HEADER DNA BINDING PROTEIN 22-OCT-18 6HZ9
TITLE STRUCTURE OF MCRBC WITHOUT DNA BINDING DOMAINS (CLASS 5)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5-METHYLCYTOSINE-SPECIFIC RESTRICTION ENZYME B;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: ECOKMCRBC;
COMPND 5 EC: 3.1.21.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN MCRC;
COMPND 9 CHAIN: M, N;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: MCRB, RGLB, B4346, JW5871;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(AI);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHIS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 13 ORGANISM_TAXID: 83333;
SOURCE 14 STRAIN: K12;
SOURCE 15 GENE: MCRC, B4345, JW5789;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(AI);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHIS
KEYWDS AAA+ SUPERFAMILY, RESTRICTION ENZYME, DNA BINDING PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.ITOH,N.NIRWAN,K.SAIKRISHNAN,A.AMUNTS
REVDAT 2 06-NOV-19 6HZ9 1 REMARK
REVDAT 1 24-JUL-19 6HZ9 0
JRNL AUTH N.NIRWAN,Y.ITOH,P.SINGH,S.BANDYOPADHYAY,K.R.VINOTHKUMAR,
JRNL AUTH 2 A.AMUNTS,K.SAIKRISHNAN
JRNL TITL STRUCTURE-BASED MECHANISM FOR ACTIVATION OF THE AAA+ GTPASE
JRNL TITL 2 MCRB BY THE ENDONUCLEASE MCRC.
JRNL REF NAT COMMUN V. 10 3058 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31296862
JRNL DOI 10.1038/S41467-019-11084-1
REMARK 2
REMARK 2 RESOLUTION. 4.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GAUTOMATCH, EPU, GCTF, COOT, PHENIX,
REMARK 3 RELION, RELION, RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL
REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : 74.000
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.800
REMARK 3 NUMBER OF PARTICLES : 225201
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6HZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012552.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : MCRB AND MCRC COMPLEX WITHOUT
REMARK 245 DNA BINDING DOMAINS
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 4.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : THE N-TERMINAL DNA BINDING
REMARK 245 DOMAIN OF MCRB IS TRUNCATED
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 3326
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 1.50
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 130000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 64950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 162130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -290.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, M, G, H, I,
REMARK 350 AND CHAINS: J, K, L, 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 162
REMARK 465 SER A 163
REMARK 465 LYS A 164
REMARK 465 THR A 165
REMARK 465 GLU A 166
REMARK 465 SER A 167
REMARK 465 ASP A 458
REMARK 465 SER A 459
REMARK 465 SER A 460
REMARK 465 GLY A 461
REMARK 465 SER A 462
REMARK 465 HIS A 463
REMARK 465 HIS A 464
REMARK 465 HIS A 465
REMARK 465 HIS A 466
REMARK 465 HIS A 467
REMARK 465 HIS A 468
REMARK 465 MET B 162
REMARK 465 SER B 163
REMARK 465 LYS B 164
REMARK 465 THR B 165
REMARK 465 GLU B 166
REMARK 465 SER B 167
REMARK 465 ASP B 458
REMARK 465 SER B 459
REMARK 465 SER B 460
REMARK 465 GLY B 461
REMARK 465 SER B 462
REMARK 465 HIS B 463
REMARK 465 HIS B 464
REMARK 465 HIS B 465
REMARK 465 HIS B 466
REMARK 465 HIS B 467
REMARK 465 HIS B 468
REMARK 465 MET C 162
REMARK 465 SER C 163
REMARK 465 LYS C 164
REMARK 465 THR C 165
REMARK 465 GLU C 166
REMARK 465 SER C 167
REMARK 465 ASP C 458
REMARK 465 SER C 459
REMARK 465 SER C 460
REMARK 465 GLY C 461
REMARK 465 SER C 462
REMARK 465 HIS C 463
REMARK 465 HIS C 464
REMARK 465 HIS C 465
REMARK 465 HIS C 466
REMARK 465 HIS C 467
REMARK 465 HIS C 468
REMARK 465 MET D 162
REMARK 465 SER D 163
REMARK 465 LYS D 164
REMARK 465 THR D 165
REMARK 465 GLU D 166
REMARK 465 SER D 167
REMARK 465 TYR D 168
REMARK 465 CYS D 169
REMARK 465 LEU D 170
REMARK 465 GLU D 171
REMARK 465 ASP D 172
REMARK 465 ALA D 173
REMARK 465 ASP D 458
REMARK 465 SER D 459
REMARK 465 SER D 460
REMARK 465 GLY D 461
REMARK 465 SER D 462
REMARK 465 HIS D 463
REMARK 465 HIS D 464
REMARK 465 HIS D 465
REMARK 465 HIS D 466
REMARK 465 HIS D 467
REMARK 465 HIS D 468
REMARK 465 MET E 162
REMARK 465 SER E 163
REMARK 465 LYS E 164
REMARK 465 THR E 165
REMARK 465 GLU E 166
REMARK 465 SER E 167
REMARK 465 TYR E 168
REMARK 465 CYS E 169
REMARK 465 LEU E 170
REMARK 465 GLU E 171
REMARK 465 ASP E 172
REMARK 465 ASP E 458
REMARK 465 SER E 459
REMARK 465 SER E 460
REMARK 465 GLY E 461
REMARK 465 SER E 462
REMARK 465 HIS E 463
REMARK 465 HIS E 464
REMARK 465 HIS E 465
REMARK 465 HIS E 466
REMARK 465 HIS E 467
REMARK 465 HIS E 468
REMARK 465 MET F 162
REMARK 465 SER F 163
REMARK 465 LYS F 164
REMARK 465 THR F 165
REMARK 465 GLU F 166
REMARK 465 SER F 167
REMARK 465 TYR F 168
REMARK 465 CYS F 169
REMARK 465 LEU F 170
REMARK 465 GLU F 171
REMARK 465 ASP F 172
REMARK 465 ASP F 458
REMARK 465 SER F 459
REMARK 465 SER F 460
REMARK 465 GLY F 461
REMARK 465 SER F 462
REMARK 465 HIS F 463
REMARK 465 HIS F 464
REMARK 465 HIS F 465
REMARK 465 HIS F 466
REMARK 465 HIS F 467
REMARK 465 HIS F 468
REMARK 465 MET M 1
REMARK 465 GLU M 2
REMARK 465 LEU M 22
REMARK 465 GLN M 23
REMARK 465 GLU M 24
REMARK 465 ILE M 25
REMARK 465 LYS M 26
REMARK 465 GLN M 27
REMARK 465 ARG M 268
REMARK 465 MET M 269
REMARK 465 GLY M 270
REMARK 465 THR M 271
REMARK 465 MET G 162
REMARK 465 SER G 163
REMARK 465 LYS G 164
REMARK 465 THR G 165
REMARK 465 GLU G 166
REMARK 465 SER G 167
REMARK 465 ASP G 458
REMARK 465 SER G 459
REMARK 465 SER G 460
REMARK 465 GLY G 461
REMARK 465 SER G 462
REMARK 465 HIS G 463
REMARK 465 HIS G 464
REMARK 465 HIS G 465
REMARK 465 HIS G 466
REMARK 465 HIS G 467
REMARK 465 HIS G 468
REMARK 465 MET H 162
REMARK 465 SER H 163
REMARK 465 LYS H 164
REMARK 465 THR H 165
REMARK 465 GLU H 166
REMARK 465 SER H 167
REMARK 465 ASP H 458
REMARK 465 SER H 459
REMARK 465 SER H 460
REMARK 465 GLY H 461
REMARK 465 SER H 462
REMARK 465 HIS H 463
REMARK 465 HIS H 464
REMARK 465 HIS H 465
REMARK 465 HIS H 466
REMARK 465 HIS H 467
REMARK 465 HIS H 468
REMARK 465 MET I 162
REMARK 465 SER I 163
REMARK 465 LYS I 164
REMARK 465 THR I 165
REMARK 465 GLU I 166
REMARK 465 SER I 167
REMARK 465 ASP I 458
REMARK 465 SER I 459
REMARK 465 SER I 460
REMARK 465 GLY I 461
REMARK 465 SER I 462
REMARK 465 HIS I 463
REMARK 465 HIS I 464
REMARK 465 HIS I 465
REMARK 465 HIS I 466
REMARK 465 HIS I 467
REMARK 465 HIS I 468
REMARK 465 MET J 162
REMARK 465 SER J 163
REMARK 465 LYS J 164
REMARK 465 THR J 165
REMARK 465 GLU J 166
REMARK 465 SER J 167
REMARK 465 TYR J 168
REMARK 465 CYS J 169
REMARK 465 LEU J 170
REMARK 465 GLU J 171
REMARK 465 ASP J 172
REMARK 465 ALA J 173
REMARK 465 ASP J 458
REMARK 465 SER J 459
REMARK 465 SER J 460
REMARK 465 GLY J 461
REMARK 465 SER J 462
REMARK 465 HIS J 463
REMARK 465 HIS J 464
REMARK 465 HIS J 465
REMARK 465 HIS J 466
REMARK 465 HIS J 467
REMARK 465 HIS J 468
REMARK 465 MET K 162
REMARK 465 SER K 163
REMARK 465 LYS K 164
REMARK 465 THR K 165
REMARK 465 GLU K 166
REMARK 465 SER K 167
REMARK 465 TYR K 168
REMARK 465 CYS K 169
REMARK 465 LEU K 170
REMARK 465 GLU K 171
REMARK 465 ASP K 172
REMARK 465 ASP K 458
REMARK 465 SER K 459
REMARK 465 SER K 460
REMARK 465 GLY K 461
REMARK 465 SER K 462
REMARK 465 HIS K 463
REMARK 465 HIS K 464
REMARK 465 HIS K 465
REMARK 465 HIS K 466
REMARK 465 HIS K 467
REMARK 465 HIS K 468
REMARK 465 MET L 162
REMARK 465 SER L 163
REMARK 465 LYS L 164
REMARK 465 THR L 165
REMARK 465 GLU L 166
REMARK 465 SER L 167
REMARK 465 TYR L 168
REMARK 465 CYS L 169
REMARK 465 LEU L 170
REMARK 465 GLU L 171
REMARK 465 ASP L 172
REMARK 465 ASP L 458
REMARK 465 SER L 459
REMARK 465 SER L 460
REMARK 465 GLY L 461
REMARK 465 SER L 462
REMARK 465 HIS L 463
REMARK 465 HIS L 464
REMARK 465 HIS L 465
REMARK 465 HIS L 466
REMARK 465 HIS L 467
REMARK 465 HIS L 468
REMARK 465 MET N 1
REMARK 465 GLU N 2
REMARK 465 LEU N 22
REMARK 465 GLN N 23
REMARK 465 GLU N 24
REMARK 465 ILE N 25
REMARK 465 LYS N 26
REMARK 465 GLN N 27
REMARK 465 ARG N 268
REMARK 465 MET N 269
REMARK 465 GLY N 270
REMARK 465 THR N 271
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 C ALA F 335 H ASP F 336 1.28
REMARK 500 C LYS E 384 H MET E 385 1.28
REMARK 500 C GLU E 438 H GLU E 439 1.28
REMARK 500 C GLU E 391 H ILE E 392 1.28
REMARK 500 C SER E 380 H LEU E 381 1.28
REMARK 500 C GLN E 383 H LYS E 384 1.29
REMARK 500 C GLU E 387 H LEU E 388 1.29
REMARK 500 O ARG I 283 HH TYR N 62 1.57
REMARK 500 O PRO D 362 H ASN D 366 1.58
REMARK 500 O PRO J 362 H ASN J 366 1.58
REMARK 500 O ILE H 242 H GLY H 257 1.59
REMARK 500 O ILE B 242 H GLY B 257 1.59
REMARK 500 OG SER J 408 O4' GDP J 1001 1.99
REMARK 500 OG SER D 408 O4' GDP D 1001 1.99
REMARK 500 O ARG I 283 OH TYR N 62 2.04
REMARK 500 O THR N 219 OG1 THR N 246 2.06
REMARK 500 O THR M 219 OG1 THR M 246 2.06
REMARK 500 NZ LYS A 255 O SER B 313 2.09
REMARK 500 OE1 GLN J 269 OH TYR J 274 2.12
REMARK 500 OE1 GLN D 269 OH TYR D 274 2.12
REMARK 500 O PHE F 441 NE2 GLN F 448 2.14
REMARK 500 O PHE L 441 NE2 GLN L 448 2.14
REMARK 500 NZ LYS N 110 O LEU N 137 2.14
REMARK 500 NZ LYS M 110 O LEU M 137 2.14
REMARK 500 OG SER N 111 O LEU N 143 2.16
REMARK 500 OG SER M 111 O LEU M 143 2.16
REMARK 500 O ALA B 173 NH2 ARG B 213 2.16
REMARK 500 O ALA H 173 NH2 ARG H 213 2.16
REMARK 500 OG1 THR B 208 O2B GNP B 1001 2.18
REMARK 500 OE1 GLU K 280 OH TYR L 344 2.18
REMARK 500 OG1 THR H 208 O2B GNP H 1001 2.18
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 LYS A 195 -1.06 70.66
REMARK 500 ILE A 242 -70.29 -104.20
REMARK 500 VAL A 250 -50.27 -130.94
REMARK 500 LYS A 371 48.59 -92.71
REMARK 500 ASP A 432 -55.17 -122.00
REMARK 500 LYS B 195 -8.52 77.58
REMARK 500 ILE B 242 -70.29 -119.60
REMARK 500 LYS B 371 53.72 -93.24
REMARK 500 ASP B 443 -51.33 -124.37
REMARK 500 LYS C 195 -0.44 70.40
REMARK 500 ILE C 242 -68.91 -104.50
REMARK 500 ASN C 285 95.27 -68.56
REMARK 500 LYS C 371 48.64 -95.16
REMARK 500 LYS D 195 -3.12 74.55
REMARK 500 ILE D 242 -69.96 -104.08
REMARK 500 LYS D 301 55.74 -91.53
REMARK 500 ASP D 444 64.87 -152.58
REMARK 500 LYS E 195 -5.57 71.88
REMARK 500 ILE E 242 -70.02 -102.91
REMARK 500 ASP E 443 -55.39 -121.92
REMARK 500 ILE F 193 -62.74 -98.84
REMARK 500 LYS F 195 -1.51 71.24
REMARK 500 ILE F 242 -72.45 -121.55
REMARK 500 ALA F 340 -54.59 -121.88
REMARK 500 HIS M 89 33.23 -99.02
REMARK 500 LEU M 137 73.80 -117.22
REMARK 500 ASN M 175 57.17 -99.80
REMARK 500 ILE M 316 -66.44 -97.18
REMARK 500 GLU M 331 141.95 -174.78
REMARK 500 LYS G 195 -1.01 70.58
REMARK 500 ILE G 242 -70.36 -104.16
REMARK 500 VAL G 250 -50.24 -130.98
REMARK 500 LYS G 371 48.61 -92.72
REMARK 500 ASP G 432 -55.15 -122.11
REMARK 500 LYS H 195 -8.56 77.60
REMARK 500 ILE H 242 -70.31 -119.53
REMARK 500 LYS H 371 53.72 -93.30
REMARK 500 ASP H 443 -51.37 -124.37
REMARK 500 LYS I 195 -0.44 70.35
REMARK 500 ILE I 242 -68.92 -104.44
REMARK 500 ASN I 285 95.29 -68.55
REMARK 500 LYS I 371 48.67 -95.17
REMARK 500 LYS J 195 -3.07 74.55
REMARK 500 ILE J 242 -69.97 -104.04
REMARK 500 LYS J 301 55.71 -91.53
REMARK 500 ASP J 444 64.95 -152.53
REMARK 500 LYS K 195 -5.58 71.90
REMARK 500 ILE K 242 -70.08 -102.87
REMARK 500 ASP K 443 -55.33 -121.95
REMARK 500 ILE L 193 -62.70 -98.86
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 208 OG1
REMARK 620 2 GNP A1001 O3G 136.8
REMARK 620 3 GNP A1001 O1B 66.0 99.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 208 OG1
REMARK 620 2 GNP B1001 O3G 114.9
REMARK 620 3 GNP B1001 O2B 64.9 96.3
REMARK 620 4 GNP B1001 O2A 86.5 151.4 75.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 208 OG1
REMARK 620 2 GNP C1001 O3G 131.2
REMARK 620 3 GNP C1001 O2B 87.3 97.4
REMARK 620 4 GNP C1001 O2A 89.8 138.4 89.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 208 OG1
REMARK 620 2 GNP G1001 O3G 136.8
REMARK 620 3 GNP G1001 O1B 66.0 99.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR H 208 OG1
REMARK 620 2 GNP H1001 O3G 114.8
REMARK 620 3 GNP H1001 O2B 64.9 96.3
REMARK 620 4 GNP H1001 O2A 86.5 151.4 75.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR I 208 OG1
REMARK 620 2 GNP I1001 O3G 131.2
REMARK 620 3 GNP I1001 O2B 87.4 97.4
REMARK 620 4 GNP I1001 O2A 89.8 138.4 89.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP D 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP F 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP G 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP H 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP I 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP J 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP K 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP L 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-0315 RELATED DB: EMDB
REMARK 900 STRUCTURE OF MCRBC WITHOUT DNA BINDING DOMAINS (CLASS 5)
DBREF 6HZ9 A 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 B 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 C 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 D 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 E 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 F 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 M 1 348 UNP P15006 MCRC_ECOLI 1 348
DBREF 6HZ9 G 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 H 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 I 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 J 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 K 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 L 162 459 UNP P15005 MCRB_ECOLI 162 459
DBREF 6HZ9 N 1 348 UNP P15006 MCRC_ECOLI 1 348
SEQADV 6HZ9 SER A 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY A 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER A 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS A 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS A 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS A 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS A 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS A 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS A 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER B 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY B 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER B 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS B 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS B 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS B 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS B 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS B 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS B 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER C 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY C 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER C 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS C 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS C 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS C 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS C 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS C 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS C 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER D 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY D 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER D 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS D 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS D 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS D 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS D 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS D 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS D 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER E 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY E 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER E 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS E 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS E 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS E 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS E 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS E 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS E 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER F 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY F 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER F 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS F 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS F 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS F 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS F 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS F 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS F 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER G 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY G 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER G 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS G 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS G 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS G 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS G 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS G 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS G 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER H 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY H 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER H 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS H 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS H 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS H 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS H 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS H 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS H 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER I 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY I 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER I 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS I 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS I 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS I 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS I 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS I 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS I 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER J 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY J 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER J 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS J 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS J 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS J 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS J 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS J 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS J 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER K 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY K 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER K 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS K 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS K 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS K 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS K 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS K 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS K 468 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER L 460 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 GLY L 461 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 SER L 462 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS L 463 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS L 464 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS L 465 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS L 466 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS L 467 UNP P15005 EXPRESSION TAG
SEQADV 6HZ9 HIS L 468 UNP P15005 EXPRESSION TAG
SEQRES 1 A 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 A 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 A 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 A 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 A 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 A 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 A 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 A 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 A 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 A 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 A 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 A 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 A 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 A 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 A 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 A 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 A 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 A 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 A 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 A 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 A 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 A 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 A 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 A 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 B 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 B 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 B 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 B 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 B 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 B 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 B 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 B 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 B 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 B 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 B 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 B 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 B 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 B 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 B 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 B 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 B 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 B 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 B 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 B 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 B 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 B 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 B 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 C 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 C 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 C 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 C 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 C 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 C 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 C 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 C 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 C 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 C 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 C 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 C 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 C 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 C 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 C 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 C 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 C 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 C 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 C 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 C 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 C 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 C 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 C 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 C 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 D 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 D 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 D 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 D 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 D 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 D 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 D 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 D 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 D 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 D 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 D 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 D 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 D 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 D 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 D 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 D 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 D 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 D 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 D 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 D 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 D 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 D 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 D 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 D 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 E 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 E 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 E 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 E 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 E 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 E 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 E 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 E 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 E 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 E 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 E 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 E 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 E 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 E 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 E 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 E 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 E 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 E 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 E 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 E 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 E 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 E 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 E 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 F 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 F 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 F 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 F 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 F 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 F 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 F 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 F 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 F 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 F 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 F 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 F 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 F 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 F 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 F 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 F 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 F 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 F 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 F 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 F 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 F 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 F 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 F 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 F 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 M 348 MET GLU GLN PRO VAL ILE PRO VAL ARG ASN ILE TYR TYR
SEQRES 2 M 348 MET LEU THR TYR ALA TRP GLY TYR LEU GLN GLU ILE LYS
SEQRES 3 M 348 GLN ALA ASN LEU GLU ALA ILE PRO GLY ASN ASN LEU LEU
SEQRES 4 M 348 ASP ILE LEU GLY TYR VAL LEU ASN LYS GLY VAL LEU GLN
SEQRES 5 M 348 LEU SER ARG ARG GLY LEU GLU LEU ASP TYR ASN PRO ASN
SEQRES 6 M 348 THR GLU ILE ILE PRO GLY ILE LYS GLY ARG ILE GLU PHE
SEQRES 7 M 348 ALA LYS THR ILE ARG GLY PHE HIS LEU ASN HIS GLY LYS
SEQRES 8 M 348 THR VAL SER THR PHE ASP MET LEU ASN GLU ASP THR LEU
SEQRES 9 M 348 ALA ASN ARG ILE ILE LYS SER THR LEU ALA ILE LEU ILE
SEQRES 10 M 348 LYS HIS GLU LYS LEU ASN SER THR ILE ARG ASP GLU ALA
SEQRES 11 M 348 ARG SER LEU TYR ARG LYS LEU PRO GLY ILE SER THR LEU
SEQRES 12 M 348 HIS LEU THR PRO GLN HIS PHE SER TYR LEU ASN GLY GLY
SEQRES 13 M 348 LYS ASN THR ARG TYR TYR LYS PHE VAL ILE SER VAL CYS
SEQRES 14 M 348 LYS PHE ILE VAL ASN ASN SER ILE PRO GLY GLN ASN LYS
SEQRES 15 M 348 GLY HIS TYR ARG PHE TYR ASP PHE GLU ARG ASN GLU LYS
SEQRES 16 M 348 GLU MET SER LEU LEU TYR GLN LYS PHE LEU TYR GLU PHE
SEQRES 17 M 348 CYS ARG ARG GLU LEU THR SER ALA ASN THR THR ARG SER
SEQRES 18 M 348 TYR LEU LYS TRP ASP ALA SER SER ILE SER ASP GLN SER
SEQRES 19 M 348 LEU ASN LEU LEU PRO ARG MET GLU THR ASP ILE THR ILE
SEQRES 20 M 348 ARG SER SER GLU LYS ILE LEU ILE VAL ASP ALA LYS TYR
SEQRES 21 M 348 TYR LYS SER ILE PHE SER ARG ARG MET GLY THR GLU LYS
SEQRES 22 M 348 PHE HIS SER GLN ASN LEU TYR GLN LEU MET ASN TYR LEU
SEQRES 23 M 348 TRP SER LEU LYS PRO GLU ASN GLY GLU ASN ILE GLY GLY
SEQRES 24 M 348 LEU LEU ILE TYR PRO HIS VAL ASP THR ALA VAL LYS HIS
SEQRES 25 M 348 ARG TYR LYS ILE ASN GLY PHE ASP ILE GLY LEU CYS THR
SEQRES 26 M 348 VAL ASN LEU GLY GLN GLU TRP PRO CYS ILE HIS GLN GLU
SEQRES 27 M 348 LEU LEU ASP ILE PHE ASP GLU TYR LEU LYS
SEQRES 1 G 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 G 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 G 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 G 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 G 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 G 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 G 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 G 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 G 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 G 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 G 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 G 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 G 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 G 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 G 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 G 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 G 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 G 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 G 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 G 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 G 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 G 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 G 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 G 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 H 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 H 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 H 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 H 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 H 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 H 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 H 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 H 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 H 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 H 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 H 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 H 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 H 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 H 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 H 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 H 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 H 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 H 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 H 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 H 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 H 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 H 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 H 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 H 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 I 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 I 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 I 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 I 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 I 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 I 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 I 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 I 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 I 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 I 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 I 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 I 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 I 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 I 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 I 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 I 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 I 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 I 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 I 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 I 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 I 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 I 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 I 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 I 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 J 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 J 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 J 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 J 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 J 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 J 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 J 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 J 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 J 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 J 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 J 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 J 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 J 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 J 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 J 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 J 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 J 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 J 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 J 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 J 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 J 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 J 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 J 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 J 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 K 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 K 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 K 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 K 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 K 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 K 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 K 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 K 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 K 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 K 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 K 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 K 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 K 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 K 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 K 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 K 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 K 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 K 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 K 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 K 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 K 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 K 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 K 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 K 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 L 307 MET SER LYS THR GLU SER TYR CYS LEU GLU ASP ALA LEU
SEQRES 2 L 307 ASN ASP LEU PHE ILE PRO GLU THR THR ILE GLU THR ILE
SEQRES 3 L 307 LEU LYS ARG LEU THR ILE LYS LYS ASN ILE ILE LEU GLN
SEQRES 4 L 307 GLY PRO PRO GLY VAL GLY LYS THR PHE VAL ALA ARG ARG
SEQRES 5 L 307 LEU ALA TYR LEU LEU THR GLY GLU LYS ALA PRO GLN ARG
SEQRES 6 L 307 VAL ASN MET VAL GLN PHE HIS GLN SER TYR SER TYR GLU
SEQRES 7 L 307 ASP PHE ILE GLN GLY TYR ARG PRO ASN GLY VAL GLY PHE
SEQRES 8 L 307 ARG ARG LYS ASP GLY ILE PHE TYR ASN PHE CYS GLN GLN
SEQRES 9 L 307 ALA LYS GLU GLN PRO GLU LYS LYS TYR ILE PHE ILE ILE
SEQRES 10 L 307 ASP GLU ILE ASN ARG ALA ASN LEU SER LYS VAL PHE GLY
SEQRES 11 L 307 GLU VAL MET MET LEU MET GLU HIS ASP LYS ARG GLY GLU
SEQRES 12 L 307 ASN TRP SER VAL PRO LEU THR TYR SER GLU ASN ASP GLU
SEQRES 13 L 307 GLU ARG PHE TYR VAL PRO GLU ASN VAL TYR ILE ILE GLY
SEQRES 14 L 307 LEU MET ASN THR ALA ASP ARG SER LEU ALA VAL VAL ASP
SEQRES 15 L 307 TYR ALA LEU ARG ARG ARG PHE SER PHE ILE ASP ILE GLU
SEQRES 16 L 307 PRO GLY PHE ASP THR PRO GLN PHE ARG ASN PHE LEU LEU
SEQRES 17 L 307 ASN LYS LYS ALA GLU PRO SER PHE VAL GLU SER LEU CYS
SEQRES 18 L 307 GLN LYS MET ASN GLU LEU ASN GLN GLU ILE SER LYS GLU
SEQRES 19 L 307 ALA THR ILE LEU GLY LYS GLY PHE ARG ILE GLY HIS SER
SEQRES 20 L 307 TYR PHE CYS CYS GLY LEU GLU ASP GLY THR SER PRO ASP
SEQRES 21 L 307 THR GLN TRP LEU ASN GLU ILE VAL MET THR ASP ILE ALA
SEQRES 22 L 307 PRO LEU LEU GLU GLU TYR PHE PHE ASP ASP PRO TYR LYS
SEQRES 23 L 307 GLN GLN LYS TRP THR ASN LYS LEU LEU GLY ASP SER SER
SEQRES 24 L 307 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 N 348 MET GLU GLN PRO VAL ILE PRO VAL ARG ASN ILE TYR TYR
SEQRES 2 N 348 MET LEU THR TYR ALA TRP GLY TYR LEU GLN GLU ILE LYS
SEQRES 3 N 348 GLN ALA ASN LEU GLU ALA ILE PRO GLY ASN ASN LEU LEU
SEQRES 4 N 348 ASP ILE LEU GLY TYR VAL LEU ASN LYS GLY VAL LEU GLN
SEQRES 5 N 348 LEU SER ARG ARG GLY LEU GLU LEU ASP TYR ASN PRO ASN
SEQRES 6 N 348 THR GLU ILE ILE PRO GLY ILE LYS GLY ARG ILE GLU PHE
SEQRES 7 N 348 ALA LYS THR ILE ARG GLY PHE HIS LEU ASN HIS GLY LYS
SEQRES 8 N 348 THR VAL SER THR PHE ASP MET LEU ASN GLU ASP THR LEU
SEQRES 9 N 348 ALA ASN ARG ILE ILE LYS SER THR LEU ALA ILE LEU ILE
SEQRES 10 N 348 LYS HIS GLU LYS LEU ASN SER THR ILE ARG ASP GLU ALA
SEQRES 11 N 348 ARG SER LEU TYR ARG LYS LEU PRO GLY ILE SER THR LEU
SEQRES 12 N 348 HIS LEU THR PRO GLN HIS PHE SER TYR LEU ASN GLY GLY
SEQRES 13 N 348 LYS ASN THR ARG TYR TYR LYS PHE VAL ILE SER VAL CYS
SEQRES 14 N 348 LYS PHE ILE VAL ASN ASN SER ILE PRO GLY GLN ASN LYS
SEQRES 15 N 348 GLY HIS TYR ARG PHE TYR ASP PHE GLU ARG ASN GLU LYS
SEQRES 16 N 348 GLU MET SER LEU LEU TYR GLN LYS PHE LEU TYR GLU PHE
SEQRES 17 N 348 CYS ARG ARG GLU LEU THR SER ALA ASN THR THR ARG SER
SEQRES 18 N 348 TYR LEU LYS TRP ASP ALA SER SER ILE SER ASP GLN SER
SEQRES 19 N 348 LEU ASN LEU LEU PRO ARG MET GLU THR ASP ILE THR ILE
SEQRES 20 N 348 ARG SER SER GLU LYS ILE LEU ILE VAL ASP ALA LYS TYR
SEQRES 21 N 348 TYR LYS SER ILE PHE SER ARG ARG MET GLY THR GLU LYS
SEQRES 22 N 348 PHE HIS SER GLN ASN LEU TYR GLN LEU MET ASN TYR LEU
SEQRES 23 N 348 TRP SER LEU LYS PRO GLU ASN GLY GLU ASN ILE GLY GLY
SEQRES 24 N 348 LEU LEU ILE TYR PRO HIS VAL ASP THR ALA VAL LYS HIS
SEQRES 25 N 348 ARG TYR LYS ILE ASN GLY PHE ASP ILE GLY LEU CYS THR
SEQRES 26 N 348 VAL ASN LEU GLY GLN GLU TRP PRO CYS ILE HIS GLN GLU
SEQRES 27 N 348 LEU LEU ASP ILE PHE ASP GLU TYR LEU LYS
HET GNP A1001 45
HET MG A1002 1
HET GNP B1001 45
HET MG B1002 1
HET GNP C1001 45
HET MG C1002 1
HET GDP D1001 40
HET GDP E1001 40
HET GDP F1001 40
HET GNP G1001 45
HET MG G1002 1
HET GNP H1001 45
HET MG H1002 1
HET GNP I1001 45
HET MG I1002 1
HET GDP J1001 40
HET GDP K1001 40
HET GDP L1001 40
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 15 GNP 6(C10 H17 N6 O13 P3)
FORMUL 16 MG 6(MG 2+)
FORMUL 21 GDP 6(C10 H15 N5 O11 P2)
HELIX 1 AA1 CYS A 169 ASN A 175 1 7
HELIX 2 AA2 PRO A 180 LYS A 195 1 16
HELIX 3 AA3 GLY A 206 GLY A 220 1 15
HELIX 4 AA4 SER A 237 ILE A 242 1 6
HELIX 5 AA5 GLY A 257 GLN A 269 1 13
HELIX 6 AA6 ILE A 281 ALA A 284 5 4
HELIX 7 AA7 ASN A 285 PHE A 290 1 6
HELIX 8 AA8 VAL A 293 GLU A 298 1 6
HELIX 9 AA9 GLY A 303 SER A 307 5 5
HELIX 10 AB1 ARG A 337 VAL A 341 5 5
HELIX 11 AB2 ASP A 343 PHE A 350 1 8
HELIX 12 AB3 THR A 361 LYS A 371 1 11
HELIX 13 AB4 GLU A 374 GLU A 395 1 22
HELIX 14 AB5 GLY A 400 ARG A 404 5 5
HELIX 15 AB6 HIS A 407 CYS A 412 1 6
HELIX 16 AB7 ASP A 421 ASP A 432 1 12
HELIX 17 AB8 ASP A 432 PHE A 441 1 10
HELIX 18 AB9 ASP A 444 GLY A 457 1 14
HELIX 19 AC1 CYS B 169 LEU B 174 1 6
HELIX 20 AC2 PRO B 180 LYS B 195 1 16
HELIX 21 AC3 GLY B 206 GLY B 220 1 15
HELIX 22 AC4 SER B 237 ILE B 242 1 6
HELIX 23 AC5 GLY B 257 LYS B 267 1 11
HELIX 24 AC6 ASN B 285 GLY B 291 1 7
HELIX 25 AC7 GLU B 292 MET B 297 1 6
HELIX 26 AC8 GLY B 303 SER B 307 5 5
HELIX 27 AC9 ASP B 343 ARG B 348 1 6
HELIX 28 AD1 THR B 361 LYS B 371 1 11
HELIX 29 AD2 GLU B 374 GLU B 395 1 22
HELIX 30 AD3 HIS B 407 CYS B 412 1 6
HELIX 31 AD4 ASP B 421 ASP B 432 1 12
HELIX 32 AD5 ASP B 432 PHE B 442 1 11
HELIX 33 AD6 ASP B 444 GLY B 457 1 14
HELIX 34 AD7 CYS C 169 ASN C 175 1 7
HELIX 35 AD8 PRO C 180 LYS C 195 1 16
HELIX 36 AD9 GLY C 206 GLY C 220 1 15
HELIX 37 AE1 SER C 237 ILE C 242 1 6
HELIX 38 AE2 GLY C 257 GLN C 269 1 13
HELIX 39 AE3 ASN C 285 GLY C 291 1 7
HELIX 40 AE4 GLY C 291 MET C 297 1 7
HELIX 41 AE5 GLY C 303 SER C 307 5 5
HELIX 42 AE6 ASP C 343 PHE C 350 1 8
HELIX 43 AE7 THR C 361 LYS C 371 1 11
HELIX 44 AE8 GLU C 374 GLU C 395 1 22
HELIX 45 AE9 GLY C 400 ARG C 404 5 5
HELIX 46 AF1 HIS C 407 CYS C 412 1 6
HELIX 47 AF2 ASP C 421 ASP C 432 1 12
HELIX 48 AF3 ASP C 432 PHE C 441 1 10
HELIX 49 AF4 ASP C 444 GLY C 457 1 14
HELIX 50 AF5 PRO D 180 LYS D 195 1 16
HELIX 51 AF6 GLY D 206 GLY D 220 1 15
HELIX 52 AF7 SER D 237 ILE D 242 1 6
HELIX 53 AF8 GLY D 257 GLN D 269 1 13
HELIX 54 AF9 ASN D 285 GLY D 291 1 7
HELIX 55 AG1 GLU D 292 MET D 297 1 6
HELIX 56 AG2 GLY D 303 SER D 307 5 5
HELIX 57 AG3 ALA D 345 PHE D 350 1 6
HELIX 58 AG4 THR D 361 ASN D 370 1 10
HELIX 59 AG5 GLU D 374 SER D 393 1 20
HELIX 60 AG6 HIS D 407 CYS D 412 1 6
HELIX 61 AG7 ASP D 421 ASP D 432 1 12
HELIX 62 AG8 ASP D 432 PHE D 441 1 10
HELIX 63 AG9 ASP D 444 GLY D 457 1 14
HELIX 64 AH1 PRO E 180 LYS E 195 1 16
HELIX 65 AH2 GLY E 206 GLY E 220 1 15
HELIX 66 AH3 SER E 237 ILE E 242 1 6
HELIX 67 AH4 GLY E 257 GLN E 269 1 13
HELIX 68 AH5 ILE E 281 ALA E 284 5 4
HELIX 69 AH6 ASN E 285 GLY E 291 1 7
HELIX 70 AH7 GLU E 292 MET E 297 1 6
HELIX 71 AH8 GLY E 303 SER E 307 5 5
HELIX 72 AH9 ASP E 343 PHE E 350 1 8
HELIX 73 AI1 THR E 361 ASN E 370 1 10
HELIX 74 AI2 GLU E 374 GLU E 395 1 22
HELIX 75 AI3 GLY E 400 ARG E 404 5 5
HELIX 76 AI4 HIS E 407 CYS E 412 1 6
HELIX 77 AI5 ASP E 421 ASP E 432 1 12
HELIX 78 AI6 ASP E 432 PHE E 442 1 11
HELIX 79 AI7 ASP E 444 GLY E 457 1 14
HELIX 80 AI8 PRO F 180 LYS F 195 1 16
HELIX 81 AI9 GLY F 206 GLY F 220 1 15
HELIX 82 AJ1 SER F 237 ILE F 242 1 6
HELIX 83 AJ2 ILE F 258 GLN F 269 1 12
HELIX 84 AJ3 ASN F 285 GLY F 291 1 7
HELIX 85 AJ4 VAL F 293 GLU F 298 1 6
HELIX 86 AJ5 GLY F 303 SER F 307 5 5
HELIX 87 AJ6 ASP F 343 PHE F 350 1 8
HELIX 88 AJ7 THR F 361 LYS F 371 1 11
HELIX 89 AJ8 GLU F 374 GLU F 395 1 22
HELIX 90 AJ9 GLY F 400 ARG F 404 5 5
HELIX 91 AK1 HIS F 407 CYS F 412 1 6
HELIX 92 AK2 ASP F 421 ASP F 432 1 12
HELIX 93 AK3 ASP F 432 PHE F 441 1 10
HELIX 94 AK4 ASP F 444 GLY F 457 1 14
HELIX 95 AK5 PRO M 7 GLY M 20 1 14
HELIX 96 AK6 ASN M 37 GLY M 57 1 21
HELIX 97 AK7 GLU M 77 PHE M 85 1 9
HELIX 98 AK8 THR M 103 HIS M 119 1 17
HELIX 99 AK9 ASN M 123 LEU M 137 1 15
HELIX 100 AL1 THR M 146 LEU M 153 1 8
HELIX 101 AL2 ASN M 154 GLY M 156 5 3
HELIX 102 AL3 THR M 159 ASN M 175 1 17
HELIX 103 AL4 ASP M 189 ARG M 192 5 4
HELIX 104 AL5 ASN M 193 LEU M 213 1 21
HELIX 105 AL6 LYS M 262 SER M 266 5 5
HELIX 106 AL7 GLN M 277 LEU M 289 1 13
HELIX 107 AL8 GLU M 331 LYS M 348 1 18
HELIX 108 AL9 CYS G 169 ASN G 175 1 7
HELIX 109 AM1 PRO G 180 LYS G 195 1 16
HELIX 110 AM2 GLY G 206 GLY G 220 1 15
HELIX 111 AM3 SER G 237 ILE G 242 1 6
HELIX 112 AM4 GLY G 257 GLN G 269 1 13
HELIX 113 AM5 ILE G 281 ALA G 284 5 4
HELIX 114 AM6 ASN G 285 PHE G 290 1 6
HELIX 115 AM7 VAL G 293 GLU G 298 1 6
HELIX 116 AM8 GLY G 303 SER G 307 5 5
HELIX 117 AM9 ARG G 337 VAL G 341 5 5
HELIX 118 AN1 ASP G 343 PHE G 350 1 8
HELIX 119 AN2 THR G 361 LYS G 371 1 11
HELIX 120 AN3 GLU G 374 GLU G 395 1 22
HELIX 121 AN4 GLY G 400 ARG G 404 5 5
HELIX 122 AN5 HIS G 407 CYS G 412 1 6
HELIX 123 AN6 ASP G 421 ASP G 432 1 12
HELIX 124 AN7 ASP G 432 PHE G 441 1 10
HELIX 125 AN8 ASP G 444 GLY G 457 1 14
HELIX 126 AN9 CYS H 169 LEU H 174 1 6
HELIX 127 AO1 PRO H 180 LYS H 195 1 16
HELIX 128 AO2 GLY H 206 GLY H 220 1 15
HELIX 129 AO3 SER H 237 ILE H 242 1 6
HELIX 130 AO4 GLY H 257 LYS H 267 1 11
HELIX 131 AO5 ASN H 285 GLY H 291 1 7
HELIX 132 AO6 GLU H 292 MET H 297 1 6
HELIX 133 AO7 GLY H 303 SER H 307 5 5
HELIX 134 AO8 ASP H 343 ARG H 348 1 6
HELIX 135 AO9 THR H 361 LYS H 371 1 11
HELIX 136 AP1 GLU H 374 GLU H 395 1 22
HELIX 137 AP2 HIS H 407 CYS H 412 1 6
HELIX 138 AP3 ASP H 421 ASP H 432 1 12
HELIX 139 AP4 ASP H 432 PHE H 442 1 11
HELIX 140 AP5 ASP H 444 GLY H 457 1 14
HELIX 141 AP6 CYS I 169 ASN I 175 1 7
HELIX 142 AP7 PRO I 180 LYS I 195 1 16
HELIX 143 AP8 GLY I 206 GLY I 220 1 15
HELIX 144 AP9 SER I 237 ILE I 242 1 6
HELIX 145 AQ1 GLY I 257 GLN I 269 1 13
HELIX 146 AQ2 ASN I 285 GLY I 291 1 7
HELIX 147 AQ3 GLY I 291 MET I 297 1 7
HELIX 148 AQ4 GLY I 303 SER I 307 5 5
HELIX 149 AQ5 ASP I 343 PHE I 350 1 8
HELIX 150 AQ6 THR I 361 LYS I 371 1 11
HELIX 151 AQ7 GLU I 374 GLU I 395 1 22
HELIX 152 AQ8 GLY I 400 ARG I 404 5 5
HELIX 153 AQ9 HIS I 407 CYS I 412 1 6
HELIX 154 AR1 ASP I 421 ASP I 432 1 12
HELIX 155 AR2 ASP I 432 PHE I 441 1 10
HELIX 156 AR3 ASP I 444 GLY I 457 1 14
HELIX 157 AR4 PRO J 180 LYS J 195 1 16
HELIX 158 AR5 GLY J 206 GLY J 220 1 15
HELIX 159 AR6 SER J 237 ILE J 242 1 6
HELIX 160 AR7 GLY J 257 GLN J 269 1 13
HELIX 161 AR8 ASN J 285 GLY J 291 1 7
HELIX 162 AR9 GLU J 292 MET J 297 1 6
HELIX 163 AS1 GLY J 303 SER J 307 5 5
HELIX 164 AS2 ALA J 345 PHE J 350 1 6
HELIX 165 AS3 THR J 361 ASN J 370 1 10
HELIX 166 AS4 GLU J 374 SER J 393 1 20
HELIX 167 AS5 HIS J 407 CYS J 412 1 6
HELIX 168 AS6 ASP J 421 ASP J 432 1 12
HELIX 169 AS7 ASP J 432 PHE J 441 1 10
HELIX 170 AS8 ASP J 444 GLY J 457 1 14
HELIX 171 AS9 PRO K 180 LYS K 195 1 16
HELIX 172 AT1 GLY K 206 GLY K 220 1 15
HELIX 173 AT2 SER K 237 ILE K 242 1 6
HELIX 174 AT3 GLY K 257 GLN K 269 1 13
HELIX 175 AT4 ILE K 281 ALA K 284 5 4
HELIX 176 AT5 ASN K 285 GLY K 291 1 7
HELIX 177 AT6 GLU K 292 MET K 297 1 6
HELIX 178 AT7 GLY K 303 SER K 307 5 5
HELIX 179 AT8 ASP K 343 PHE K 350 1 8
HELIX 180 AT9 THR K 361 ASN K 370 1 10
HELIX 181 AU1 GLU K 374 GLU K 395 1 22
HELIX 182 AU2 GLY K 400 ARG K 404 5 5
HELIX 183 AU3 HIS K 407 CYS K 412 1 6
HELIX 184 AU4 ASP K 421 ASP K 432 1 12
HELIX 185 AU5 ASP K 432 PHE K 442 1 11
HELIX 186 AU6 ASP K 444 GLY K 457 1 14
HELIX 187 AU7 PRO L 180 LYS L 195 1 16
HELIX 188 AU8 GLY L 206 GLY L 220 1 15
HELIX 189 AU9 SER L 237 ILE L 242 1 6
HELIX 190 AV1 ILE L 258 GLN L 269 1 12
HELIX 191 AV2 ASN L 285 GLY L 291 1 7
HELIX 192 AV3 VAL L 293 GLU L 298 1 6
HELIX 193 AV4 GLY L 303 SER L 307 5 5
HELIX 194 AV5 ASP L 343 PHE L 350 1 8
HELIX 195 AV6 THR L 361 LYS L 371 1 11
HELIX 196 AV7 GLU L 374 GLU L 395 1 22
HELIX 197 AV8 GLY L 400 ARG L 404 5 5
HELIX 198 AV9 HIS L 407 CYS L 412 1 6
HELIX 199 AW1 ASP L 421 ASP L 432 1 12
HELIX 200 AW2 ASP L 432 PHE L 441 1 10
HELIX 201 AW3 ASP L 444 GLY L 457 1 14
HELIX 202 AW4 PRO N 7 GLY N 20 1 14
HELIX 203 AW5 ASN N 37 GLY N 57 1 21
HELIX 204 AW6 GLU N 77 PHE N 85 1 9
HELIX 205 AW7 THR N 103 HIS N 119 1 17
HELIX 206 AW8 ASN N 123 LEU N 137 1 15
HELIX 207 AW9 THR N 146 LEU N 153 1 8
HELIX 208 AX1 ASN N 154 GLY N 156 5 3
HELIX 209 AX2 THR N 159 ASN N 175 1 17
HELIX 210 AX3 ASP N 189 ARG N 192 5 4
HELIX 211 AX4 ASN N 193 LEU N 213 1 21
HELIX 212 AX5 LYS N 262 SER N 266 5 5
HELIX 213 AX6 GLN N 277 LEU N 289 1 13
HELIX 214 AX7 GLU N 331 LYS N 348 1 18
SHEET 1 AA1 5 VAL A 227 GLN A 231 0
SHEET 2 AA1 5 TYR A 274 ASP A 279 1 O ASP A 279 N VAL A 230
SHEET 3 AA1 5 VAL A 326 MET A 332 1 O ILE A 329 N PHE A 276
SHEET 4 AA1 5 ASN A 196 GLN A 200 1 N LEU A 199 O GLY A 330
SHEET 5 AA1 5 SER A 351 ASP A 354 1 O ILE A 353 N GLN A 200
SHEET 1 AA2 2 GLN A 243 PRO A 247 0
SHEET 2 AA2 2 PHE A 252 ASP A 256 -1 O ARG A 253 N ARG A 246
SHEET 1 AA3 5 VAL B 227 GLN B 231 0
SHEET 2 AA3 5 TYR B 274 ASP B 279 1 O ILE B 277 N ASN B 228
SHEET 3 AA3 5 VAL B 326 ASN B 333 1 O TYR B 327 N TYR B 274
SHEET 4 AA3 5 ASN B 196 GLY B 201 1 N LEU B 199 O GLY B 330
SHEET 5 AA3 5 SER B 351 ASP B 354 1 O SER B 351 N ILE B 198
SHEET 1 AA4 2 GLN B 243 PRO B 247 0
SHEET 2 AA4 2 PHE B 252 ASP B 256 -1 O LYS B 255 N GLY B 244
SHEET 1 AA5 2 VAL B 308 PRO B 309 0
SHEET 2 AA5 2 ARG B 319 PHE B 320 -1 O PHE B 320 N VAL B 308
SHEET 1 AA6 5 VAL C 227 GLN C 231 0
SHEET 2 AA6 5 TYR C 274 ASP C 279 1 O ILE C 277 N ASN C 228
SHEET 3 AA6 5 VAL C 326 ASN C 333 1 O TYR C 327 N TYR C 274
SHEET 4 AA6 5 ASN C 196 GLY C 201 1 N LEU C 199 O GLY C 330
SHEET 5 AA6 5 SER C 351 ASP C 354 1 O ILE C 353 N ILE C 198
SHEET 1 AA7 2 GLN C 243 PRO C 247 0
SHEET 2 AA7 2 PHE C 252 ASP C 256 -1 O LYS C 255 N GLY C 244
SHEET 1 AA8 5 VAL D 227 GLN D 231 0
SHEET 2 AA8 5 ILE D 275 ASP D 279 1 O ASP D 279 N VAL D 230
SHEET 3 AA8 5 TYR D 327 ASN D 333 1 O LEU D 331 N ILE D 278
SHEET 4 AA8 5 ASN D 196 GLY D 201 1 N LEU D 199 O GLY D 330
SHEET 5 AA8 5 SER D 351 ASP D 354 1 O ILE D 353 N ILE D 198
SHEET 1 AA9 2 TYR D 245 PRO D 247 0
SHEET 2 AA9 2 PHE D 252 ARG D 254 -1 O ARG D 253 N ARG D 246
SHEET 1 AB1 5 VAL E 227 GLN E 231 0
SHEET 2 AB1 5 TYR E 274 ASP E 279 1 O ASP E 279 N VAL E 230
SHEET 3 AB1 5 VAL E 326 ASN E 333 1 O ILE E 329 N PHE E 276
SHEET 4 AB1 5 ASN E 196 GLY E 201 1 N LEU E 199 O MET E 332
SHEET 5 AB1 5 SER E 351 ASP E 354 1 O ILE E 353 N GLN E 200
SHEET 1 AB2 2 GLN E 243 PRO E 247 0
SHEET 2 AB2 2 PHE E 252 ASP E 256 -1 O LYS E 255 N GLY E 244
SHEET 1 AB3 5 VAL F 227 GLN F 231 0
SHEET 2 AB3 5 TYR F 274 ASP F 279 1 O ASP F 279 N VAL F 230
SHEET 3 AB3 5 VAL F 326 LEU F 331 1 O ILE F 329 N ILE F 278
SHEET 4 AB3 5 ASN F 196 LEU F 199 1 N LEU F 199 O GLY F 330
SHEET 5 AB3 5 SER F 351 ILE F 353 1 O SER F 351 N ILE F 198
SHEET 1 AB4 2 GLN F 243 PRO F 247 0
SHEET 2 AB4 2 PHE F 252 ASP F 256 -1 O LYS F 255 N GLY F 244
SHEET 1 AB5 3 ASP M 61 ILE M 69 0
SHEET 2 AB5 3 THR M 92 ASN M 100 -1 O PHE M 96 N ASN M 65
SHEET 3 AB5 3 ARG M 75 ILE M 76 -1 N ARG M 75 O THR M 95
SHEET 1 AB6 2 SER M 176 PRO M 178 0
SHEET 2 AB6 2 TYR M 185 PHE M 187 -1 O ARG M 186 N ILE M 177
SHEET 1 AB7 6 ASN M 217 THR M 219 0
SHEET 2 AB7 6 ILE M 245 ARG M 248 -1 O THR M 246 N THR M 219
SHEET 3 AB7 6 ILE M 253 ASP M 257 -1 O LEU M 254 N ILE M 247
SHEET 4 AB7 6 ILE M 297 HIS M 305 1 O LEU M 300 N ASP M 257
SHEET 5 AB7 6 ASP M 320 ASN M 327 1 O GLY M 322 N LEU M 301
SHEET 6 AB7 6 LYS M 311 LYS M 315 -1 N HIS M 312 O LEU M 323
SHEET 1 AB8 5 VAL G 227 GLN G 231 0
SHEET 2 AB8 5 TYR G 274 ASP G 279 1 O ASP G 279 N VAL G 230
SHEET 3 AB8 5 VAL G 326 MET G 332 1 O ILE G 329 N PHE G 276
SHEET 4 AB8 5 ASN G 196 GLN G 200 1 N LEU G 199 O GLY G 330
SHEET 5 AB8 5 SER G 351 ASP G 354 1 O ILE G 353 N GLN G 200
SHEET 1 AB9 2 GLN G 243 PRO G 247 0
SHEET 2 AB9 2 PHE G 252 ASP G 256 -1 O ARG G 253 N ARG G 246
SHEET 1 AC1 5 VAL H 227 GLN H 231 0
SHEET 2 AC1 5 TYR H 274 ASP H 279 1 O ILE H 277 N ASN H 228
SHEET 3 AC1 5 VAL H 326 ASN H 333 1 O TYR H 327 N TYR H 274
SHEET 4 AC1 5 ASN H 196 GLY H 201 1 N LEU H 199 O GLY H 330
SHEET 5 AC1 5 SER H 351 ASP H 354 1 O SER H 351 N ILE H 198
SHEET 1 AC2 2 GLN H 243 PRO H 247 0
SHEET 2 AC2 2 PHE H 252 ASP H 256 -1 O LYS H 255 N GLY H 244
SHEET 1 AC3 2 VAL H 308 PRO H 309 0
SHEET 2 AC3 2 ARG H 319 PHE H 320 -1 O PHE H 320 N VAL H 308
SHEET 1 AC4 5 VAL I 227 GLN I 231 0
SHEET 2 AC4 5 TYR I 274 ASP I 279 1 O ILE I 277 N ASN I 228
SHEET 3 AC4 5 VAL I 326 ASN I 333 1 O TYR I 327 N TYR I 274
SHEET 4 AC4 5 ASN I 196 GLY I 201 1 N LEU I 199 O GLY I 330
SHEET 5 AC4 5 SER I 351 ASP I 354 1 O ILE I 353 N ILE I 198
SHEET 1 AC5 2 GLN I 243 PRO I 247 0
SHEET 2 AC5 2 PHE I 252 ASP I 256 -1 O LYS I 255 N GLY I 244
SHEET 1 AC6 5 VAL J 227 GLN J 231 0
SHEET 2 AC6 5 ILE J 275 ASP J 279 1 O ASP J 279 N VAL J 230
SHEET 3 AC6 5 TYR J 327 ASN J 333 1 O LEU J 331 N ILE J 278
SHEET 4 AC6 5 ASN J 196 GLY J 201 1 N LEU J 199 O GLY J 330
SHEET 5 AC6 5 SER J 351 ASP J 354 1 O ILE J 353 N ILE J 198
SHEET 1 AC7 2 TYR J 245 PRO J 247 0
SHEET 2 AC7 2 PHE J 252 ARG J 254 -1 O ARG J 253 N ARG J 246
SHEET 1 AC8 5 VAL K 227 GLN K 231 0
SHEET 2 AC8 5 TYR K 274 ASP K 279 1 O ASP K 279 N VAL K 230
SHEET 3 AC8 5 VAL K 326 ASN K 333 1 O ILE K 329 N PHE K 276
SHEET 4 AC8 5 ASN K 196 GLY K 201 1 N LEU K 199 O MET K 332
SHEET 5 AC8 5 SER K 351 ASP K 354 1 O ILE K 353 N GLN K 200
SHEET 1 AC9 2 GLN K 243 PRO K 247 0
SHEET 2 AC9 2 PHE K 252 ASP K 256 -1 O LYS K 255 N GLY K 244
SHEET 1 AD1 5 VAL L 227 GLN L 231 0
SHEET 2 AD1 5 TYR L 274 ASP L 279 1 O ASP L 279 N VAL L 230
SHEET 3 AD1 5 VAL L 326 LEU L 331 1 O ILE L 329 N ILE L 278
SHEET 4 AD1 5 ASN L 196 LEU L 199 1 N LEU L 199 O GLY L 330
SHEET 5 AD1 5 SER L 351 ILE L 353 1 O SER L 351 N ILE L 198
SHEET 1 AD2 2 GLN L 243 PRO L 247 0
SHEET 2 AD2 2 PHE L 252 ASP L 256 -1 O LYS L 255 N GLY L 244
SHEET 1 AD3 3 ASP N 61 ILE N 69 0
SHEET 2 AD3 3 THR N 92 ASN N 100 -1 O PHE N 96 N ASN N 65
SHEET 3 AD3 3 ARG N 75 ILE N 76 -1 N ARG N 75 O THR N 95
SHEET 1 AD4 2 SER N 176 PRO N 178 0
SHEET 2 AD4 2 TYR N 185 PHE N 187 -1 O ARG N 186 N ILE N 177
SHEET 1 AD5 6 ASN N 217 THR N 219 0
SHEET 2 AD5 6 ILE N 245 ARG N 248 -1 O THR N 246 N THR N 219
SHEET 3 AD5 6 ILE N 253 ASP N 257 -1 O LEU N 254 N ILE N 247
SHEET 4 AD5 6 ILE N 297 HIS N 305 1 O LEU N 300 N ASP N 257
SHEET 5 AD5 6 ASP N 320 ASN N 327 1 O GLY N 322 N LEU N 301
SHEET 6 AD5 6 LYS N 311 LYS N 315 -1 N HIS N 312 O LEU N 323
LINK OG1 THR A 208 MG MG A1002 1555 1555 2.14
LINK OG1 THR B 208 MG MG B1002 1555 1555 2.09
LINK OG1 THR C 208 MG MG C1002 1555 1555 2.06
LINK OG1 THR G 208 MG MG G1002 1555 1555 2.14
LINK OG1 THR H 208 MG MG H1002 1555 1555 2.09
LINK OG1 THR I 208 MG MG I1002 1555 1555 2.05
LINK O3G GNP A1001 MG MG A1002 1555 1555 1.96
LINK O1B GNP A1001 MG MG A1002 1555 1555 2.01
LINK O3G GNP B1001 MG MG B1002 1555 1555 2.33
LINK O2B GNP B1001 MG MG B1002 1555 1555 1.97
LINK O2A GNP B1001 MG MG B1002 1555 1555 2.54
LINK O3G GNP C1001 MG MG C1002 1555 1555 2.00
LINK O2B GNP C1001 MG MG C1002 1555 1555 1.96
LINK O2A GNP C1001 MG MG C1002 1555 1555 2.00
LINK O3G GNP G1001 MG MG G1002 1555 1555 1.96
LINK O1B GNP G1001 MG MG G1002 1555 1555 2.01
LINK O3G GNP H1001 MG MG H1002 1555 1555 2.33
LINK O2B GNP H1001 MG MG H1002 1555 1555 1.97
LINK O2A GNP H1001 MG MG H1002 1555 1555 2.54
LINK O3G GNP I1001 MG MG I1002 1555 1555 2.00
LINK O2B GNP I1001 MG MG I1002 1555 1555 1.96
LINK O2A GNP I1001 MG MG I1002 1555 1555 2.00
SITE 1 AC1 19 ASP A 176 PHE A 178 PRO A 203 GLY A 204
SITE 2 AC1 19 GLY A 206 LYS A 207 THR A 208 PHE A 209
SITE 3 AC1 19 ASP A 279 GLU A 280 HIS A 407 SER A 408
SITE 4 AC1 19 CYS A 411 CYS A 412 MG A1002 ASP B 300
SITE 5 AC1 19 LYS B 301 ARG B 348 ARG B 349
SITE 1 AC2 4 THR A 208 ASP A 279 GNP A1001 ARG B 349
SITE 1 AC3 20 ASP B 176 LEU B 177 PHE B 178 PRO B 203
SITE 2 AC3 20 GLY B 204 VAL B 205 GLY B 206 LYS B 207
SITE 3 AC3 20 THR B 208 PHE B 209 GLU B 280 HIS B 407
SITE 4 AC3 20 SER B 408 CYS B 411 CYS B 412 MG B1002
SITE 5 AC3 20 ASP C 300 LYS C 301 ARG C 348 ARG C 349
SITE 1 AC4 3 THR B 208 GNP B1001 ARG C 349
SITE 1 AC5 20 ASP C 176 LEU C 177 PHE C 178 PRO C 202
SITE 2 AC5 20 PRO C 203 GLY C 204 VAL C 205 GLY C 206
SITE 3 AC5 20 LYS C 207 THR C 208 PHE C 209 HIS C 407
SITE 4 AC5 20 SER C 408 CYS C 411 CYS C 412 MG C1002
SITE 5 AC5 20 ASP D 300 LYS D 301 ARG D 348 ARG D 349
SITE 1 AC6 2 THR C 208 GNP C1001
SITE 1 AC7 12 ASP D 176 PHE D 178 PRO D 203 GLY D 204
SITE 2 AC7 12 VAL D 205 GLY D 206 LYS D 207 THR D 208
SITE 3 AC7 12 PHE D 209 HIS D 407 SER D 408 CYS D 411
SITE 1 AC8 12 ASP E 176 LEU E 177 PHE E 178 GLY E 204
SITE 2 AC8 12 VAL E 205 GLY E 206 LYS E 207 PHE E 209
SITE 3 AC8 12 HIS E 407 SER E 408 CYS E 412 ARG F 348
SITE 1 AC9 11 ARG A 348 ASP F 176 PHE F 178 GLY F 206
SITE 2 AC9 11 LYS F 207 THR F 208 PHE F 209 HIS F 407
SITE 3 AC9 11 SER F 408 CYS F 411 CYS F 412
SITE 1 AD1 19 ASP G 176 PHE G 178 PRO G 203 GLY G 204
SITE 2 AD1 19 GLY G 206 LYS G 207 THR G 208 PHE G 209
SITE 3 AD1 19 ASP G 279 GLU G 280 HIS G 407 SER G 408
SITE 4 AD1 19 CYS G 411 CYS G 412 MG G1002 ASP H 300
SITE 5 AD1 19 LYS H 301 ARG H 348 ARG H 349
SITE 1 AD2 4 THR G 208 ASP G 279 GNP G1001 ARG H 349
SITE 1 AD3 20 ASP H 176 LEU H 177 PHE H 178 PRO H 203
SITE 2 AD3 20 GLY H 204 VAL H 205 GLY H 206 LYS H 207
SITE 3 AD3 20 THR H 208 PHE H 209 GLU H 280 HIS H 407
SITE 4 AD3 20 SER H 408 CYS H 411 CYS H 412 MG H1002
SITE 5 AD3 20 ASP I 300 LYS I 301 ARG I 348 ARG I 349
SITE 1 AD4 3 THR H 208 GNP H1001 ARG I 349
SITE 1 AD5 20 ASP I 176 LEU I 177 PHE I 178 PRO I 202
SITE 2 AD5 20 PRO I 203 GLY I 204 VAL I 205 GLY I 206
SITE 3 AD5 20 LYS I 207 THR I 208 PHE I 209 HIS I 407
SITE 4 AD5 20 SER I 408 CYS I 411 CYS I 412 MG I1002
SITE 5 AD5 20 ASP J 300 LYS J 301 ARG J 348 ARG J 349
SITE 1 AD6 2 THR I 208 GNP I1001
SITE 1 AD7 12 ASP J 176 PHE J 178 PRO J 203 GLY J 204
SITE 2 AD7 12 VAL J 205 GLY J 206 LYS J 207 THR J 208
SITE 3 AD7 12 PHE J 209 HIS J 407 SER J 408 CYS J 411
SITE 1 AD8 13 ASP K 176 LEU K 177 PHE K 178 GLY K 204
SITE 2 AD8 13 VAL K 205 GLY K 206 LYS K 207 PHE K 209
SITE 3 AD8 13 HIS K 407 SER K 408 CYS K 412 GLU L 298
SITE 4 AD8 13 ARG L 348
SITE 1 AD9 11 ARG G 348 ASP L 176 PHE L 178 GLY L 206
SITE 2 AD9 11 LYS L 207 THR L 208 PHE L 209 HIS L 407
SITE 3 AD9 11 SER L 408 CYS L 411 CYS L 412
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
