
REMARK 610 PO4 G 1525
REMARK 610 PO4 H 1525
REMARK 610 PO4 I 1525
REMARK 610 PO4 J 1525
REMARK 610 PO4 K 1525
REMARK 610 PO4 L 1525
REMARK 610 PO4 M 1525
REMARK 610 PO4 N 1525
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A1527 O1B
REMARK 620 2 ATP A1527 O2A 87.1
REMARK 620 3 ASP A 87 OD1 119.8 150.7
REMARK 620 4 ASP A 87 OD2 87.3 106.2 67.0
REMARK 620 5 ATP A1527 O3G 92.2 95.3 94.9 158.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP B1527 O2A
REMARK 620 2 ASP B 87 OD1 149.3
REMARK 620 3 ASP B 87 OD2 101.6 67.4
REMARK 620 4 ATP B1527 O3G 99.6 94.4 158.8
REMARK 620 5 ATP B1527 O1B 87.1 120.0 89.4 90.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP C1527 O1B
REMARK 620 2 ATP C1527 O2A 87.1
REMARK 620 3 ASP C 87 OD1 119.8 150.7
REMARK 620 4 ASP C 87 OD2 87.3 106.2 67.0
REMARK 620 5 ATP C1527 O3G 92.3 95.3 94.9 158.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 87 OD1
REMARK 620 2 ASP D 87 OD2 67.1
REMARK 620 3 ATP D1527 O3G 92.9 156.9
REMARK 620 4 ATP D1527 O1B 120.1 89.4 91.2
REMARK 620 5 ATP D1527 O2A 150.2 104.7 98.5 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 87 OD2
REMARK 620 2 ASP E 87 OD1 66.9
REMARK 620 3 ATP E1527 O1B 87.3 119.7
REMARK 620 4 ATP E1527 O3G 158.4 94.9 92.3
REMARK 620 5 ATP E1527 O2A 106.2 150.7 87.1 95.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP F1527 O2A
REMARK 620 2 ATP F1527 O3G 98.5
REMARK 620 3 ASP F 87 OD1 150.2 92.9
REMARK 620 4 ATP F1527 O1B 87.3 91.2 120.1
REMARK 620 5 ASP F 87 OD2 104.6 156.9 67.1 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 87 OD2
REMARK 620 2 ATP G1527 O1B 87.4
REMARK 620 3 ASP G 87 OD1 67.0 119.8
REMARK 620 4 ATP G1527 O3G 158.4 92.3 94.9
REMARK 620 5 ATP G1527 O2A 106.3 87.1 150.7 95.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 87 OD1
REMARK 620 2 ATP H1527 O1B 127.8
REMARK 620 3 ATP H1527 O2A 141.8 88.7
REMARK 620 4 ASP H 87 OD2 66.8 89.3 108.1
REMARK 620 5 ATP H1527 O3G 96.6 90.1 94.0 157.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP I1527 O1B
REMARK 620 2 ATP I1527 O3G 90.2
REMARK 620 3 ATP I1527 O2A 88.6 94.0
REMARK 620 4 ASP I 87 OD2 89.3 158.0 108.0
REMARK 620 5 ASP I 87 OD1 127.7 96.7 141.9 66.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP J 87 OD1
REMARK 620 2 ATP J1527 O3G 96.6
REMARK 620 3 ATP J1527 O2A 141.9 94.0
REMARK 620 4 ATP J1527 O1B 127.7 90.1 88.6
REMARK 620 5 ASP J 87 OD2 66.8 157.9 108.1 89.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP K1527 O3G
REMARK 620 2 ATP K1527 O2A 94.0
REMARK 620 3 ASP K 87 OD2 157.9 108.1
REMARK 620 4 ASP K 87 OD1 96.6 141.8 66.8
REMARK 620 5 ATP K1527 O1B 90.1 88.7 89.3 127.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP L1527 O1B
REMARK 620 2 ATP L1527 O2A 88.6
REMARK 620 3 ATP L1527 O3G 90.2 94.0
REMARK 620 4 ASP L 87 OD2 89.3 108.0 157.9
REMARK 620 5 ASP L 87 OD1 127.8 141.8 96.6 66.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG M1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP M1527 O3G
REMARK 620 2 ATP M1527 O2A 94.0
REMARK 620 3 ATP M1527 O1B 90.1 88.6
REMARK 620 4 ASP M 87 OD2 157.9 108.0 89.3
REMARK 620 5 ASP M 87 OD1 96.6 141.9 127.8 66.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N1526 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP N1527 O3G
REMARK 620 2 ATP N1527 O2A 94.0
REMARK 620 3 ATP N1527 O1B 90.1 88.7
REMARK 620 4 ASP N 87 OD2 158.0 108.0 89.3
REMARK 620 5 ASP N 87 OD1 96.6 141.8 127.7 66.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP F 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP G 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP H 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 I 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP I 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 J 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP J 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 K 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP K 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 L 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP L 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 M 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG M 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP M 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 N 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP N 1527
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-2003 RELATED DB: EMDB
REMARK 900 ATP-TRIGGERED MOLECULAR MECHANICS OF THE CHAPERONIN GROEL
REMARK 900 RELATED ID: 1AON RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/
REMARK 900 (ADP)7
REMARK 900 RELATED ID: 1DK7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL
REMARK 900 RELATED ID: 1DKD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC
REMARK 900 PEPTIDE COMPLEX
REMARK 900 RELATED ID: 1FY9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THEMOLECULAR
REMARK 900 CHAPERONIN GROEL APICAL DOMAIN
REMARK 900 RELATED ID: 1FYA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THEMOLECULAR
REMARK 900 CHAPERONIN GROEL APICAL DOMAIN
REMARK 900 RELATED ID: 1GR5 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON MICROSCOPY
REMARK 900 RELATED ID: 1GRL RELATED DB: PDB
REMARK 900 RELATED ID: 1GRU RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM
REMARK 900 RELATED ID: 1J4Z RELATED DB: PDB
REMARK 900 STRUCTURAL AND MECHANISTIC BASIS FOR ALLOSTERY IN THEBACTERIAL
REMARK 900 CHAPERONIN GROEL; SEE REMARK 400
REMARK 900 RELATED ID: 1JON RELATED DB: PDB
REMARK 900 GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191 - 345
REMARK 900 RELATED ID: 1KID RELATED DB: PDB
REMARK 900 GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES
REMARK 900 191-376, MUTANT WITH ALA 262 REPLACED WITH LEU AND ILE 267 REPLACED
REMARK 900 WITH MET
REMARK 900 RELATED ID: 1KP8 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR GROEL-ASSISTED PROTEIN FOLDING FROMTHE CRYSTAL
REMARK 900 STRUCTURE OF (GROEL-KMGATP)14 AT 2.0 ARESOLUTION
REMARK 900 RELATED ID: 1KPO RELATED DB: PDB
REMARK 900 STRUCTURAL AND MECHANISTIC BASIS FOR ALLOSTERY IN THEBACTERIAL
REMARK 900 CHAPERONIN GROEL; SEE REMARK 400
REMARK 900 RELATED ID: 1LA1 RELATED DB: PDB
REMARK 900 GRO-EL FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 188 -379
REMARK 900 RELATED ID: 1MNF RELATED DB: PDB
REMARK 900 DOMAIN MOTIONS IN GROEL UPON BINDING OF AN OLIGOPEPTIDE
REMARK 900 RELATED ID: 1OEL RELATED DB: PDB
REMARK 900 RELATED ID: 1PCQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GROEL-GROES
REMARK 900 RELATED ID: 1PF9 RELATED DB: PDB
REMARK 900 GROEL-GROES-ADP
REMARK 900 RELATED ID: 1SS8 RELATED DB: PDB
REMARK 900 GROEL
REMARK 900 RELATED ID: 1SVT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GROEL14-GROES7-(ADP-ALFX)7
REMARK 900 RELATED ID: 1SX3 RELATED DB: PDB
REMARK 900 GROEL14-(ATPGAMMAS)14
REMARK 900 RELATED ID: 1SX4 RELATED DB: PDB
REMARK 900 GROEL-GROES-ADP7
REMARK 900 RELATED ID: 1XCK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO GROEL
REMARK 900 RELATED ID: 2C7C RELATED DB: PDB
REMARK 900 FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)
REMARK 900 RELATED ID: 2C7D RELATED DB: PDB
REMARK 900 FITTED COORDINATES FOR GROEL-ADP7-GROES CRYO-EM COMPLEX (EMD-1181)
REMARK 900 RELATED ID: 2C7E RELATED DB: PDB
REMARK 900 REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)- ATP7 CRYO-EM
REMARK 900 MAP (EMD 1047)
REMARK 900 RELATED ID: 2CGT RELATED DB: PDB
REMARK 900 GROEL-ADP-GP31 COMPLEX
REMARK 900 RELATED ID: 2YEY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ALLOSTERIC-DEFECTIVE CHAPERONIN GROEL
REMARK 900 E434K MUTANT
REMARK 900 RELATED ID: 4AAQ RELATED DB: PDB
REMARK 900 ATP-TRIGGERED MOLECULAR MECHANICS OF THE CHAPERONIN GROEL
REMARK 900 RELATED ID: 4AAR RELATED DB: PDB
REMARK 900 ATP-TRIGGERED MOLECULAR MECHANICS OF THE CHAPERONIN GROEL
REMARK 900 RELATED ID: 4AAS RELATED DB: PDB
REMARK 900 ATP-TRIGGERED MOLECULAR MECHANICS OF THE CHAPERONIN GROEL
REMARK 900 RELATED ID: 4AAU RELATED DB: PDB
REMARK 900 ATP-TRIGGERED MOLECULAR MECHANICS OF THE CHAPERONIN GROEL
REMARK 900 RELATED ID: 4AB2 RELATED DB: PDB
REMARK 900 ATP-TRIGGERED MOLECULAR MECHANICS OF THE CHAPERONIN GROEL
DBREF 4AB3 A 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 B 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 C 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 D 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 E 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 F 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 G 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 H 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 I 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 J 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 K 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 L 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 M 1 548 UNP P0A6F5 CH60_ECOLI 1 548
DBREF 4AB3 N 1 548 UNP P0A6F5 CH60_ECOLI 1 548
SEQADV 4AB3 ALA A 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA B 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA C 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA D 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA E 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA F 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA G 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA H 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA I 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA J 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA K 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA L 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA M 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQADV 4AB3 ALA N 398 UNP P0A6F5 ASP 398 ENGINEERED MUTATION
SEQRES 1 A 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 A 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 A 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 A 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 A 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 A 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 A 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 A 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 A 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 A 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 A 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 A 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 A 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 A 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 A 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 A 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 A 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 A 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 A 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 A 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 A 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 A 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 A 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 A 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 A 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 A 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 A 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 A 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 A 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 A 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 A 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 A 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 A 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 A 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 A 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 A 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 A 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 A 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 A 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 A 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 A 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 A 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 A 548 MET MET
SEQRES 1 B 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 B 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 B 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 B 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 B 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 B 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 B 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 B 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 B 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 B 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 B 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 B 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 B 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 B 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 B 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 B 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 B 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 B 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 B 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 B 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 B 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 B 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 B 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 B 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 B 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 B 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 B 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 B 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 B 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 B 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 B 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 B 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 B 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 B 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 B 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 B 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 B 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 B 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 B 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 B 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 B 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 B 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 B 548 MET MET
SEQRES 1 C 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 C 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 C 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 C 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 C 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 C 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 C 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 C 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 C 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 C 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 C 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 C 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 C 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 C 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 C 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 C 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 C 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 C 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 C 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 C 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 C 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 C 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 C 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 C 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 C 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 C 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 C 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 C 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 C 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 C 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 C 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 C 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 C 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 C 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 C 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 C 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 C 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 C 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 C 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 C 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 C 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 C 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 C 548 MET MET
SEQRES 1 D 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 D 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 D 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 D 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 D 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 D 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 D 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 D 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 D 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 D 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 D 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 D 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 D 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 D 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 D 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 D 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 D 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 D 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 D 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 D 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 D 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 D 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 D 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 D 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 D 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 D 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 D 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 D 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 D 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 D 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 D 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 D 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 D 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 D 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 D 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 D 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 D 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 D 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 D 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 D 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 D 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 D 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 D 548 MET MET
SEQRES 1 E 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 E 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 E 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 E 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 E 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 E 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 E 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 E 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 E 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 E 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 E 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 E 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 E 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 E 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 E 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 E 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 E 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 E 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 E 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 E 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 E 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 E 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 E 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 E 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 E 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 E 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 E 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 E 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 E 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 E 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 E 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 E 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 E 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 E 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 E 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 E 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 E 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 E 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 E 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 E 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 E 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 E 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 E 548 MET MET
SEQRES 1 F 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 F 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 F 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 F 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 F 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 F 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 F 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 F 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 F 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 F 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 F 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 F 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 F 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 F 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 F 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 F 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 F 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 F 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 F 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 F 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 F 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 F 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 F 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 F 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 F 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 F 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 F 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 F 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 F 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 F 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 F 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 F 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 F 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 F 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 F 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 F 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 F 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 F 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 F 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 F 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 F 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 F 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 F 548 MET MET
SEQRES 1 G 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 G 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 G 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 G 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 G 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 G 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 G 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 G 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 G 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 G 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 G 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 G 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 G 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 G 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 G 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 G 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 G 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 G 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 G 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 G 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 G 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 G 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 G 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 G 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 G 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 G 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 G 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 G 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 G 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 G 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 G 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 G 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 G 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 G 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 G 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 G 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 G 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 G 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 G 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 G 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 G 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 G 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 G 548 MET MET
SEQRES 1 H 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 H 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 H 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 H 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 H 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 H 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 H 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 H 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 H 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 H 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 H 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 H 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 H 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 H 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 H 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 H 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 H 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 H 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 H 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 H 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 H 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 H 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 H 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 H 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 H 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 H 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 H 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 H 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 H 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 H 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 H 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 H 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 H 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 H 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 H 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 H 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 H 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 H 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 H 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 H 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 H 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 H 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 H 548 MET MET
SEQRES 1 I 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 I 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 I 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 I 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 I 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 I 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 I 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 I 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 I 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 I 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 I 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 I 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 I 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 I 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 I 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 I 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 I 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 I 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 I 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 I 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 I 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 I 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 I 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 I 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 I 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 I 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 I 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 I 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 I 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 I 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 I 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 I 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 I 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 I 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 I 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 I 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 I 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 I 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 I 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 I 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 I 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 I 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 I 548 MET MET
SEQRES 1 J 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 J 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 J 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 J 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 J 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 J 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 J 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 J 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 J 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 J 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 J 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 J 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 J 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 J 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 J 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 J 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 J 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 J 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 J 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 J 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 J 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 J 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 J 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 J 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 J 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 J 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 J 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 J 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 J 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 J 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 J 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 J 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 J 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 J 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 J 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 J 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 J 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 J 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 J 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 J 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 J 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 J 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 J 548 MET MET
SEQRES 1 K 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 K 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 K 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 K 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 K 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 K 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 K 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 K 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 K 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 K 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 K 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 K 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 K 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 K 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 K 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 K 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 K 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 K 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 K 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 K 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 K 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 K 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 K 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 K 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 K 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 K 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 K 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 K 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 K 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 K 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 K 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 K 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 K 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 K 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 K 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 K 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 K 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 K 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 K 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 K 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 K 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 K 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 K 548 MET MET
SEQRES 1 L 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 L 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 L 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 L 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 L 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 L 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 L 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 L 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 L 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 L 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 L 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 L 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 L 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 L 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 L 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 L 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 L 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 L 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 L 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 L 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 L 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 L 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 L 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 L 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 L 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 L 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 L 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 L 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 L 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 L 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 L 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 L 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 L 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 L 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 L 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 L 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 L 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 L 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 L 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 L 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 L 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 L 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 L 548 MET MET
SEQRES 1 M 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 M 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 M 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 M 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 M 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 M 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 M 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 M 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 M 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 M 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 M 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 M 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 M 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 M 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 M 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 M 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 M 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 M 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 M 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 M 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 M 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 M 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 M 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 M 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 M 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 M 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 M 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 M 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 M 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 M 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 M 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 M 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 M 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 M 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 M 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 M 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 M 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 M 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 M 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 M 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 M 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 M 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 M 548 MET MET
SEQRES 1 N 548 MET ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG
SEQRES 2 N 548 VAL LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA
SEQRES 3 N 548 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL
SEQRES 4 N 548 LEU ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP
SEQRES 5 N 548 GLY VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS
SEQRES 6 N 548 PHE GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA
SEQRES 7 N 548 SER LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR
SEQRES 8 N 548 ALA THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU
SEQRES 9 N 548 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS
SEQRES 10 N 548 ARG GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU
SEQRES 11 N 548 LEU LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA
SEQRES 12 N 548 ILE ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU
SEQRES 13 N 548 THR VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL
SEQRES 14 N 548 GLY LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY
SEQRES 15 N 548 LEU GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE
SEQRES 16 N 548 ASP ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO
SEQRES 17 N 548 GLU THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU
SEQRES 18 N 548 LEU ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU
SEQRES 19 N 548 PRO VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU
SEQRES 20 N 548 LEU ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA
SEQRES 21 N 548 THR LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL
SEQRES 22 N 548 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS
SEQRES 23 N 548 ALA MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR
SEQRES 24 N 548 VAL ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA
SEQRES 25 N 548 THR LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE
SEQRES 26 N 548 ASN LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU
SEQRES 27 N 548 GLU ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN
SEQRES 28 N 548 GLN ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS
SEQRES 29 N 548 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA
SEQRES 30 N 548 VAL ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS
SEQRES 31 N 548 GLU LYS LYS ALA ARG VAL GLU ALA ALA LEU HIS ALA THR
SEQRES 32 N 548 ARG ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY
SEQRES 33 N 548 VAL ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU
SEQRES 34 N 548 ARG GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL
SEQRES 35 N 548 ALA LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL
SEQRES 36 N 548 LEU ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR
SEQRES 37 N 548 VAL LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA
SEQRES 38 N 548 THR GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU
SEQRES 39 N 548 ASP PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA
SEQRES 40 N 548 ALA SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET
SEQRES 41 N 548 VAL THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY
SEQRES 42 N 548 ALA ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY
SEQRES 43 N 548 MET MET
HET PO4 A1525 1
HET MG A1526 1
HET ATP A1527 31
HET PO4 B1525 1
HET MG B1526 1
HET ATP B1527 31
HET PO4 C1525 1
HET MG C1526 1
HET ATP C1527 31
HET PO4 D1525 1
HET MG D1526 1
HET ATP D1527 31
HET PO4 E1525 1
HET MG E1526 1
HET ATP E1527 31
HET PO4 F1525 1
HET MG F1526 1
HET ATP F1527 31
HET PO4 G1525 1
HET MG G1526 1
HET ATP G1527 31
HET PO4 H1525 1
HET MG H1526 1
HET ATP H1527 31
HET PO4 I1525 1
HET MG I1526 1
HET ATP I1527 31
HET PO4 J1525 1
HET MG J1526 1
HET ATP J1527 31
HET PO4 K1525 1
HET MG K1526 1
HET ATP K1527 31
HET PO4 L1525 1
HET MG L1526 1
HET ATP L1527 31
HET PO4 M1525 1
HET MG M1526 1
HET ATP M1527 31
HET PO4 N1525 1
HET MG N1526 1
HET ATP N1527 31
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 15 PO4 14(O4 P 3-)
FORMUL 16 MG 14(MG 2+)
FORMUL 17 ATP 14(C10 H16 N5 O13 P3)
HELIX 1 1 GLY A 9 VAL A 29 1 21
HELIX 2 2 ASP A 52 ILE A 60 1 9
HELIX 3 3 ASP A 64 GLY A 86 1 23
HELIX 4 4 GLY A 88 ALA A 109 1 22
HELIX 5 5 ASN A 112 SER A 135 1 24
HELIX 6 6 ASP A 140 ALA A 152 1 13
HELIX 7 7 ASP A 155 GLY A 170 1 16
HELIX 8 8 SER A 201 ILE A 205 5 5
HELIX 9 9 ASN A 229 LYS A 242 1 14
HELIX 10 10 GLY A 256 THR A 266 1 11
HELIX 11 11 PHE A 281 GLY A 297 1 17
HELIX 12 12 GLU A 338 ALA A 356 1 19
HELIX 13 13 SER A 358 GLY A 375 1 18
HELIX 14 14 THR A 385 GLY A 410 1 26
HELIX 15 15 GLY A 416 LEU A 426 1 11
HELIX 16 16 ASN A 433 MET A 447 1 15
HELIX 17 17 GLU A 448 CYS A 458 1 11
HELIX 18 18 GLU A 461 GLY A 472 1 12
HELIX 19 19 THR A 497 THR A 516 1 20
HELIX 20 20 GLY B 9 VAL B 29 1 21
HELIX 21 21 ASP B 52 ILE B 60 1 9
HELIX 22 22 ASP B 64 GLY B 86 1 23
HELIX 23 23 GLY B 88 ALA B 109 1 22
HELIX 24 24 ASN B 112 SER B 135 1 24
HELIX 25 25 ASP B 140 ALA B 152 1 13
HELIX 26 26 ASP B 155 GLY B 170 1 16
HELIX 27 27 SER B 201 ILE B 205 5 5
HELIX 28 28 ASN B 229 LYS B 242 1 14
HELIX 29 29 GLY B 256 THR B 266 1 11
HELIX 30 30 PHE B 281 GLY B 297 1 17
HELIX 31 31 GLU B 338 ALA B 356 1 19
HELIX 32 32 SER B 358 GLY B 375 1 18
HELIX 33 33 THR B 385 GLY B 410 1 26
HELIX 34 34 GLY B 416 LEU B 426 1 11
HELIX 35 35 ASN B 433 MET B 447 1 15
HELIX 36 36 GLU B 448 CYS B 458 1 11
HELIX 37 37 GLU B 461 GLY B 472 1 12
HELIX 38 38 THR B 497 THR B 516 1 20
HELIX 39 39 GLY C 9 VAL C 29 1 21
HELIX 40 40 ASP C 52 ILE C 60 1 9
HELIX 41 41 ASP C 64 GLY C 86 1 23
HELIX 42 42 GLY C 88 ALA C 109 1 22
HELIX 43 43 ASN C 112 SER C 135 1 24
HELIX 44 44 ASP C 140 ALA C 152 1 13
HELIX 45 45 ASP C 155 GLY C 170 1 16
HELIX 46 46 SER C 201 ILE C 205 5 5
HELIX 47 47 ASN C 229 LYS C 242 1 14
HELIX 48 48 GLY C 256 THR C 266 1 11
HELIX 49 49 PHE C 281 GLY C 297 1 17
HELIX 50 50 GLU C 338 ALA C 356 1 19
HELIX 51 51 SER C 358 GLY C 375 1 18
HELIX 52 52 THR C 385 GLY C 410 1 26
HELIX 53 53 GLY C 416 LEU C 426 1 11
HELIX 54 54 ASN C 433 MET C 447 1 15
HELIX 55 55 GLU C 448 CYS C 458 1 11
HELIX 56 56 GLU C 461 GLY C 472 1 12
HELIX 57 57 THR C 497 THR C 516 1 20
HELIX 58 58 GLY D 9 VAL D 29 1 21
HELIX 59 59 ASP D 52 ILE D 60 1 9
HELIX 60 60 ASP D 64 GLY D 86 1 23
HELIX 61 61 GLY D 88 ALA D 109 1 22
HELIX 62 62 ASN D 112 SER D 135 1 24
HELIX 63 63 ASP D 140 ALA D 152 1 13
HELIX 64 64 ASP D 155 GLY D 170 1 16
HELIX 65 65 SER D 201 ILE D 205 5 5
HELIX 66 66 ASN D 229 LYS D 242 1 14
HELIX 67 67 GLY D 256 THR D 266 1 11
HELIX 68 68 PHE D 281 GLY D 297 1 17
HELIX 69 69 GLU D 338 ALA D 356 1 19
HELIX 70 70 SER D 358 GLY D 375 1 18
HELIX 71 71 THR D 385 GLY D 410 1 26
HELIX 72 72 GLY D 416 LEU D 426 1 11
HELIX 73 73 ASN D 433 MET D 447 1 15
HELIX 74 74 GLU D 448 CYS D 458 1 11
HELIX 75 75 GLU D 461 GLY D 472 1 12
HELIX 76 76 THR D 497 THR D 516 1 20
HELIX 77 77 GLY E 9 VAL E 29 1 21
HELIX 78 78 ASP E 52 ILE E 60 1 9
HELIX 79 79 ASP E 64 GLY E 86 1 23
HELIX 80 80 GLY E 88 ALA E 109 1 22
HELIX 81 81 ASN E 112 SER E 135 1 24
HELIX 82 82 ASP E 140 ALA E 152 1 13
HELIX 83 83 ASP E 155 GLY E 170 1 16
HELIX 84 84 SER E 201 ILE E 205 5 5
HELIX 85 85 ASN E 229 LYS E 242 1 14
HELIX 86 86 GLY E 256 THR E 266 1 11
HELIX 87 87 PHE E 281 GLY E 297 1 17
HELIX 88 88 GLU E 338 ALA E 356 1 19
HELIX 89 89 SER E 358 GLY E 375 1 18
HELIX 90 90 THR E 385 GLY E 410 1 26
HELIX 91 91 GLY E 416 LEU E 426 1 11
HELIX 92 92 ASN E 433 MET E 447 1 15
HELIX 93 93 GLU E 448 CYS E 458 1 11
HELIX 94 94 GLU E 461 GLY E 472 1 12
HELIX 95 95 THR E 497 THR E 516 1 20
HELIX 96 96 GLY F 9 VAL F 29 1 21
HELIX 97 97 ASP F 52 ILE F 60 1 9
HELIX 98 98 ASP F 64 GLY F 86 1 23
HELIX 99 99 GLY F 88 ALA F 109 1 22
HELIX 100 100 ASN F 112 SER F 135 1 24
HELIX 101 101 ASP F 140 ALA F 152 1 13
HELIX 102 102 ASP F 155 GLY F 170 1 16
HELIX 103 103 SER F 201 ILE F 205 5 5
HELIX 104 104 ASN F 229 LYS F 242 1 14
HELIX 105 105 GLY F 256 THR F 266 1 11
HELIX 106 106 PHE F 281 GLY F 297 1 17
HELIX 107 107 GLU F 338 ALA F 356 1 19
HELIX 108 108 SER F 358 GLY F 375 1 18
HELIX 109 109 THR F 385 GLY F 410 1 26
HELIX 110 110 GLY F 416 LEU F 426 1 11
HELIX 111 111 ASN F 433 MET F 447 1 15
HELIX 112 112 GLU F 448 CYS F 458 1 11
HELIX 113 113 GLU F 461 GLY F 472 1 12
HELIX 114 114 THR F 497 THR F 516 1 20
HELIX 115 115 GLY G 9 VAL G 29 1 21
HELIX 116 116 ASP G 52 ILE G 60 1 9
HELIX 117 117 ASP G 64 GLY G 86 1 23
HELIX 118 118 GLY G 88 ALA G 109 1 22
HELIX 119 119 ASN G 112 SER G 135 1 24
HELIX 120 120 ASP G 140 ALA G 152 1 13
HELIX 121 121 ASP G 155 GLY G 170 1 16
HELIX 122 122 SER G 201 ILE G 205 5 5
HELIX 123 123 ASN G 229 LYS G 242 1 14
HELIX 124 124 GLY G 256 THR G 266 1 11
HELIX 125 125 PHE G 281 GLY G 297 1 17
HELIX 126 126 GLU G 338 ALA G 356 1 19
HELIX 127 127 SER G 358 GLY G 375 1 18
HELIX 128 128 THR G 385 GLY G 410 1 26
HELIX 129 129 GLY G 416 LEU G 426 1 11
HELIX 130 130 ASN G 433 MET G 447 1 15
HELIX 131 131 GLU G 448 CYS G 458 1 11
HELIX 132 132 GLU G 461 GLY G 472 1 12
HELIX 133 133 THR G 497 THR G 516 1 20
HELIX 134 134 GLY H 9 LEU H 31 1 23
HELIX 135 135 ASP H 52 ILE H 60 1 9
HELIX 136 136 ASP H 64 GLY H 86 1 23
HELIX 137 137 GLY H 88 GLY H 110 1 23
HELIX 138 138 ASN H 112 SER H 135 1 24
HELIX 139 139 ASP H 140 ASN H 153 1 14
HELIX 140 140 ASP H 155 GLY H 170 1 16
HELIX 141 141 SER H 201 ILE H 205 5 5
HELIX 142 142 ASN H 229 LYS H 242 1 14
HELIX 143 143 GLU H 255 GLY H 269 1 15
HELIX 144 144 PHE H 281 GLY H 297 1 17
HELIX 145 145 GLU H 338 ALA H 356 1 19
HELIX 146 146 SER H 358 GLY H 375 1 18
HELIX 147 147 THR H 385 GLY H 410 1 26
HELIX 148 148 GLY H 416 LEU H 429 1 14
HELIX 149 149 ASN H 433 GLY H 459 1 27
HELIX 150 150 GLU H 461 GLY H 472 1 12
HELIX 151 151 ASN H 487 GLY H 492 1 6
HELIX 152 152 THR H 497 THR H 516 1 20
HELIX 153 153 GLY I 9 LEU I 31 1 23
HELIX 154 154 ASP I 52 ILE I 60 1 9
HELIX 155 155 ASP I 64 GLY I 86 1 23
HELIX 156 156 GLY I 88 GLY I 110 1 23
HELIX 157 157 ASN I 112 SER I 135 1 24
HELIX 158 158 ASP I 140 ASN I 153 1 14
HELIX 159 159 ASP I 155 GLY I 170 1 16
HELIX 160 160 SER I 201 ILE I 205 5 5
HELIX 161 161 ASN I 229 LYS I 242 1 14
HELIX 162 162 GLU I 255 GLY I 269 1 15
HELIX 163 163 PHE I 281 GLY I 297 1 17
HELIX 164 164 GLU I 338 ALA I 356 1 19
HELIX 165 165 SER I 358 GLY I 375 1 18
HELIX 166 166 THR I 385 GLY I 410 1 26
HELIX 167 167 GLY I 416 LEU I 429 1 14
HELIX 168 168 ASN I 433 GLY I 459 1 27
HELIX 169 169 GLU I 461 GLY I 472 1 12
HELIX 170 170 ASN I 487 GLY I 492 1 6
HELIX 171 171 THR I 497 THR I 516 1 20
HELIX 172 172 GLY J 9 LEU J 31 1 23
HELIX 173 173 ASP J 52 ILE J 60 1 9
HELIX 174 174 ASP J 64 GLY J 86 1 23
HELIX 175 175 GLY J 88 GLY J 110 1 23
HELIX 176 176 ASN J 112 SER J 135 1 24
HELIX 177 177 ASP J 140 ASN J 153 1 14
HELIX 178 178 ASP J 155 GLY J 170 1 16
HELIX 179 179 SER J 201 ILE J 205 5 5
HELIX 180 180 ASN J 229 LYS J 242 1 14
HELIX 181 181 GLU J 255 GLY J 269 1 15
HELIX 182 182 PHE J 281 GLY J 297 1 17
HELIX 183 183 GLU J 338 ALA J 356 1 19
HELIX 184 184 SER J 358 GLY J 375 1 18
HELIX 185 185 THR J 385 GLY J 410 1 26
HELIX 186 186 GLY J 416 LEU J 429 1 14
HELIX 187 187 ASN J 433 GLY J 459 1 27
HELIX 188 188 GLU J 461 GLY J 472 1 12
HELIX 189 189 ASN J 487 GLY J 492 1 6
HELIX 190 190 THR J 497 THR J 516 1 20
HELIX 191 191 GLY K 9 LEU K 31 1 23
HELIX 192 192 ASP K 52 ILE K 60 1 9
HELIX 193 193 ASP K 64 GLY K 86 1 23
HELIX 194 194 GLY K 88 GLY K 110 1 23
HELIX 195 195 ASN K 112 SER K 135 1 24
HELIX 196 196 ASP K 140 ASN K 153 1 14
HELIX 197 197 ASP K 155 GLY K 170 1 16
HELIX 198 198 SER K 201 ILE K 205 5 5
HELIX 199 199 ASN K 229 LYS K 242 1 14
HELIX 200 200 GLU K 255 GLY K 269 1 15
HELIX 201 201 PHE K 281 GLY K 297 1 17
HELIX 202 202 GLU K 338 ALA K 356 1 19
HELIX 203 203 SER K 358 GLY K 375 1 18
HELIX 204 204 THR K 385 GLY K 410 1 26
HELIX 205 205 GLY K 416 LEU K 429 1 14
HELIX 206 206 ASN K 433 GLY K 459 1 27
HELIX 207 207 GLU K 461 GLY K 472 1 12
HELIX 208 208 ASN K 487 GLY K 492 1 6
HELIX 209 209 THR K 497 THR K 516 1 20
HELIX 210 210 GLY L 9 LEU L 31 1 23
HELIX 211 211 ASP L 52 ILE L 60 1 9
HELIX 212 212 ASP L 64 GLY L 86 1 23
HELIX 213 213 GLY L 88 GLY L 110 1 23
HELIX 214 214 ASN L 112 SER L 135 1 24
HELIX 215 215 ASP L 140 ASN L 153 1 14
HELIX 216 216 ASP L 155 GLY L 170 1 16
HELIX 217 217 SER L 201 ILE L 205 5 5
HELIX 218 218 ASN L 229 LYS L 242 1 14
HELIX 219 219 GLU L 255 GLY L 269 1 15
HELIX 220 220 PHE L 281 GLY L 297 1 17
HELIX 221 221 GLU L 338 ALA L 356 1 19
HELIX 222 222 SER L 358 GLY L 375 1 18
HELIX 223 223 THR L 385 GLY L 410 1 26
HELIX 224 224 GLY L 416 LEU L 429 1 14
HELIX 225 225 ASN L 433 GLY L 459 1 27
HELIX 226 226 GLU L 461 GLY L 472 1 12
HELIX 227 227 ASN L 487 GLY L 492 1 6
HELIX 228 228 THR L 497 THR L 516 1 20
HELIX 229 229 GLY M 9 LEU M 31 1 23
HELIX 230 230 ASP M 52 ILE M 60 1 9
HELIX 231 231 ASP M 64 GLY M 86 1 23
HELIX 232 232 GLY M 88 GLY M 110 1 23
HELIX 233 233 ASN M 112 SER M 135 1 24
HELIX 234 234 ASP M 140 ASN M 153 1 14
HELIX 235 235 ASP M 155 GLY M 170 1 16
HELIX 236 236 SER M 201 ILE M 205 5 5
HELIX 237 237 ASN M 229 LYS M 242 1 14
HELIX 238 238 GLU M 255 GLY M 269 1 15
HELIX 239 239 PHE M 281 GLY M 297 1 17
HELIX 240 240 GLU M 338 ALA M 356 1 19
HELIX 241 241 SER M 358 GLY M 375 1 18
HELIX 242 242 THR M 385 GLY M 410 1 26
HELIX 243 243 GLY M 416 LEU M 429 1 14
HELIX 244 244 ASN M 433 GLY M 459 1 27
HELIX 245 245 GLU M 461 GLY M 472 1 12
HELIX 246 246 ASN M 487 GLY M 492 1 6
HELIX 247 247 THR M 497 THR M 516 1 20
HELIX 248 248 GLY N 9 LEU N 31 1 23
HELIX 249 249 ASP N 52 ILE N 60 1 9
HELIX 250 250 ASP N 64 GLY N 86 1 23
HELIX 251 251 GLY N 88 GLY N 110 1 23
HELIX 252 252 ASN N 112 SER N 135 1 24
HELIX 253 253 ASP N 140 ASN N 153 1 14
HELIX 254 254 ASP N 155 GLY N 170 1 16
HELIX 255 255 SER N 201 ILE N 205 5 5
HELIX 256 256 ASN N 229 LYS N 242 1 14
HELIX 257 257 GLU N 255 GLY N 269 1 15
HELIX 258 258 PHE N 281 GLY N 297 1 17
HELIX 259 259 GLU N 338 ALA N 356 1 19
HELIX 260 260 SER N 358 GLY N 375 1 18
HELIX 261 261 THR N 385 GLY N 410 1 26
HELIX 262 262 GLY N 416 LEU N 429 1 14
HELIX 263 263 ASN N 433 GLY N 459 1 27
HELIX 264 264 GLU N 461 GLY N 472 1 12
HELIX 265 265 ASN N 487 GLY N 492 1 6
HELIX 266 266 THR N 497 THR N 516 1 20
SHEET 1 AA 2 LYS A 4 PHE A 8 0
SHEET 2 AA 2 CYS A 519 ASP A 523 -1 O MET A 520 N LYS A 7
SHEET 1 AB 2 VAL A 38 LEU A 40 0
SHEET 2 AB 2 THR A 48 THR A 50 -1 O THR A 48 N LEU A 40
SHEET 1 AC 3 ILE A 175 ASP A 179 0
SHEET 2 AC 3 VAL A 376 VAL A 381 1 O ALA A 377 N THR A 176
SHEET 3 AC 3 GLU A 186 VAL A 190 -1 O GLU A 186 N LYS A 380
SHEET 1 AD 4 MET A 193 PHE A 195 0
SHEET 2 AD 4 THR A 330 ILE A 333 -1 O THR A 330 N PHE A 195
SHEET 3 AD 4 ARG A 322 ILE A 325 -1 O ARG A 322 N ILE A 333
SHEET 4 AD 4 VAL A 213 GLU A 216 -1 O VAL A 213 N ILE A 325
SHEET 1 AE 4 VAL A 273 LYS A 277 0
SHEET 2 AE 4 LEU A 247 ALA A 251 1 O LEU A 247 N ALA A 274
SHEET 3 AE 4 PHE A 219 LEU A 221 1 O PHE A 219 N LEU A 248
SHEET 4 AE 4 GLY A 318 GLN A 319 -1 O GLY A 318 N ILE A 220
SHEET 1 AF 2 VAL A 411 ALA A 413 0
SHEET 2 AF 2 LEU A 494 PRO A 496 -1 O ASP A 495 N VAL A 412
SHEET 1 AG 2 TYR A 476 ASN A 479 0
SHEET 2 AG 2 GLU A 484 ASN A 487 -1 O GLU A 484 N ASN A 479
SHEET 1 BA 2 LYS B 4 PHE B 8 0
SHEET 2 BA 2 CYS B 519 ASP B 523 -1 O MET B 520 N LYS B 7
SHEET 1 BB 2 VAL B 38 LEU B 40 0
SHEET 2 BB 2 THR B 48 THR B 50 -1 O THR B 48 N LEU B 40
SHEET 1 BC 3 ILE B 175 ASP B 179 0
SHEET 2 BC 3 VAL B 376 VAL B 381 1 O ALA B 377 N THR B 176
SHEET 3 BC 3 GLU B 186 VAL B 190 -1 O GLU B 186 N LYS B 380
SHEET 1 BD 4 MET B 193 PHE B 195 0
SHEET 2 BD 4 THR B 330 ILE B 333 -1 O THR B 330 N PHE B 195
SHEET 3 BD 4 ARG B 322 ILE B 325 -1 O ARG B 322 N ILE B 333
SHEET 4 BD 4 VAL B 213 GLU B 216 -1 O VAL B 213 N ILE B 325
SHEET 1 BE 4 VAL B 273 LYS B 277 0
SHEET 2 BE 4 LEU B 247 ALA B 251 1 O LEU B 247 N ALA B 274
SHEET 3 BE 4 PHE B 219 LEU B 221 1 O PHE B 219 N LEU B 248
SHEET 4 BE 4 GLY B 318 GLN B 319 -1 O GLY B 318 N ILE B 220
SHEET 1 BF 2 VAL B 411 ALA B 413 0
SHEET 2 BF 2 LEU B 494 PRO B 496 -1 O ASP B 495 N VAL B 412
SHEET 1 BG 2 TYR B 476 ASN B 479 0
SHEET 2 BG 2 GLU B 484 ASN B 487 -1 O GLU B 484 N ASN B 479
SHEET 1 CA 2 LYS C 4 PHE C 8 0
SHEET 2 CA 2 CYS C 519 ASP C 523 -1 O MET C 520 N LYS C 7
SHEET 1 CB 2 VAL C 38 LEU C 40 0
SHEET 2 CB 2 THR C 48 THR C 50 -1 O THR C 48 N LEU C 40
SHEET 1 CC 3 ILE C 175 ASP C 179 0
SHEET 2 CC 3 VAL C 376 VAL C 381 1 O ALA C 377 N THR C 176
SHEET 3 CC 3 GLU C 186 VAL C 190 -1 O GLU C 186 N LYS C 380
SHEET 1 CD 4 MET C 193 PHE C 195 0
SHEET 2 CD 4 THR C 330 ILE C 333 -1 O THR C 330 N PHE C 195
SHEET 3 CD 4 ARG C 322 ILE C 325 -1 O ARG C 322 N ILE C 333
SHEET 4 CD 4 VAL C 213 GLU C 216 -1 O VAL C 213 N ILE C 325
SHEET 1 CE 4 VAL C 273 LYS C 277 0
SHEET 2 CE 4 LEU C 247 ALA C 251 1 O LEU C 247 N ALA C 274
SHEET 3 CE 4 PHE C 219 LEU C 221 1 O PHE C 219 N LEU C 248
SHEET 4 CE 4 GLY C 318 GLN C 319 -1 O GLY C 318 N ILE C 220
SHEET 1 CF 2 VAL C 411 ALA C 413 0
SHEET 2 CF 2 LEU C 494 PRO C 496 -1 O ASP C 495 N VAL C 412
SHEET 1 CG 2 TYR C 476 ASN C 479 0
SHEET 2 CG 2 GLU C 484 ASN C 487 -1 O GLU C 484 N ASN C 479
SHEET 1 DA 2 LYS D 4 PHE D 8 0
SHEET 2 DA 2 CYS D 519 ASP D 523 -1 O MET D 520 N LYS D 7
SHEET 1 DB 2 VAL D 38 LEU D 40 0
SHEET 2 DB 2 THR D 48 THR D 50 -1 O THR D 48 N LEU D 40
SHEET 1 DC 3 ILE D 175 ASP D 179 0
SHEET 2 DC 3 VAL D 376 VAL D 381 1 O ALA D 377 N THR D 176
SHEET 3 DC 3 GLU D 186 VAL D 190 -1 O GLU D 186 N LYS D 380
SHEET 1 DD 4 MET D 193 PHE D 195 0
SHEET 2 DD 4 THR D 330 ILE D 333 -1 O THR D 330 N PHE D 195
SHEET 3 DD 4 ARG D 322 ILE D 325 -1 O ARG D 322 N ILE D 333
SHEET 4 DD 4 VAL D 213 GLU D 216 -1 O VAL D 213 N ILE D 325
SHEET 1 DE 4 VAL D 273 LYS D 277 0
SHEET 2 DE 4 LEU D 247 ALA D 251 1 O LEU D 247 N ALA D 274
SHEET 3 DE 4 PHE D 219 LEU D 221 1 O PHE D 219 N LEU D 248
SHEET 4 DE 4 GLY D 318 GLN D 319 -1 O GLY D 318 N ILE D 220
SHEET 1 DF 2 VAL D 411 ALA D 413 0
SHEET 2 DF 2 LEU D 494 PRO D 496 -1 O ASP D 495 N VAL D 412
SHEET 1 DG 2 TYR D 476 ASN D 479 0
SHEET 2 DG 2 GLU D 484 ASN D 487 -1 O GLU D 484 N ASN D 479
SHEET 1 EA 2 LYS E 4 PHE E 8 0
SHEET 2 EA 2 CYS E 519 ASP E 523 -1 O MET E 520 N LYS E 7
SHEET 1 EB 2 VAL E 38 LEU E 40 0
SHEET 2 EB 2 THR E 48 THR E 50 -1 O THR E 48 N LEU E 40
SHEET 1 EC 3 ILE E 175 ASP E 179 0
SHEET 2 EC 3 VAL E 376 VAL E 381 1 O ALA E 377 N THR E 176
SHEET 3 EC 3 GLU E 186 VAL E 190 -1 O GLU E 186 N LYS E 380
SHEET 1 ED 4 MET E 193 PHE E 195 0
SHEET 2 ED 4 THR E 330 ILE E 333 -1 O THR E 330 N PHE E 195
SHEET 3 ED 4 ARG E 322 ILE E 325 -1 O ARG E 322 N ILE E 333
SHEET 4 ED 4 VAL E 213 GLU E 216 -1 O VAL E 213 N ILE E 325
SHEET 1 EE 4 VAL E 273 LYS E 277 0
SHEET 2 EE 4 LEU E 247 ALA E 251 1 O LEU E 247 N ALA E 274
SHEET 3 EE 4 PHE E 219 LEU E 221 1 O PHE E 219 N LEU E 248
SHEET 4 EE 4 GLY E 318 GLN E 319 -1 O GLY E 318 N ILE E 220
SHEET 1 EF 2 VAL E 411 ALA E 413 0
SHEET 2 EF 2 LEU E 494 PRO E 496 -1 O ASP E 495 N VAL E 412
SHEET 1 EG 2 TYR E 476 ASN E 479 0
SHEET 2 EG 2 GLU E 484 ASN E 487 -1 O GLU E 484 N ASN E 479
SHEET 1 FA 2 LYS F 4 PHE F 8 0
SHEET 2 FA 2 CYS F 519 ASP F 523 -1 O MET F 520 N LYS F 7
SHEET 1 FB 2 VAL F 38 LEU F 40 0
SHEET 2 FB 2 THR F 48 THR F 50 -1 O THR F 48 N LEU F 40
SHEET 1 FC 3 ILE F 175 ASP F 179 0
SHEET 2 FC 3 VAL F 376 VAL F 381 1 O ALA F 377 N THR F 176
SHEET 3 FC 3 GLU F 186 VAL F 190 -1 O GLU F 186 N LYS F 380
SHEET 1 FD 4 MET F 193 PHE F 195 0
SHEET 2 FD 4 THR F 330 ILE F 333 -1 O THR F 330 N PHE F 195
SHEET 3 FD 4 ARG F 322 ILE F 325 -1 O ARG F 322 N ILE F 333
SHEET 4 FD 4 VAL F 213 GLU F 216 -1 O VAL F 213 N ILE F 325
SHEET 1 FE 4 VAL F 273 LYS F 277 0
SHEET 2 FE 4 LEU F 247 ALA F 251 1 O LEU F 247 N ALA F 274
SHEET 3 FE 4 PHE F 219 LEU F 221 1 O PHE F 219 N LEU F 248
SHEET 4 FE 4 GLY F 318 GLN F 319 -1 O GLY F 318 N ILE F 220
SHEET 1 FF 2 VAL F 411 ALA F 413 0
SHEET 2 FF 2 LEU F 494 PRO F 496 -1 O ASP F 495 N VAL F 412
SHEET 1 FG 2 TYR F 476 ASN F 479 0
SHEET 2 FG 2 GLU F 484 ASN F 487 -1 O GLU F 484 N ASN F 479
SHEET 1 GA 2 LYS G 4 PHE G 8 0
SHEET 2 GA 2 CYS G 519 ASP G 523 -1 O MET G 520 N LYS G 7
SHEET 1 GB 2 VAL G 38 LEU G 40 0
SHEET 2 GB 2 THR G 48 THR G 50 -1 O THR G 48 N LEU G 40
SHEET 1 GC 3 ILE G 175 ASP G 179 0
SHEET 2 GC 3 VAL G 376 VAL G 381 1 O ALA G 377 N THR G 176
SHEET 3 GC 3 GLU G 186 VAL G 190 -1 O GLU G 186 N LYS G 380
SHEET 1 GD 4 MET G 193 PHE G 195 0
SHEET 2 GD 4 THR G 330 ILE G 333 -1 O THR G 330 N PHE G 195
SHEET 3 GD 4 ARG G 322 ILE G 325 -1 O ARG G 322 N ILE G 333
SHEET 4 GD 4 VAL G 213 GLU G 216 -1 O VAL G 213 N ILE G 325
SHEET 1 GE 4 VAL G 273 LYS G 277 0
SHEET 2 GE 4 LEU G 247 ALA G 251 1 O LEU G 247 N ALA G 274
SHEET 3 GE 4 PHE G 219 LEU G 221 1 O PHE G 219 N LEU G 248
SHEET 4 GE 4 GLY G 318 GLN G 319 -1 O GLY G 318 N ILE G 220
SHEET 1 GF 2 VAL G 411 ALA G 413 0
SHEET 2 GF 2 LEU G 494 PRO G 496 -1 O ASP G 495 N VAL G 412
SHEET 1 GG 2 TYR G 476 ASN G 479 0
SHEET 2 GG 2 GLU G 484 ASN G 487 -1 O GLU G 484 N ASN G 479
SHEET 1 HA 4 LYS H 4 LYS H 7 0
SHEET 2 HA 4 GLU H 518 ASP H 523 -1 O MET H 520 N LYS H 7
SHEET 3 HA 4 ASN N 37 LEU N 40 1 N VAL N 38 O GLU H 518
SHEET 4 HA 4 THR N 48 ILE N 49 -1 O THR N 48 N LEU N 40
SHEET 1 HB 4 THR H 48 ILE H 49 0
SHEET 2 HB 4 ASN H 37 LEU H 40 -1 O LEU H 40 N THR H 48
SHEET 3 HB 4 GLU I 518 ASP I 523 1 O GLU I 518 N VAL H 38
SHEET 4 HB 4 LYS I 4 LYS I 7 -1 O ASP I 5 N THR I 522
SHEET 1 HC 3 ILE H 175 ASP H 179 0
SHEET 2 HC 3 VAL H 376 VAL H 381 1 O ALA H 377 N THR H 176
SHEET 3 HC 3 GLU H 186 VAL H 190 -1 O GLU H 186 N LYS H 380
SHEET 1 HD 6 GLN H 194 PHE H 195 0
SHEET 2 HD 6 THR H 330 GLY H 335 -1 O THR H 330 N PHE H 195
SHEET 3 HD 6 GLY H 318 ILE H 325 -1 N LYS H 321 O ASP H 334
SHEET 4 HD 6 PHE H 219 ALA H 223 -1 O ILE H 220 N GLY H 318
SHEET 5 HD 6 LEU H 247 ALA H 251 1 O LEU H 248 N LEU H 221
SHEET 6 HD 6 VAL H 273 LYS H 277 1 O ALA H 274 N ILE H 249
SHEET 1 HE 4 GLN H 194 PHE H 195 0
SHEET 2 HE 4 THR H 330 GLY H 335 -1 O THR H 330 N PHE H 195
SHEET 3 HE 4 GLY H 318 ILE H 325 -1 N LYS H 321 O ASP H 334
SHEET 4 HE 4 VAL H 213 GLU H 216 1 O VAL H 213 N ILE H 325
SHEET 1 HF 2 VAL H 411 ALA H 413 0
SHEET 2 HF 2 LEU H 494 PRO H 496 -1 O ASP H 495 N VAL H 412
SHEET 1 HG 2 GLY H 477 ASN H 479 0
SHEET 2 HG 2 GLU H 484 GLY H 486 -1 O GLU H 484 N ASN H 479
SHEET 1 IA 4 THR I 48 ILE I 49 0
SHEET 2 IA 4 ASN I 37 LEU I 40 -1 O LEU I 40 N THR I 48
SHEET 3 IA 4 GLU J 518 ASP J 523 1 O GLU J 518 N VAL I 38
SHEET 4 IA 4 LYS J 4 LYS J 7 -1 O ASP J 5 N THR J 522
SHEET 1 IB 3 ILE I 175 ASP I 179 0
SHEET 2 IB 3 VAL I 376 VAL I 381 1 O ALA I 377 N THR I 176
SHEET 3 IB 3 GLU I 186 VAL I 190 -1 O GLU I 186 N LYS I 380
SHEET 1 IC 6 GLN I 194 PHE I 195 0
SHEET 2 IC 6 THR I 330 GLY I 335 -1 O THR I 330 N PHE I 195
SHEET 3 IC 6 GLY I 318 ILE I 325 -1 N LYS I 321 O ASP I 334
SHEET 4 IC 6 PHE I 219 ALA I 223 -1 O ILE I 220 N GLY I 318
SHEET 5 IC 6 LEU I 247 ALA I 251 1 O LEU I 248 N LEU I 221
SHEET 6 IC 6 VAL I 273 LYS I 277 1 O ALA I 274 N ILE I 249
SHEET 1 ID 4 GLN I 194 PHE I 195 0
SHEET 2 ID 4 THR I 330 GLY I 335 -1 O THR I 330 N PHE I 195
SHEET 3 ID 4 GLY I 318 ILE I 325 -1 N LYS I 321 O ASP I 334
SHEET 4 ID 4 VAL I 213 GLU I 216 1 O VAL I 213 N ILE I 325
SHEET 1 IE 2 VAL I 411 ALA I 413 0
SHEET 2 IE 2 LEU I 494 PRO I 496 -1 O ASP I 495 N VAL I 412
SHEET 1 IF 2 GLY I 477 ASN I 479 0
SHEET 2 IF 2 GLU I 484 GLY I 486 -1 O GLU I 484 N ASN I 479
SHEET 1 JA 4 THR J 48 ILE J 49 0
SHEET 2 JA 4 ASN J 37 LEU J 40 -1 O LEU J 40 N THR J 48
SHEET 3 JA 4 GLU K 518 ASP K 523 1 O GLU K 518 N VAL J 38
SHEET 4 JA 4 LYS K 4 LYS K 7 -1 O ASP K 5 N THR K 522
SHEET 1 JB 3 ILE J 175 ASP J 179 0
SHEET 2 JB 3 VAL J 376 VAL J 381 1 O ALA J 377 N THR J 176
SHEET 3 JB 3 GLU J 186 VAL J 190 -1 O GLU J 186 N LYS J 380
SHEET 1 JC 6 GLN J 194 PHE J 195 0
SHEET 2 JC 6 THR J 330 GLY J 335 -1 O THR J 330 N PHE J 195
SHEET 3 JC 6 GLY J 318 ILE J 325 -1 N LYS J 321 O ASP J 334
SHEET 4 JC 6 PHE J 219 ALA J 223 -1 O ILE J 220 N GLY J 318
SHEET 5 JC 6 LEU J 247 ALA J 251 1 O LEU J 248 N LEU J 221
SHEET 6 JC 6 VAL J 273 LYS J 277 1 O ALA J 274 N ILE J 249
SHEET 1 JD 4 GLN J 194 PHE J 195 0
SHEET 2 JD 4 THR J 330 GLY J 335 -1 O THR J 330 N PHE J 195
SHEET 3 JD 4 GLY J 318 ILE J 325 -1 N LYS J 321 O ASP J 334
SHEET 4 JD 4 VAL J 213 GLU J 216 1 O VAL J 213 N ILE J 325
SHEET 1 JE 2 VAL J 411 ALA J 413 0
SHEET 2 JE 2 LEU J 494 PRO J 496 -1 O ASP J 495 N VAL J 412
SHEET 1 JF 2 GLY J 477 ASN J 479 0
SHEET 2 JF 2 GLU J 484 GLY J 486 -1 O GLU J 484 N ASN J 479
SHEET 1 KA 4 THR K 48 ILE K 49 0
SHEET 2 KA 4 ASN K 37 LEU K 40 -1 O LEU K 40 N THR K 48
SHEET 3 KA 4 GLU L 518 ASP L 523 1 O GLU L 518 N VAL K 38
SHEET 4 KA 4 LYS L 4 LYS L 7 -1 O ASP L 5 N THR L 522
SHEET 1 KB 3 ILE K 175 ASP K 179 0
SHEET 2 KB 3 VAL K 376 VAL K 381 1 O ALA K 377 N THR K 176
SHEET 3 KB 3 GLU K 186 VAL K 190 -1 O GLU K 186 N LYS K 380
SHEET 1 KC 6 GLN K 194 PHE K 195 0
SHEET 2 KC 6 THR K 330 GLY K 335 -1 O THR K 330 N PHE K 195
SHEET 3 KC 6 GLY K 318 ILE K 325 -1 N LYS K 321 O ASP K 334
SHEET 4 KC 6 PHE K 219 ALA K 223 -1 O ILE K 220 N GLY K 318
SHEET 5 KC 6 LEU K 247 ALA K 251 1 O LEU K 248 N LEU K 221
SHEET 6 KC 6 VAL K 273 LYS K 277 1 O ALA K 274 N ILE K 249
SHEET 1 KD 4 GLN K 194 PHE K 195 0
SHEET 2 KD 4 THR K 330 GLY K 335 -1 O THR K 330 N PHE K 195
SHEET 3 KD 4 GLY K 318 ILE K 325 -1 N LYS K 321 O ASP K 334
SHEET 4 KD 4 VAL K 213 GLU K 216 1 O VAL K 213 N ILE K 325
SHEET 1 KE 2 VAL K 411 ALA K 413 0
SHEET 2 KE 2 LEU K 494 PRO K 496 -1 O ASP K 495 N VAL K 412
SHEET 1 KF 2 GLY K 477 ASN K 479 0
SHEET 2 KF 2 GLU K 484 GLY K 486 -1 O GLU K 484 N ASN K 479
SHEET 1 LA 4 THR L 48 ILE L 49 0
SHEET 2 LA 4 ASN L 37 LEU L 40 -1 O LEU L 40 N THR L 48
SHEET 3 LA 4 GLU M 518 ASP M 523 1 O GLU M 518 N VAL L 38
SHEET 4 LA 4 LYS M 4 LYS M 7 -1 O ASP M 5 N THR M 522
SHEET 1 LB 3 VAL L 177 ASP L 179 0
SHEET 2 LB 3 VAL L 376 VAL L 381 1 O ILE L 379 N GLU L 178
SHEET 3 LB 3 GLU L 186 VAL L 190 -1 O GLU L 186 N LYS L 380
SHEET 1 LC 6 GLN L 194 PHE L 195 0
SHEET 2 LC 6 THR L 330 GLY L 335 -1 O THR L 330 N PHE L 195
SHEET 3 LC 6 GLY L 318 ILE L 325 -1 N LYS L 321 O ASP L 334
SHEET 4 LC 6 PHE L 219 ALA L 223 -1 O ILE L 220 N GLY L 318
SHEET 5 LC 6 LEU L 247 ALA L 251 1 O LEU L 248 N LEU L 221
SHEET 6 LC 6 VAL L 273 LYS L 277 1 O ALA L 274 N ILE L 249
SHEET 1 LD 4 GLN L 194 PHE L 195 0
SHEET 2 LD 4 THR L 330 GLY L 335 -1 O THR L 330 N PHE L 195
SHEET 3 LD 4 GLY L 318 ILE L 325 -1 N LYS L 321 O ASP L 334
SHEET 4 LD 4 VAL L 213 GLU L 216 1 O VAL L 213 N ILE L 325
SHEET 1 LE 2 VAL L 411 ALA L 413 0
SHEET 2 LE 2 LEU L 494 PRO L 496 -1 O ASP L 495 N VAL L 412
SHEET 1 LF 2 GLY L 477 ASN L 479 0
SHEET 2 LF 2 GLU L 484 GLY L 486 -1 O GLU L 484 N ASN L 479
SHEET 1 MA 4 THR M 48 ILE M 49 0
SHEET 2 MA 4 ASN M 37 LEU M 40 -1 O LEU M 40 N THR M 48
SHEET 3 MA 4 GLU N 518 ASP N 523 1 O GLU N 518 N VAL M 38
SHEET 4 MA 4 LYS N 4 LYS N 7 -1 O ASP N 5 N THR N 522
SHEET 1 MB 3 ILE M 175 ASP M 179 0
SHEET 2 MB 3 VAL M 376 VAL M 381 1 O ALA M 377 N THR M 176
SHEET 3 MB 3 GLU M 186 VAL M 190 -1 O GLU M 186 N LYS M 380
SHEET 1 MC 6 GLN M 194 PHE M 195 0
SHEET 2 MC 6 THR M 330 GLY M 335 -1 O THR M 330 N PHE M 195
SHEET 3 MC 6 GLY M 318 ILE M 325 -1 N LYS M 321 O ASP M 334
SHEET 4 MC 6 PHE M 219 ALA M 223 -1 O ILE M 220 N GLY M 318
SHEET 5 MC 6 LEU M 247 ALA M 251 1 O LEU M 248 N LEU M 221
SHEET 6 MC 6 VAL M 273 LYS M 277 1 O ALA M 274 N ILE M 249
SHEET 1 MD 4 GLN M 194 PHE M 195 0
SHEET 2 MD 4 THR M 330 GLY M 335 -1 O THR M 330 N PHE M 195
SHEET 3 MD 4 GLY M 318 ILE M 325 -1 N LYS M 321 O ASP M 334
SHEET 4 MD 4 VAL M 213 GLU M 216 1 O VAL M 213 N ILE M 325
SHEET 1 ME 2 VAL M 411 ALA M 413 0
SHEET 2 ME 2 LEU M 494 PRO M 496 -1 O ASP M 495 N VAL M 412
SHEET 1 MF 2 GLY M 477 ASN M 479 0
SHEET 2 MF 2 GLU M 484 GLY M 486 -1 O GLU M 484 N ASN M 479
SHEET 1 NA 3 ILE N 175 ASP N 179 0
SHEET 2 NA 3 VAL N 376 VAL N 381 1 O ALA N 377 N THR N 176
SHEET 3 NA 3 GLU N 186 VAL N 190 -1 O GLU N 186 N LYS N 380
SHEET 1 NB 6 GLN N 194 PHE N 195 0
SHEET 2 NB 6 THR N 330 GLY N 335 -1 O THR N 330 N PHE N 195
SHEET 3 NB 6 GLY N 318 ILE N 325 -1 N LYS N 321 O ASP N 334
SHEET 4 NB 6 PHE N 219 ALA N 223 -1 O ILE N 220 N GLY N 318
SHEET 5 NB 6 LEU N 247 ALA N 251 1 O LEU N 248 N LEU N 221
SHEET 6 NB 6 VAL N 273 LYS N 277 1 O ALA N 274 N ILE N 249
SHEET 1 NC 4 GLN N 194 PHE N 195 0
SHEET 2 NC 4 THR N 330 GLY N 335 -1 O THR N 330 N PHE N 195
SHEET 3 NC 4 GLY N 318 ILE N 325 -1 N LYS N 321 O ASP N 334
SHEET 4 NC 4 VAL N 213 GLU N 216 1 O VAL N 213 N ILE N 325
SHEET 1 ND 2 VAL N 411 ALA N 413 0
SHEET 2 ND 2 LEU N 494 PRO N 496 -1 O ASP N 495 N VAL N 412
SHEET 1 NE 2 GLY N 477 ASN N 479 0
SHEET 2 NE 2 GLU N 484 GLY N 486 -1 O GLU N 484 N ASN N 479
LINK MG MG A1526 O1B ATP A1527 1555 1555 1.81
LINK MG MG A1526 O2A ATP A1527 1555 1555 1.82
LINK MG MG A1526 OD1 ASP A 87 1555 1555 1.86
LINK MG MG A1526 OD2 ASP A 87 1555 1555 1.93
LINK MG MG A1526 O3G ATP A1527 1555 1555 1.80
LINK MG MG B1526 O2A ATP B1527 1555 1555 1.82
LINK MG MG B1526 OD1 ASP B 87 1555 1555 1.86
LINK MG MG B1526 OD2 ASP B 87 1555 1555 1.91
LINK MG MG B1526 O3G ATP B1527 1555 1555 1.80
LINK MG MG B1526 O1B ATP B1527 1555 1555 1.83
LINK MG MG C1526 O1B ATP C1527 1555 1555 1.81
LINK MG MG C1526 O2A ATP C1527 1555 1555 1.82
LINK MG MG C1526 OD1 ASP C 87 1555 1555 1.85
LINK MG MG C1526 OD2 ASP C 87 1555 1555 1.93
LINK MG MG C1526 O3G ATP C1527 1555 1555 1.80
LINK MG MG D1526 OD1 ASP D 87 1555 1555 1.87
LINK MG MG D1526 OD2 ASP D 87 1555 1555 1.91
LINK MG MG D1526 O3G ATP D1527 1555 1555 1.80
LINK MG MG D1526 O1B ATP D1527 1555 1555 1.82
LINK MG MG D1526 O2A ATP D1527 1555 1555 1.83
LINK MG MG E1526 OD2 ASP E 87 1555 1555 1.93
LINK MG MG E1526 OD1 ASP E 87 1555 1555 1.86
LINK MG MG E1526 O1B ATP E1527 1555 1555 1.81
LINK MG MG E1526 O3G ATP E1527 1555 1555 1.80
LINK MG MG E1526 O2A ATP E1527 1555 1555 1.82
LINK MG MG F1526 O2A ATP F1527 1555 1555 1.83
LINK MG MG F1526 O3G ATP F1527 1555 1555 1.80
LINK MG MG F1526 OD1 ASP F 87 1555 1555 1.87
LINK MG MG F1526 O1B ATP F1527 1555 1555 1.82
LINK MG MG F1526 OD2 ASP F 87 1555 1555 1.91
LINK MG MG G1526 OD2 ASP G 87 1555 1555 1.93
LINK MG MG G1526 O1B ATP G1527 1555 1555 1.81
LINK MG MG G1526 OD1 ASP G 87 1555 1555 1.86
LINK MG MG G1526 O3G ATP G1527 1555 1555 1.80
LINK MG MG G1526 O2A ATP G1527 1555 1555 1.82
LINK MG MG H1526 OD1 ASP H 87 1555 1555 1.85
LINK MG MG H1526 O1B ATP H1527 1555 1555 1.81
LINK MG MG H1526 O2A ATP H1527 1555 1555 1.82
LINK MG MG H1526 OD2 ASP H 87 1555 1555 1.92
LINK MG MG H1526 O3G ATP H1527 1555 1555 1.78
LINK MG MG I1526 O1B ATP I1527 1555 1555 1.81
LINK MG MG I1526 O3G ATP I1527 1555 1555 1.78
LINK MG MG I1526 O2A ATP I1527 1555 1555 1.82
LINK MG MG I1526 OD2 ASP I 87 1555 1555 1.92
LINK MG MG I1526 OD1 ASP I 87 1555 1555 1.85
LINK MG MG J1526 OD1 ASP J 87 1555 1555 1.85
LINK MG MG J1526 O3G ATP J1527 1555 1555 1.78
LINK MG MG J1526 O2A ATP J1527 1555 1555 1.82
LINK MG MG J1526 O1B ATP J1527 1555 1555 1.81
LINK MG MG J1526 OD2 ASP J 87 1555 1555 1.92
LINK MG MG K1526 O3G ATP K1527 1555 1555 1.78
LINK MG MG K1526 O2A ATP K1527 1555 1555 1.82
LINK MG MG K1526 OD2 ASP K 87 1555 1555 1.92
LINK MG MG K1526 OD1 ASP K 87 1555 1555 1.85
LINK MG MG K1526 O1B ATP K1527 1555 1555 1.81
LINK MG MG L1526 O1B ATP L1527 1555 1555 1.81
LINK MG MG L1526 O2A ATP L1527 1555 1555 1.82
LINK MG MG L1526 O3G ATP L1527 1555 1555 1.78
LINK MG MG L1526 OD2 ASP L 87 1555 1555 1.92
LINK MG MG L1526 OD1 ASP L 87 1555 1555 1.85
LINK MG MG M1526 O3G ATP M1527 1555 1555 1.78
LINK MG MG M1526 O2A ATP M1527 1555 1555 1.82
LINK MG MG M1526 O1B ATP M1527 1555 1555 1.81
LINK MG MG M1526 OD2 ASP M 87 1555 1555 1.92
LINK MG MG M1526 OD1 ASP M 87 1555 1555 1.85
LINK MG MG N1526 O3G ATP N1527 1555 1555 1.78
LINK MG MG N1526 O2A ATP N1527 1555 1555 1.82
LINK MG MG N1526 O1B ATP N1527 1555 1555 1.81
LINK MG MG N1526 OD2 ASP N 87 1555 1555 1.92
LINK MG MG N1526 OD1 ASP N 87 1555 1555 1.85
CISPEP 1 ALA A 384 THR A 385 0 14.57
CISPEP 2 ALA B 384 THR B 385 0 14.61
CISPEP 3 ALA C 384 THR C 385 0 14.57
CISPEP 4 ALA D 384 THR D 385 0 14.56
CISPEP 5 ALA E 384 THR E 385 0 14.52
CISPEP 6 ALA F 384 THR F 385 0 14.59
CISPEP 7 ALA G 384 THR G 385 0 14.52
CISPEP 8 PHE H 8 GLY H 9 0 22.61
CISPEP 9 ASN H 153 SER H 154 0 -6.01
CISPEP 10 GLY H 182 LEU H 183 0 -2.31
CISPEP 11 LYS H 242 ALA H 243 0 -11.43
CISPEP 12 ALA H 384 THR H 385 0 -7.53
CISPEP 13 PHE I 8 GLY I 9 0 22.56
CISPEP 14 ASN I 153 SER I 154 0 -6.01
CISPEP 15 GLY I 182 LEU I 183 0 -10.55
CISPEP 16 LYS I 242 ALA I 243 0 -11.45
CISPEP 17 ALA I 384 THR I 385 0 -7.44
CISPEP 18 PHE J 8 GLY J 9 0 22.48
CISPEP 19 ASN J 153 SER J 154 0 -5.96
CISPEP 20 GLY J 182 LEU J 183 0 -10.49
CISPEP 21 LYS J 242 ALA J 243 0 -11.47
CISPEP 22 ALA J 384 THR J 385 0 -7.54
CISPEP 23 PHE K 8 GLY K 9 0 22.53
CISPEP 24 ASN K 153 SER K 154 0 -6.00
CISPEP 25 GLY K 182 LEU K 183 0 -10.51
CISPEP 26 LYS K 242 ALA K 243 0 -11.37
CISPEP 27 ALA K 384 THR K 385 0 -7.62
CISPEP 28 PHE L 8 GLY L 9 0 22.48
CISPEP 29 ASN L 153 SER L 154 0 -5.96
CISPEP 30 GLY L 182 LEU L 183 0 -8.25
CISPEP 31 LYS L 242 ALA L 243 0 -11.40
CISPEP 32 ALA L 384 THR L 385 0 -7.47
CISPEP 33 PHE M 8 GLY M 9 0 22.50
CISPEP 34 ASN M 153 SER M 154 0 -5.97
CISPEP 35 GLY M 182 LEU M 183 0 -10.46
CISPEP 36 LYS M 242 ALA M 243 0 -11.46
CISPEP 37 ALA M 384 THR M 385 0 -7.47
CISPEP 38 PHE N 8 GLY N 9 0 22.48
CISPEP 39 ASN N 153 SER N 154 0 -5.97
CISPEP 40 GLY N 182 LEU N 183 0 -10.48
CISPEP 41 LYS N 242 ALA N 243 0 -11.42
CISPEP 42 ALA N 384 THR N 385 0 -7.57
SITE 1 AC1 3 LYS A 51 ASP A 52 ATP A1527
SITE 1 AC2 4 ASP A 87 GLY A 88 SER A 151 ATP A1527
SITE 1 AC3 15 LEU A 31 GLY A 53 ASP A 87 GLY A 88
SITE 2 AC3 15 THR A 89 THR A 90 THR A 91 ILE A 150
SITE 3 AC3 15 ASN A 153 GLY A 414 GLY A 415 ILE A 454
SITE 4 AC3 15 ASP A 495 PO4 A1525 MG A1526
SITE 1 AC4 3 LYS B 51 ASP B 52 ATP B1527
SITE 1 AC5 4 ASP B 87 GLY B 88 SER B 151 ATP B1527
SITE 1 AC6 16 LEU B 31 GLY B 53 ASP B 87 GLY B 88
SITE 2 AC6 16 THR B 89 THR B 90 THR B 91 ILE B 150
SITE 3 AC6 16 SER B 151 ASN B 153 GLY B 414 GLY B 415
SITE 4 AC6 16 ILE B 454 ASP B 495 PO4 B1525 MG B1526
SITE 1 AC7 3 LYS C 51 ASP C 52 ATP C1527
SITE 1 AC8 4 ASP C 87 GLY C 88 SER C 151 ATP C1527
SITE 1 AC9 15 LEU C 31 GLY C 53 ASP C 87 GLY C 88
SITE 2 AC9 15 THR C 89 THR C 90 THR C 91 ILE C 150
SITE 3 AC9 15 ASN C 153 GLY C 414 GLY C 415 ILE C 454
SITE 4 AC9 15 ASP C 495 PO4 C1525 MG C1526
SITE 1 BC1 2 ASP D 52 ATP D1527
SITE 1 BC2 4 ASP D 87 GLY D 88 SER D 151 ATP D1527
SITE 1 BC3 15 LEU D 31 GLY D 53 ASP D 87 GLY D 88
SITE 2 BC3 15 THR D 89 THR D 90 THR D 91 ILE D 150
SITE 3 BC3 15 ASN D 153 GLY D 414 GLY D 415 ILE D 454
SITE 4 BC3 15 ASP D 495 PO4 D1525 MG D1526
SITE 1 BC4 3 LYS E 51 ASP E 52 ATP E1527
SITE 1 BC5 4 ASP E 87 GLY E 88 SER E 151 ATP E1527
SITE 1 BC6 15 LEU E 31 GLY E 53 ASP E 87 GLY E 88
SITE 2 BC6 15 THR E 89 THR E 90 THR E 91 ILE E 150
SITE 3 BC6 15 ASN E 153 GLY E 414 GLY E 415 ILE E 454
SITE 4 BC6 15 ASP E 495 PO4 E1525 MG E1526
SITE 1 BC7 2 ASP F 52 ATP F1527
SITE 1 BC8 4 ASP F 87 GLY F 88 SER F 151 ATP F1527
SITE 1 BC9 15 LEU F 31 GLY F 53 ASP F 87 GLY F 88
SITE 2 BC9 15 THR F 89 THR F 90 THR F 91 ILE F 150
SITE 3 BC9 15 ASN F 153 GLY F 414 GLY F 415 ILE F 454
SITE 4 BC9 15 ASP F 495 PO4 F1525 MG F1526
SITE 1 CC1 3 LYS G 51 ASP G 52 ATP G1527
SITE 1 CC2 4 ASP G 87 GLY G 88 SER G 151 ATP G1527
SITE 1 CC3 15 LEU G 31 GLY G 53 ASP G 87 GLY G 88
SITE 2 CC3 15 THR G 89 THR G 90 THR G 91 ILE G 150
SITE 3 CC3 15 ASN G 153 GLY G 414 GLY G 415 ILE G 454
SITE 4 CC3 15 ASP G 495 PO4 G1525 MG G1526
SITE 1 CC4 4 ASP H 52 ASN H 153 MG H1526 ATP H1527
SITE 1 CC5 4 ASP H 87 GLY H 88 PO4 H1525 ATP H1527
SITE 1 CC6 20 LEU H 31 ASP H 52 GLY H 53 ASP H 87
SITE 2 CC6 20 GLY H 88 THR H 89 THR H 90 THR H 91
SITE 3 CC6 20 ASN H 153 GLY H 414 GLY H 415 ILE H 454
SITE 4 CC6 20 TYR H 478 ASN H 479 ALA H 480 ALA H 481
SITE 5 CC6 20 ILE H 493 ASP H 495 PO4 H1525 MG H1526
SITE 1 CC7 4 ASP I 52 ASN I 153 MG I1526 ATP I1527
SITE 1 CC8 4 ASP I 87 GLY I 88 PO4 I1525 ATP I1527
SITE 1 CC9 20 LEU I 31 ASP I 52 GLY I 53 ASP I 87
SITE 2 CC9 20 GLY I 88 THR I 89 THR I 90 THR I 91
SITE 3 CC9 20 ASN I 153 GLY I 414 GLY I 415 ILE I 454
SITE 4 CC9 20 TYR I 478 ASN I 479 ALA I 480 ALA I 481
SITE 5 CC9 20 ILE I 493 ASP I 495 PO4 I1525 MG I1526
SITE 1 DC1 4 ASP J 52 ASN J 153 MG J1526 ATP J1527
SITE 1 DC2 4 ASP J 87 GLY J 88 PO4 J1525 ATP J1527
SITE 1 DC3 20 LEU J 31 ASP J 52 GLY J 53 ASP J 87
SITE 2 DC3 20 GLY J 88 THR J 89 THR J 90 THR J 91
SITE 3 DC3 20 ASN J 153 GLY J 414 GLY J 415 ILE J 454
SITE 4 DC3 20 TYR J 478 ASN J 479 ALA J 480 ALA J 481
SITE 5 DC3 20 ILE J 493 ASP J 495 PO4 J1525 MG J1526
SITE 1 DC4 4 ASP K 52 ASN K 153 MG K1526 ATP K1527
SITE 1 DC5 4 ASP K 87 GLY K 88 PO4 K1525 ATP K1527
SITE 1 DC6 20 LEU K 31 ASP K 52 GLY K 53 ASP K 87
SITE 2 DC6 20 GLY K 88 THR K 89 THR K 90 THR K 91
SITE 3 DC6 20 ASN K 153 GLY K 414 GLY K 415 ILE K 454
SITE 4 DC6 20 TYR K 478 ASN K 479 ALA K 480 ALA K 481
SITE 5 DC6 20 ILE K 493 ASP K 495 PO4 K1525 MG K1526
SITE 1 DC7 4 ASP L 52 ASN L 153 MG L1526 ATP L1527
SITE 1 DC8 4 ASP L 87 GLY L 88 PO4 L1525 ATP L1527
SITE 1 DC9 20 LEU L 31 ASP L 52 GLY L 53 ASP L 87
SITE 2 DC9 20 GLY L 88 THR L 89 THR L 90 THR L 91
SITE 3 DC9 20 ASN L 153 GLY L 414 GLY L 415 ILE L 454
SITE 4 DC9 20 TYR L 478 ASN L 479 ALA L 480 ALA L 481
SITE 5 DC9 20 ILE L 493 ASP L 495 PO4 L1525 MG L1526
SITE 1 EC1 4 ASP M 52 ASN M 153 MG M1526 ATP M1527
SITE 1 EC2 4 ASP M 87 GLY M 88 PO4 M1525 ATP M1527
SITE 1 EC3 20 LEU M 31 ASP M 52 GLY M 53 ASP M 87
SITE 2 EC3 20 GLY M 88 THR M 89 THR M 90 THR M 91
SITE 3 EC3 20 ASN M 153 GLY M 414 GLY M 415 ILE M 454
SITE 4 EC3 20 TYR M 478 ASN M 479 ALA M 480 ALA M 481
SITE 5 EC3 20 ILE M 493 ASP M 495 PO4 M1525 MG M1526
SITE 1 EC4 4 ASP N 52 ASN N 153 MG N1526 ATP N1527
SITE 1 EC5 4 ASP N 87 GLY N 88 PO4 N1525 ATP N1527
SITE 1 EC6 20 LEU N 31 ASP N 52 GLY N 53 ASP N 87
SITE 2 EC6 20 GLY N 88 THR N 89 THR N 90 THR N 91
SITE 3 EC6 20 ASN N 153 GLY N 414 GLY N 415 ILE N 454
SITE 4 EC6 20 TYR N 478 ASN N 479 ALA N 480 ALA N 481
SITE 5 EC6 20 ILE N 493 ASP N 495 PO4 N1525 MG N1526
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
