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HEADER BIOSYNTHETIC PROTEIN 14-FEB-23 8G5T
TITLE CRYSTAL STRUCTURE OF APO TNMK2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TNMK2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. CB03234;
SOURCE 3 ORGANISM_TAXID: 1703937;
SOURCE 4 GENE: TNMK2, AMK26_32040;
SOURCE 5 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1916
KEYWDS BIOSYNTHESIS, NATURAL PRODUCT, TIANCIMYCIN, ENEDIYNE, BIOSYNTHETIC
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-C.LIU,C.GUI,B.SHEN
REVDAT 1 18-OCT-23 8G5T 0
JRNL AUTH C.GUI,E.KALKREUTER,Y.-C.LIU,G.LI,B.SHEN
JRNL TITL CONSECUTIVELY-ACTING COFACTORLESS OXYGENASES GUIDE
JRNL TITL 2 ANTHRAQUINONE-FUSED ENEDIYNE BIOSYNTHESIS
JRNL REF NAT.CHEM.BIOL. 2023
JRNL REFN ESSN 1552-4469
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2689: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 197921
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 10149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.6810 - 5.7236 0.99 6513 293 0.1973 0.2144
REMARK 3 2 5.7236 - 4.5483 1.00 6433 397 0.1873 0.2007
REMARK 3 3 4.5483 - 3.9749 1.00 6518 334 0.1863 0.2065
REMARK 3 4 3.9749 - 3.6121 1.00 6500 330 0.2001 0.2004
REMARK 3 5 3.6121 - 3.3536 1.00 6475 366 0.2160 0.2469
REMARK 3 6 3.3536 - 3.1561 1.00 6557 263 0.2111 0.2377
REMARK 3 7 3.1561 - 2.9982 1.00 6514 299 0.2230 0.2716
REMARK 3 8 2.9982 - 2.8678 1.00 6536 338 0.2281 0.2546
REMARK 3 9 2.8678 - 2.7575 1.00 6436 396 0.2251 0.2596
REMARK 3 10 2.7575 - 2.6624 1.00 6429 378 0.2317 0.2777
REMARK 3 11 2.6624 - 2.5792 1.00 6488 354 0.2338 0.2695
REMARK 3 12 2.5792 - 2.5055 1.00 6502 387 0.2261 0.2476
REMARK 3 13 2.5055 - 2.4396 1.00 6374 378 0.2347 0.2730
REMARK 3 14 2.4396 - 2.3801 1.00 6470 414 0.2462 0.2845
REMARK 3 15 2.3801 - 2.3260 1.00 6517 320 0.2411 0.2550
REMARK 3 16 2.3260 - 2.2765 1.00 6439 333 0.2401 0.2732
REMARK 3 17 2.2765 - 2.2310 1.00 6578 316 0.2335 0.2629
REMARK 3 18 2.2310 - 2.1889 1.00 6480 363 0.2549 0.2832
REMARK 3 19 2.1889 - 2.1498 1.00 6398 393 0.2552 0.2737
REMARK 3 20 2.1498 - 2.1134 1.00 6475 386 0.2537 0.2566
REMARK 3 21 2.1134 - 2.0793 1.00 6538 316 0.2470 0.2861
REMARK 3 22 2.0793 - 2.0473 1.00 6485 349 0.2491 0.2936
REMARK 3 23 2.0473 - 2.0172 1.00 6624 268 0.2723 0.3346
REMARK 3 24 2.0172 - 1.9888 0.99 6374 355 0.2725 0.2866
REMARK 3 25 1.9888 - 1.9620 0.97 6258 366 0.2641 0.3105
REMARK 3 26 1.9620 - 1.9365 0.90 5850 310 0.2773 0.3113
REMARK 3 27 1.9365 - 1.9123 0.85 5475 314 0.2870 0.3124
REMARK 3 28 1.9123 - 1.8893 0.81 5184 298 0.2929 0.3191
REMARK 3 29 1.8893 - 1.8673 0.75 4913 247 0.2761 0.3192
REMARK 3 30 1.8673 - 1.8463 0.69 4439 288 0.2947 0.3317
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 15248
REMARK 3 ANGLE : 0.844 20820
REMARK 3 CHIRALITY : 0.048 2272
REMARK 3 PLANARITY : 0.006 2784
REMARK 3 DIHEDRAL : 13.258 9056
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8G5T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1000271012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 197921
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.846
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 30.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 0.1 M
REMARK 280 IMIDAZOLE/HCL, PH 8.0, 20% W/V PEG 1000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 67.06150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.71798
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 118.72467
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 67.06150
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 38.71798
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 118.72467
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 67.06150
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 38.71798
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 118.72467
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.43595
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 237.44933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 77.43595
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 237.44933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 77.43595
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 237.44933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 949 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 955 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 972 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 973 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 974 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 956 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 958 LIES ON A SPECIAL POSITION.
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 THR A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ARG A 5
REMARK 465 HIS A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 489
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ARG B 5
REMARK 465 HIS B 6
REMARK 465 GLU B 7
REMARK 465 VAL B 489
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ALA C 3
REMARK 465 ALA C 4
REMARK 465 ARG C 5
REMARK 465 HIS C 6
REMARK 465 GLU C 7
REMARK 465 VAL C 489
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 ARG D 5
REMARK 465 HIS D 6
REMARK 465 GLU D 7
REMARK 465 VAL D 489
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 HH21 ARG B 146 O HOH B 502 1.21
REMARK 500 HE2 HIS B 318 O HOH B 504 1.26
REMARK 500 H THR D 203 O HOH D 502 1.35
REMARK 500 HH21 ARG B 16 O HOH B 510 1.38
REMARK 500 H GLY A 36 O HOH A 514 1.42
REMARK 500 HH21 ARG B 400 O HOH B 503 1.45
REMARK 500 HH21 ARG C 289 O HOH C 519 1.47
REMARK 500 HH11 ARG C 289 O HOH C 521 1.50
REMARK 500 H PHE C 329 O HOH C 501 1.50
REMARK 500 HH22 ARG A 186 O HOH A 510 1.51
REMARK 500 O ASP C 112 HG SER C 119 1.52
REMARK 500 O ASP D 112 HG SER D 119 1.52
REMARK 500 H GLY B 36 O HOH B 521 1.53
REMARK 500 HE ARG C 64 O HOH C 515 1.53
REMARK 500 HH21 ARG D 289 O HOH D 517 1.53
REMARK 500 OD2 ASP B 222 HE ARG B 428 1.54
REMARK 500 OE2 GLU B 237 H PHE B 376 1.54
REMARK 500 H THR C 203 O HOH C 506 1.54
REMARK 500 HH21 ARG A 289 O HOH A 525 1.55
REMARK 500 HH22 ARG B 186 O HOH B 512 1.55
REMARK 500 OE2 GLU A 237 H PHE A 376 1.56
REMARK 500 OD2 ASP A 222 HE ARG A 428 1.58
REMARK 500 HE ARG C 365 O HOH C 504 1.59
REMARK 500 H SER D 341 O HOH D 508 1.60
REMARK 500 O HOH A 595 O HOH A 717 1.80
REMARK 500 O HIS D 63 O HOH D 501 1.81
REMARK 500 O ALA C 325 O HOH C 501 1.83
REMARK 500 O HOH B 815 O HOH B 822 1.83
REMARK 500 N THR D 203 O HOH D 502 1.83
REMARK 500 O SER D 437 O HOH D 503 1.84
REMARK 500 O ALA C 258 O HOH C 502 1.85
REMARK 500 O HOH B 943 O HOH B 949 1.88
REMARK 500 O ALA A 266 O HOH A 501 1.88
REMARK 500 O HOH A 883 O HOH A 892 1.88
REMARK 500 O HOH A 547 O HOH A 858 1.90
REMARK 500 OE1 GLU A 471 O HOH A 502 1.91
REMARK 500 OD1 ASN C 481 O HOH C 503 1.92
REMARK 500 O HOH A 802 O HOH A 936 1.93
REMARK 500 O HOH B 849 O HOH B 883 1.93
REMARK 500 O PRO B 121 O HOH B 501 1.93
REMARK 500 O HOH C 543 O HOH C 698 1.93
REMARK 500 NH2 ARG B 146 O HOH B 502 1.94
REMARK 500 NH2 ARG B 400 O HOH B 503 1.95
REMARK 500 O ARG A 35 O HOH A 503 1.96
REMARK 500 O HOH B 876 O HOH B 916 1.96
REMARK 500 O ASP A 253 O HOH A 504 1.96
REMARK 500 O PRO D 403 O HOH D 504 1.97
REMARK 500 O HOH A 803 O HOH A 899 1.97
REMARK 500 O HOH C 504 O HOH C 708 1.97
REMARK 500 O HOH A 505 O HOH A 603 1.97
REMARK 500
REMARK 500 THIS ENTRY HAS 137 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 712 O HOH D 628 3655 1.52
REMARK 500 HH22 ARG A 146 OE1 GLU C 364 3655 1.53
REMARK 500 HH22 ARG B 146 OE1 GLU D 364 3655 1.58
REMARK 500 O HOH B 708 O HOH D 681 3655 1.77
REMARK 500 O HOH A 679 O HOH C 651 3655 1.87
REMARK 500 O HOH A 576 O HOH C 687 3655 1.94
REMARK 500 OD1 ASP D 361 O HOH B 502 2545 1.96
REMARK 500 O HOH B 803 O HOH C 622 5445 1.98
REMARK 500 O HOH B 835 O HOH C 699 5445 1.99
REMARK 500 O HOH A 916 O HOH A 916 3555 2.12
REMARK 500 O HOH A 739 O HOH C 533 3655 2.17
REMARK 500 O HOH B 576 O HOH D 529 3655 2.17
REMARK 500 O HOH A 521 O HOH C 666 3655 2.17
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 ARG A 212 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 212 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 212 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 212 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
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 HIS A 63 -62.96 -97.38
REMARK 500 ARG A 64 130.28 104.96
REMARK 500 ASP A 81 -86.49 -91.73
REMARK 500 PHE A 115 12.46 87.85
REMARK 500 SER A 193 -117.40 55.09
REMARK 500 ASP A 211 -84.53 -94.73
REMARK 500 SER A 217 91.16 70.38
REMARK 500 ASP A 277 6.36 59.49
REMARK 500 ASP A 288 -169.28 -101.98
REMARK 500 HIS A 318 -78.97 -99.02
REMARK 500 MET A 333 -76.84 -77.14
REMARK 500 MET A 419 -63.41 -90.46
REMARK 500 ARG A 449 81.55 76.32
REMARK 500 HIS B 63 -63.12 -99.98
REMARK 500 ARG B 64 130.40 103.69
REMARK 500 ASP B 81 -86.71 -91.90
REMARK 500 PHE B 115 12.29 88.74
REMARK 500 SER B 193 -117.30 54.35
REMARK 500 ASP B 211 -86.06 -93.91
REMARK 500 SER B 217 90.46 68.91
REMARK 500 ASP B 277 5.84 58.33
REMARK 500 HIS B 318 -74.21 -103.31
REMARK 500 MET B 333 -72.25 -86.81
REMARK 500 PHE B 334 -167.69 -104.66
REMARK 500 ARG B 449 79.96 78.62
REMARK 500 HIS C 63 -75.03 -87.09
REMARK 500 ARG C 64 135.38 119.08
REMARK 500 ASP C 81 -78.16 -93.75
REMARK 500 PHE C 115 10.90 89.11
REMARK 500 SER C 193 -110.13 50.41
REMARK 500 ASP C 211 -90.73 -83.40
REMARK 500 SER C 217 94.94 68.67
REMARK 500 VAL C 224 108.34 -57.37
REMARK 500 ALA C 283 35.57 -98.60
REMARK 500 LEU C 300 2.77 -66.71
REMARK 500 HIS C 318 -80.09 -106.75
REMARK 500 PHE C 334 -160.88 -109.30
REMARK 500 ARG C 449 78.27 76.99
REMARK 500 ALA C 483 76.16 -106.37
REMARK 500 HIS D 63 -73.79 -87.04
REMARK 500 ARG D 64 134.21 117.61
REMARK 500 ASP D 81 -79.70 -87.35
REMARK 500 GLN D 97 -10.64 -151.03
REMARK 500 PHE D 115 10.49 89.41
REMARK 500 SER D 193 -109.44 47.94
REMARK 500 ASP D 211 -90.37 -84.61
REMARK 500 SER D 217 92.66 69.15
REMARK 500 VAL D 224 107.60 -58.64
REMARK 500 ALA D 283 32.66 -99.08
REMARK 500 LEU D 300 3.28 -66.78
REMARK 500
REMARK 500 THIS ENTRY HAS 55 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 SER C 217 ILE C 218 -148.64
REMARK 500 SER D 217 ILE D 218 -149.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 971 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 972 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 973 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 974 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH A 975 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B 956 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B 957 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B 958 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B 959 DISTANCE = 6.69 ANGSTROMS
DBREF1 8G5T A 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5T A A0A125SA15 1 489
DBREF1 8G5T B 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5T B A0A125SA15 1 489
DBREF1 8G5T C 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5T C A0A125SA15 1 489
DBREF1 8G5T D 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5T D A0A125SA15 1 489
SEQRES 1 A 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 A 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 A 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 A 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 A 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 A 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 A 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 A 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 A 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 A 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 A 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 A 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 A 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 A 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 A 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 A 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 A 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 A 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 A 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 A 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 A 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 A 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 A 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 A 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 A 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 A 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 A 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 A 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 A 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 A 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 A 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 A 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 A 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 A 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 A 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 A 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 A 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 A 489 PRO ALA PRO MET VAL PRO THR VAL
SEQRES 1 B 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 B 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 B 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 B 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 B 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 B 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 B 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 B 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 B 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 B 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 B 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 B 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 B 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 B 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 B 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 B 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 B 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 B 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 B 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 B 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 B 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 B 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 B 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 B 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 B 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 B 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 B 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 B 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 B 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 B 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 B 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 B 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 B 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 B 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 B 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 B 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 B 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 B 489 PRO ALA PRO MET VAL PRO THR VAL
SEQRES 1 C 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 C 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 C 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 C 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 C 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 C 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 C 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 C 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 C 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 C 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 C 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 C 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 C 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 C 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 C 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 C 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 C 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 C 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 C 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 C 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 C 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 C 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 C 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 C 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 C 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 C 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 C 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 C 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 C 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 C 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 C 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 C 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 C 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 C 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 C 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 C 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 C 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 C 489 PRO ALA PRO MET VAL PRO THR VAL
SEQRES 1 D 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 D 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 D 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 D 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 D 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 D 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 D 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 D 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 D 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 D 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 D 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 D 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 D 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 D 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 D 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 D 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 D 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 D 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 D 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 D 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 D 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 D 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 D 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 D 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 D 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 D 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 D 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 D 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 D 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 D 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 D 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 D 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 D 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 D 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 D 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 D 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 D 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 D 489 PRO ALA PRO MET VAL PRO THR VAL
FORMUL 5 HOH *1437(H2 O)
HELIX 1 AA1 LEU A 11 GLN A 19 1 9
HELIX 2 AA2 GLU A 31 ARG A 35 5 5
HELIX 3 AA3 ALA A 67 ARG A 71 5 5
HELIX 4 AA4 ARG A 86 GLY A 96 1 11
HELIX 5 AA5 PRO A 99 GLN A 105 1 7
HELIX 6 AA6 GLU A 129 TRP A 133 5 5
HELIX 7 AA7 ASP A 140 LEU A 160 1 21
HELIX 8 AA8 ILE A 162 ALA A 166 5 5
HELIX 9 AA9 SER A 167 LEU A 182 1 16
HELIX 10 AB1 SER A 193 GLY A 207 1 15
HELIX 11 AB2 ARG A 226 ASP A 231 1 6
HELIX 12 AB3 ASP A 231 ALA A 249 1 19
HELIX 13 AB4 THR A 259 ASP A 275 1 17
HELIX 14 AB5 THR A 290 LEU A 300 1 11
HELIX 15 AB6 ASN A 301 ARG A 304 5 4
HELIX 16 AB7 ASN A 305 HIS A 318 1 14
HELIX 17 AB8 GLU A 323 PHE A 334 1 12
HELIX 18 AB9 GLU A 339 ASP A 353 1 15
HELIX 19 AC1 ASN A 359 HIS A 374 1 16
HELIX 20 AC2 THR A 377 GLY A 383 1 7
HELIX 21 AC3 LYS A 385 TRP A 390 5 6
HELIX 22 AC4 PRO A 422 GLY A 434 1 13
HELIX 23 AC5 ASN A 456 GLY A 470 1 15
HELIX 24 AC6 LEU B 11 GLN B 19 1 9
HELIX 25 AC7 GLU B 31 ARG B 35 5 5
HELIX 26 AC8 ALA B 67 ARG B 71 5 5
HELIX 27 AC9 ARG B 86 GLY B 96 1 11
HELIX 28 AD1 PRO B 99 GLN B 105 1 7
HELIX 29 AD2 GLU B 129 TRP B 133 5 5
HELIX 30 AD3 ASP B 140 LEU B 160 1 21
HELIX 31 AD4 ILE B 162 ALA B 166 5 5
HELIX 32 AD5 SER B 167 LEU B 182 1 16
HELIX 33 AD6 SER B 193 GLY B 207 1 15
HELIX 34 AD7 SER B 220 VAL B 224 5 5
HELIX 35 AD8 ARG B 226 ASP B 231 1 6
HELIX 36 AD9 ASP B 231 ALA B 249 1 19
HELIX 37 AE1 THR B 259 ASP B 275 1 17
HELIX 38 AE2 THR B 290 LEU B 300 1 11
HELIX 39 AE3 ASN B 301 ARG B 304 5 4
HELIX 40 AE4 ASN B 305 HIS B 318 1 14
HELIX 41 AE5 GLU B 323 PHE B 334 1 12
HELIX 42 AE6 GLU B 339 ASP B 353 1 15
HELIX 43 AE7 ASN B 359 HIS B 374 1 16
HELIX 44 AE8 THR B 377 GLY B 383 1 7
HELIX 45 AE9 LYS B 385 TRP B 390 5 6
HELIX 46 AF1 PRO B 422 GLY B 434 1 13
HELIX 47 AF2 ASN B 456 GLY B 470 1 15
HELIX 48 AF3 LEU C 11 ALA C 20 1 10
HELIX 49 AF4 GLU C 31 ARG C 35 5 5
HELIX 50 AF5 ALA C 67 ARG C 71 5 5
HELIX 51 AF6 ARG C 86 LEU C 98 1 13
HELIX 52 AF7 GLU C 101 GLN C 105 1 5
HELIX 53 AF8 GLU C 127 TRP C 133 5 7
HELIX 54 AF9 ASP C 140 LEU C 160 1 21
HELIX 55 AG1 ILE C 162 ALA C 166 5 5
HELIX 56 AG2 SER C 167 LEU C 182 1 16
HELIX 57 AG3 SER C 193 GLY C 207 1 15
HELIX 58 AG4 SER C 220 VAL C 224 5 5
HELIX 59 AG5 TRP C 225 ASP C 231 1 7
HELIX 60 AG6 ASP C 231 ALA C 249 1 19
HELIX 61 AG7 THR C 259 ASP C 275 1 17
HELIX 62 AG8 THR C 290 LEU C 300 1 11
HELIX 63 AG9 ASN C 301 ARG C 304 5 4
HELIX 64 AH1 ASN C 305 HIS C 318 1 14
HELIX 65 AH2 GLU C 323 PHE C 334 1 12
HELIX 66 AH3 GLU C 339 ASP C 353 1 15
HELIX 67 AH4 ASN C 359 HIS C 374 1 16
HELIX 68 AH5 THR C 377 GLY C 383 1 7
HELIX 69 AH6 LYS C 385 TRP C 390 5 6
HELIX 70 AH7 PRO C 422 GLY C 434 1 13
HELIX 71 AH8 ASN C 456 GLY C 470 1 15
HELIX 72 AH9 LEU D 11 ALA D 20 1 10
HELIX 73 AI1 GLU D 31 ARG D 35 5 5
HELIX 74 AI2 ALA D 67 ARG D 71 5 5
HELIX 75 AI3 ARG D 86 GLY D 96 1 11
HELIX 76 AI4 PRO D 99 GLN D 105 1 7
HELIX 77 AI5 GLU D 127 TRP D 133 5 7
HELIX 78 AI6 ASP D 140 LEU D 160 1 21
HELIX 79 AI7 ILE D 162 ALA D 166 5 5
HELIX 80 AI8 SER D 167 LEU D 182 1 16
HELIX 81 AI9 SER D 193 GLY D 207 1 15
HELIX 82 AJ1 SER D 220 VAL D 224 5 5
HELIX 83 AJ2 TRP D 225 ASP D 231 1 7
HELIX 84 AJ3 ASP D 231 ALA D 249 1 19
HELIX 85 AJ4 THR D 259 ASP D 275 1 17
HELIX 86 AJ5 THR D 290 LEU D 300 1 11
HELIX 87 AJ6 ASN D 301 ARG D 304 5 4
HELIX 88 AJ7 ASN D 305 HIS D 318 1 14
HELIX 89 AJ8 GLU D 323 PHE D 334 1 12
HELIX 90 AJ9 GLU D 339 ASP D 353 1 15
HELIX 91 AK1 ASN D 359 HIS D 374 1 16
HELIX 92 AK2 THR D 377 GLY D 383 1 7
HELIX 93 AK3 LYS D 385 TRP D 390 5 6
HELIX 94 AK4 PRO D 422 GLY D 434 1 13
HELIX 95 AK5 ASN D 456 GLY D 470 1 15
SHEET 1 AA110 ARG A 26 PRO A 27 0
SHEET 2 AA110 GLU A 38 PRO A 45 -1 O ALA A 39 N ARG A 26
SHEET 3 AA110 THR A 55 ARG A 62 -1 O LEU A 56 N VAL A 44
SHEET 4 AA110 TYR A 106 PHE A 111 -1 O ALA A 110 N VAL A 61
SHEET 5 AA110 GLY A 73 VAL A 77 1 N VAL A 77 O VAL A 109
SHEET 6 AA110 ILE A 187 TYR A 192 1 O SER A 188 N LEU A 76
SHEET 7 AA110 ALA A 210 ASP A 216 1 O VAL A 214 N TYR A 189
SHEET 8 AA110 ILE A 410 ALA A 415 1 O LEU A 411 N VAL A 213
SHEET 9 AA110 SER A 437 VAL A 442 1 O ARG A 438 N LEU A 412
SHEET 10 AA110 VAL A 477 ARG A 479 1 O VAL A 477 N THR A 441
SHEET 1 AA210 ARG B 26 PRO B 27 0
SHEET 2 AA210 GLU B 38 PRO B 45 -1 O ALA B 39 N ARG B 26
SHEET 3 AA210 THR B 55 ARG B 62 -1 O LEU B 56 N VAL B 44
SHEET 4 AA210 TYR B 106 PHE B 111 -1 O ALA B 110 N VAL B 61
SHEET 5 AA210 GLY B 73 VAL B 77 1 N VAL B 77 O VAL B 109
SHEET 6 AA210 ILE B 187 TYR B 192 1 O SER B 188 N LEU B 76
SHEET 7 AA210 ALA B 210 ASP B 216 1 O VAL B 214 N TYR B 189
SHEET 8 AA210 ILE B 410 ALA B 415 1 O LEU B 411 N VAL B 213
SHEET 9 AA210 SER B 437 VAL B 442 1 O ARG B 438 N LEU B 412
SHEET 10 AA210 VAL B 477 ARG B 479 1 O VAL B 477 N THR B 441
SHEET 1 AA310 ARG C 26 PRO C 27 0
SHEET 2 AA310 GLU C 38 PRO C 45 -1 O ALA C 39 N ARG C 26
SHEET 3 AA310 THR C 55 ARG C 62 -1 O LEU C 56 N VAL C 44
SHEET 4 AA310 TYR C 106 PHE C 111 -1 O ALA C 110 N VAL C 61
SHEET 5 AA310 GLY C 73 VAL C 77 1 N VAL C 77 O VAL C 109
SHEET 6 AA310 ILE C 187 TYR C 192 1 O SER C 188 N LEU C 76
SHEET 7 AA310 ALA C 210 ASP C 216 1 O VAL C 214 N TYR C 189
SHEET 8 AA310 ILE C 410 ALA C 415 1 O VAL C 413 N LEU C 215
SHEET 9 AA310 SER C 437 VAL C 442 1 O ARG C 438 N LEU C 412
SHEET 10 AA310 VAL C 477 ARG C 479 1 O VAL C 477 N THR C 441
SHEET 1 AA410 ARG D 26 PRO D 27 0
SHEET 2 AA410 GLU D 38 PRO D 45 -1 O ALA D 39 N ARG D 26
SHEET 3 AA410 THR D 55 ARG D 62 -1 O LEU D 56 N VAL D 44
SHEET 4 AA410 TYR D 106 PHE D 111 -1 O ALA D 110 N VAL D 61
SHEET 5 AA410 GLY D 73 VAL D 77 1 N VAL D 77 O VAL D 109
SHEET 6 AA410 ILE D 187 TYR D 192 1 O SER D 188 N LEU D 76
SHEET 7 AA410 ALA D 210 ASP D 216 1 O VAL D 214 N TYR D 189
SHEET 8 AA410 ILE D 410 ALA D 415 1 O VAL D 413 N LEU D 215
SHEET 9 AA410 SER D 437 VAL D 442 1 O ARG D 438 N LEU D 412
SHEET 10 AA410 VAL D 477 ARG D 479 1 O VAL D 477 N THR D 441
CISPEP 1 VAL A 224 TRP A 225 0 -18.74
CISPEP 2 PHE A 451 PRO A 452 0 -3.76
CISPEP 3 VAL B 224 TRP B 225 0 -17.75
CISPEP 4 PHE B 451 PRO B 452 0 -4.76
CISPEP 5 VAL C 224 TRP C 225 0 -15.60
CISPEP 6 PHE C 451 PRO C 452 0 -3.70
CISPEP 7 VAL D 224 TRP D 225 0 -14.37
CISPEP 8 PHE D 451 PRO D 452 0 -2.47
CRYST1 134.123 134.123 356.174 90.00 90.00 120.00 H 3 36
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007456 0.004305 0.000000 0.00000
SCALE2 0.000000 0.008609 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002808 0.00000
TER 7343 THR A 488
TER 14686 THR B 488
TER 22028 THR C 488
TER 29370 THR D 488
MASTER 536 0 0 95 40 0 0 616297 4 0 152
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