content |
HEADER HYDROLASE 16-NOV-16 5TXC
TITLE ATXE2 ISOPEPTIDASE - APO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATXE2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASTICCACAULIS EXCENTRICUS (STRAIN ATCC 15261 /
SOURCE 3 DSM 4724 / VKM B-1370 / CB 48);
SOURCE 4 ORGANISM_TAXID: 573065;
SOURCE 5 STRAIN: ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48;
SOURCE 6 GENE: ASTEX_2444;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LASSO PEPTIDE, ISOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.CHEKAN,S.K.NAIR
REVDAT 1 21-DEC-16 5TXC 0
JRNL AUTH J.R.CHEKAN,J.D.KOOS,C.ZONG,M.O.MAKSIMOV,J.A.LINK,S.K.NAIR
JRNL TITL STRUCTURE OF THE LASSO PEPTIDE ISOPEPTIDASE IDENTIFIES A
JRNL TITL 2 TOPOLOGY FOR PROCESSING THREADED SUBSTRATES
JRNL REF J.AM.CHEM.SOC. 2016
JRNL REFN ESSN 1520-5126
JRNL DOI 10.1021/JACS.6B10389
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 62464
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3164
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.7263 - 6.8238 0.97 2795 138 0.1517 0.1802
REMARK 3 2 6.8238 - 5.4184 0.99 2713 151 0.1692 0.2045
REMARK 3 3 5.4184 - 4.7341 1.00 2704 142 0.1464 0.1846
REMARK 3 4 4.7341 - 4.3015 1.00 2699 159 0.1433 0.1850
REMARK 3 5 4.3015 - 3.9933 1.00 2707 144 0.1627 0.2116
REMARK 3 6 3.9933 - 3.7580 1.00 2647 163 0.1823 0.2202
REMARK 3 7 3.7580 - 3.5698 1.00 2687 155 0.1939 0.2468
REMARK 3 8 3.5698 - 3.4145 1.00 2657 144 0.1972 0.2333
REMARK 3 9 3.4145 - 3.2830 1.00 2702 145 0.2139 0.2431
REMARK 3 10 3.2830 - 3.1698 1.00 2676 137 0.2210 0.2612
REMARK 3 11 3.1698 - 3.0707 1.00 2662 116 0.2279 0.2624
REMARK 3 12 3.0707 - 2.9829 1.00 2682 147 0.2300 0.2847
REMARK 3 13 2.9829 - 2.9044 1.00 2680 128 0.2349 0.2820
REMARK 3 14 2.9044 - 2.8335 1.00 2639 159 0.2370 0.2771
REMARK 3 15 2.8335 - 2.7691 1.00 2678 125 0.2341 0.2992
REMARK 3 16 2.7691 - 2.7102 1.00 2664 134 0.2347 0.2829
REMARK 3 17 2.7102 - 2.6560 1.00 2628 139 0.2406 0.2947
REMARK 3 18 2.6560 - 2.6059 0.99 2630 143 0.2415 0.3255
REMARK 3 19 2.6059 - 2.5593 0.97 2562 153 0.2480 0.2804
REMARK 3 20 2.5593 - 2.5160 0.92 2430 129 0.2510 0.3375
REMARK 3 21 2.5160 - 2.4754 0.86 2266 125 0.2568 0.2995
REMARK 3 22 2.4754 - 2.4373 0.79 2111 112 0.2766 0.3028
REMARK 3 23 2.4373 - 2.4014 0.63 1681 76 0.2967 0.3694
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.550
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 : 0.008 10576
REMARK 3 ANGLE : 1.076 14426
REMARK 3 CHIRALITY : 0.063 1578
REMARK 3 PLANARITY : 0.007 1906
REMARK 3 DIHEDRAL : 12.620 6376
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 5TXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000224985.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64978
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13800
REMARK 200 FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.74900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.300
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 (%): 53.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG3350, 0.4 M SODIUM CHLORIDE,
REMARK 280 0.1 M BIS-TRIS, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 75.24600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 100.87100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 75.24600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 100.87100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 75.24600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.87100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 75.24600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 100.87100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 927 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 ARG A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ILE A 6
REMARK 465 ARG A 7
REMARK 465 CYS A 8
REMARK 465 PRO A 9
REMARK 465 GLY A 10
REMARK 465 ALA A 11
REMARK 465 ILE A 12
REMARK 465 ARG A 13
REMARK 465 VAL A 14
REMARK 465 GLY A 15
REMARK 465 THR A 16
REMARK 465 LEU A 17
REMARK 465 VAL A 18
REMARK 465 THR A 19
REMARK 465 ALA A 20
REMARK 465 PHE A 21
REMARK 465 GLY A 22
REMARK 465 CYS A 23
REMARK 465 LEU A 24
REMARK 465 PRO A 25
REMARK 465 HIS A 26
REMARK 465 VAL A 27
REMARK 465 ALA A 28
REMARK 465 PHE A 29
REMARK 465 ALA A 30
REMARK 465 ALA A 31
REMARK 465 ALA A 32
REMARK 465 ARG A 33
REMARK 465 LYS A 687
REMARK 465 SER A 688
REMARK 465 PRO A 689
REMARK 465 SER A 690
REMARK 465 PRO A 691
REMARK 465 THR A 692
REMARK 465 PRO A 693
REMARK 465 ALA A 694
REMARK 465 PRO A 695
REMARK 465 GLY A 696
REMARK 465 SER A 697
REMARK 465 ARG A 698
REMARK 465 SER A 699
REMARK 465 HIS A 700
REMARK 465 HIS A 701
REMARK 465 HIS A 702
REMARK 465 HIS A 703
REMARK 465 HIS A 704
REMARK 465 HIS A 705
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 ILE B 6
REMARK 465 ARG B 7
REMARK 465 CYS B 8
REMARK 465 PRO B 9
REMARK 465 GLY B 10
REMARK 465 ALA B 11
REMARK 465 ILE B 12
REMARK 465 ARG B 13
REMARK 465 VAL B 14
REMARK 465 GLY B 15
REMARK 465 THR B 16
REMARK 465 LEU B 17
REMARK 465 VAL B 18
REMARK 465 THR B 19
REMARK 465 ALA B 20
REMARK 465 PHE B 21
REMARK 465 GLY B 22
REMARK 465 CYS B 23
REMARK 465 LEU B 24
REMARK 465 PRO B 25
REMARK 465 HIS B 26
REMARK 465 VAL B 27
REMARK 465 ALA B 28
REMARK 465 PHE B 29
REMARK 465 ALA B 30
REMARK 465 ALA B 31
REMARK 465 ALA B 32
REMARK 465 ARG B 33
REMARK 465 LYS B 687
REMARK 465 SER B 688
REMARK 465 PRO B 689
REMARK 465 SER B 690
REMARK 465 PRO B 691
REMARK 465 THR B 692
REMARK 465 PRO B 693
REMARK 465 ALA B 694
REMARK 465 PRO B 695
REMARK 465 GLY B 696
REMARK 465 SER B 697
REMARK 465 ARG B 698
REMARK 465 SER B 699
REMARK 465 HIS B 700
REMARK 465 HIS B 701
REMARK 465 HIS B 702
REMARK 465 HIS B 703
REMARK 465 HIS B 704
REMARK 465 HIS B 705
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 988 O HOH A 1063 1.92
REMARK 500 N GLN B 131 O HOH B 801 1.98
REMARK 500 O HOH B 973 O HOH B 985 1.99
REMARK 500 O HOH B 827 O HOH B 970 2.01
REMARK 500 O THR A 448 O HOH A 801 2.05
REMARK 500 O HOH B 947 O HOH B 975 2.06
REMARK 500 O HOH B 912 O HOH B 989 2.07
REMARK 500 O LEU B 339 O HOH B 802 2.07
REMARK 500 O GLU B 56 O HOH B 803 2.08
REMARK 500 O HOH A 1098 O HOH A 1109 2.08
REMARK 500 O ARG A 205 NH2 ARG B 652 2.09
REMARK 500 O GLU A 248 O HOH A 802 2.09
REMARK 500 NH1 ARG A 205 O HOH A 803 2.10
REMARK 500 O HOH A 1103 O HOH A 1133 2.13
REMARK 500 O HOH A 954 O HOH A 1083 2.13
REMARK 500 O GLU B 34 O HOH B 804 2.13
REMARK 500 O SER B 228 O HOH B 805 2.13
REMARK 500 O HOH A 910 O HOH B 902 2.13
REMARK 500 O HOH A 908 O HOH A 1129 2.13
REMARK 500 OD1 ASP A 599 O HOH A 804 2.13
REMARK 500 NH1 ARG A 652 O HOH A 805 2.13
REMARK 500 ND2 ASN A 84 O HOH A 806 2.14
REMARK 500 OD1 ASN A 498 O HOH A 807 2.14
REMARK 500 OG1 THR B 267 O HOH B 806 2.16
REMARK 500 OG SER A 55 O HOH A 808 2.16
REMARK 500 NE ARG A 306 O HOH A 809 2.16
REMARK 500 O HOH A 971 O HOH A 1105 2.17
REMARK 500 OD2 ASP A 505 O HOH A 810 2.17
REMARK 500 OE1 GLN A 357 NH2 ARG A 360 2.17
REMARK 500 OD2 ASP B 103 OH TYR B 143 2.18
REMARK 500 OE1 GLU B 200 O HOH B 807 2.18
REMARK 500 O HOH A 839 O HOH A 1107 2.19
REMARK 500 OD1 ASP B 508 O HOH B 808 2.19
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 A 837 O HOH A 1076 6575 1.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 58 C PRO A 59 N 0.118
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 398 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU A 407 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 445 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ALA A 35 125.31 73.96
REMARK 500 SER A 53 55.00 -99.64
REMARK 500 SER A 55 -165.56 -128.89
REMARK 500 SER A 115 -33.40 -147.76
REMARK 500 ALA A 163 -115.90 -85.94
REMARK 500 SER A 164 111.77 72.87
REMARK 500 VAL A 166 -44.51 -140.03
REMARK 500 ASP A 210 -152.16 -154.11
REMARK 500 ALA A 358 -116.26 57.16
REMARK 500 ASP A 424 44.74 -94.46
REMARK 500 ARG A 445 -93.16 -109.60
REMARK 500 SER A 527 -123.34 58.32
REMARK 500 CYS A 552 112.49 126.80
REMARK 500 ALA B 35 102.57 74.60
REMARK 500 SER B 53 53.98 -97.46
REMARK 500 ASN B 82 -141.53 59.82
REMARK 500 LEU B 83 144.33 54.03
REMARK 500 LYS B 159 -10.94 -149.90
REMARK 500 GLU B 161 84.55 54.41
REMARK 500 ALA B 163 -118.91 -92.88
REMARK 500 SER B 164 118.54 75.28
REMARK 500 VAL B 166 -48.82 -137.14
REMARK 500 ASP B 210 -155.79 -153.37
REMARK 500 THR B 312 -73.85 -64.44
REMARK 500 GLN B 357 -67.30 -103.43
REMARK 500 ALA B 358 -106.95 -131.21
REMARK 500 ASP B 424 57.04 -94.63
REMARK 500 SER B 440 -160.33 -128.26
REMARK 500 ARG B 445 -92.83 -111.30
REMARK 500 ASP B 450 71.37 42.18
REMARK 500 SER B 527 -127.44 57.89
REMARK 500 CYS B 552 114.33 134.50
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 GLY A 160 GLU A 161 -132.70
REMARK 500 GLY A 382 GLN A 383 -149.34
REMARK 500 CYS A 551 CYS A 552 127.02
REMARK 500 CYS B 551 CYS B 552 118.36
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 A1172 DISTANCE = 5.84 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TXE RELATED DB: PDB
DBREF 5TXC A 1 695 UNP E8RUP5 E8RUP5_ASTEC 1 695
DBREF 5TXC B 1 695 UNP E8RUP5 E8RUP5_ASTEC 1 695
SEQADV 5TXC GLY A 696 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC SER A 697 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC ARG A 698 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC SER A 699 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS A 700 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS A 701 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS A 702 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS A 703 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS A 704 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS A 705 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC GLY B 696 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC SER B 697 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC ARG B 698 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC SER B 699 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS B 700 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS B 701 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS B 702 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS B 703 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS B 704 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXC HIS B 705 UNP E8RUP5 EXPRESSION TAG
SEQRES 1 A 705 MET ARG SER SER LYS ILE ARG CYS PRO GLY ALA ILE ARG
SEQRES 2 A 705 VAL GLY THR LEU VAL THR ALA PHE GLY CYS LEU PRO HIS
SEQRES 3 A 705 VAL ALA PHE ALA ALA ALA ARG GLU ALA PRO PRO VAL THR
SEQRES 4 A 705 PRO GLU VAL LEU VAL ARG LEU ALA ASP ILE GLY THR MET
SEQRES 5 A 705 SER ALA SER GLU THR THR PRO LEU LEU SER LEU SER PRO
SEQRES 6 A 705 ASP GLY ARG TYR VAL ALA PHE GLN VAL ARG GLN ALA ASP
SEQRES 7 A 705 PRO VAL THR ASN LEU ASN VAL PHE ARG MET VAL VAL LYS
SEQRES 8 A 705 ALA THR ASP GLY ALA THR ASP ALA ILE ASP VAL ASP VAL
SEQRES 9 A 705 GLY GLY GLU TYR LEU PHE TRP THR ILE PRO SER TRP GLY
SEQRES 10 A 705 TYR ALA ARG ASN ALA PRO SER GLY ALA ASN LEU THR ILE
SEQRES 11 A 705 GLN PRO ARG TRP SER PRO SER GLY THR HIS LEU ALA TYR
SEQRES 12 A 705 LEU ARG GLN ASP GLN GLY ARG VAL ARG VAL TRP ARG ALA
SEQRES 13 A 705 SER VAL LYS GLY GLU GLY ALA SER PRO VAL ILE GLU ASP
SEQRES 14 A 705 ALA TYR ASP ILE GLU ASP VAL GLN TRP LEU ASP ASP ASN
SEQRES 15 A 705 THR LEU ILE TYR SER GLY ARG PRO GLY PHE VAL GLU ALA
SEQRES 16 A 705 GLU ALA GLU ILE GLU ARG GLU GLY ARG ARG GLY TRP VAL
SEQRES 17 A 705 TYR ASP GLU ARG PHE HIS PRO LEU THR GLY ALA ARG PRO
SEQRES 18 A 705 ARG VAL LEU GLU PRO ILE SER ILE VAL TYR GLN VAL LEU
SEQRES 19 A 705 ASP LEU LYS THR GLY THR ARG ARG ALA ALA THR PRO THR
SEQRES 20 A 705 GLU VAL ALA ARG LEU ARG GLU LYS PRO ASP PRO LEU ARG
SEQRES 21 A 705 ALA MET VAL GLY ARG THR THR PHE SER VAL SER ARG THR
SEQRES 22 A 705 ASP PRO GLN ASN ILE ASN ALA PRO THR THR LEU VAL ALA
SEQRES 23 A 705 ARG ARG GLY GLU GLY GLU PRO VAL ARG CYS ASP GLU GLU
SEQRES 24 A 705 ALA CYS GLN ASN ILE THR ARG MET TRP GLY ASP GLU THR
SEQRES 25 A 705 ALA ASN VAL LEU TYR PHE LEU ARG ARG GLU GLY TRP ALA
SEQRES 26 A 705 SER ASN GLU MET ALA LEU TYR ARG MET PRO ALA ASP ALA
SEQRES 27 A 705 LEU LYS PRO VAL ARG ILE TRP HIS ALA THR GLY LEU LEU
SEQRES 28 A 705 GLN GLY CYS GLU ARG GLN ALA LYS ARG LEU ILE CYS ALA
SEQRES 29 A 705 GLN GLU SER ALA LEU GLN PRO ARG ARG LEU VAL THR LEU
SEQRES 30 A 705 ASN LEU THR SER GLY GLN MET SER PRO LEU TYR ASP PRO
SEQRES 31 A 705 ASN PRO ASP LEU SER ARG TYR ARG LEU PRO LYS VAL GLU
SEQRES 32 A 705 ARG LEU THR LEU ARG ASN ARG ASN GLY ILE GLU VAL PHE
SEQRES 33 A 705 SER ASP LEU VAL LEU PRO PRO ASP TYR GLN LEU GLY THR
SEQRES 34 A 705 ARG LEU PRO LEU VAL ILE VAL GLN TYR SER SER ARG GLY
SEQRES 35 A 705 PHE LEU ARG GLY GLY THR GLY ASP GLU ASN PRO ILE LEU
SEQRES 36 A 705 PRO LEU ALA THR ALA GLY PHE ALA VAL LEU SER PHE HIS
SEQRES 37 A 705 SER PRO ARG SER GLU ALA SER TYR GLN ARG PHE THR SER
SEQRES 38 A 705 PRO ILE ALA GLN SER LYS ALA GLU TYR SER ASN TRP ARG
SEQRES 39 A 705 ASN ARG TRP ASN ILE LEU HIS THR LEU GLU ASP LEU ILE
SEQRES 40 A 705 ASP ASP LEU ASP ARG ARG GLY VAL ILE ASP PRO ALA ARG
SEQRES 41 A 705 VAL GLY LEU THR GLY LEU SER ASP GLY ALA THR THR VAL
SEQRES 42 A 705 HIS PHE GLY LEU ILE ASN SER HIS ARG PHE ALA ALA ALA
SEQRES 43 A 705 VAL THR SER SER CYS CYS THR ASP SER PHE THR ALA SER
SEQRES 44 A 705 VAL MET ASN GLY PRO ARG ILE SER GLY ALA LEU LYS ALA
SEQRES 45 A 705 TYR GLY ILE GLU THR ASP GLN ALA ASP ASP GLY PRO PHE
SEQRES 46 A 705 TRP ALA ALA THR SER PHE VAL VAL ASN ALA SER ARG LEU
SEQRES 47 A 705 ASP THR PRO LEU LEU ILE GLN SER ALA ASP GLU GLU TYR
SEQRES 48 A 705 LEU GLY ALA LEU PRO GLY PHE THR ALA LEU GLN GLN ALA
SEQRES 49 A 705 ARG LYS PRO VAL GLU LEU ILE ILE TYR PRO ASN GLU HIS
SEQRES 50 A 705 HIS VAL LYS TRP GLN PRO ALA HIS ARG LEU ALA VAL TYR
SEQRES 51 A 705 ASN ARG THR ILE ASP TRP PHE ARG PHE TRP LEU MET ASP
SEQRES 52 A 705 GLN SER ASP PRO ALA PRO ASP LYS ALA ALA GLN TYR ASP
SEQRES 53 A 705 ARG TRP ARG ALA LEU ARG ALA LEU ARG GLN LYS SER PRO
SEQRES 54 A 705 SER PRO THR PRO ALA PRO GLY SER ARG SER HIS HIS HIS
SEQRES 55 A 705 HIS HIS HIS
SEQRES 1 B 705 MET ARG SER SER LYS ILE ARG CYS PRO GLY ALA ILE ARG
SEQRES 2 B 705 VAL GLY THR LEU VAL THR ALA PHE GLY CYS LEU PRO HIS
SEQRES 3 B 705 VAL ALA PHE ALA ALA ALA ARG GLU ALA PRO PRO VAL THR
SEQRES 4 B 705 PRO GLU VAL LEU VAL ARG LEU ALA ASP ILE GLY THR MET
SEQRES 5 B 705 SER ALA SER GLU THR THR PRO LEU LEU SER LEU SER PRO
SEQRES 6 B 705 ASP GLY ARG TYR VAL ALA PHE GLN VAL ARG GLN ALA ASP
SEQRES 7 B 705 PRO VAL THR ASN LEU ASN VAL PHE ARG MET VAL VAL LYS
SEQRES 8 B 705 ALA THR ASP GLY ALA THR ASP ALA ILE ASP VAL ASP VAL
SEQRES 9 B 705 GLY GLY GLU TYR LEU PHE TRP THR ILE PRO SER TRP GLY
SEQRES 10 B 705 TYR ALA ARG ASN ALA PRO SER GLY ALA ASN LEU THR ILE
SEQRES 11 B 705 GLN PRO ARG TRP SER PRO SER GLY THR HIS LEU ALA TYR
SEQRES 12 B 705 LEU ARG GLN ASP GLN GLY ARG VAL ARG VAL TRP ARG ALA
SEQRES 13 B 705 SER VAL LYS GLY GLU GLY ALA SER PRO VAL ILE GLU ASP
SEQRES 14 B 705 ALA TYR ASP ILE GLU ASP VAL GLN TRP LEU ASP ASP ASN
SEQRES 15 B 705 THR LEU ILE TYR SER GLY ARG PRO GLY PHE VAL GLU ALA
SEQRES 16 B 705 GLU ALA GLU ILE GLU ARG GLU GLY ARG ARG GLY TRP VAL
SEQRES 17 B 705 TYR ASP GLU ARG PHE HIS PRO LEU THR GLY ALA ARG PRO
SEQRES 18 B 705 ARG VAL LEU GLU PRO ILE SER ILE VAL TYR GLN VAL LEU
SEQRES 19 B 705 ASP LEU LYS THR GLY THR ARG ARG ALA ALA THR PRO THR
SEQRES 20 B 705 GLU VAL ALA ARG LEU ARG GLU LYS PRO ASP PRO LEU ARG
SEQRES 21 B 705 ALA MET VAL GLY ARG THR THR PHE SER VAL SER ARG THR
SEQRES 22 B 705 ASP PRO GLN ASN ILE ASN ALA PRO THR THR LEU VAL ALA
SEQRES 23 B 705 ARG ARG GLY GLU GLY GLU PRO VAL ARG CYS ASP GLU GLU
SEQRES 24 B 705 ALA CYS GLN ASN ILE THR ARG MET TRP GLY ASP GLU THR
SEQRES 25 B 705 ALA ASN VAL LEU TYR PHE LEU ARG ARG GLU GLY TRP ALA
SEQRES 26 B 705 SER ASN GLU MET ALA LEU TYR ARG MET PRO ALA ASP ALA
SEQRES 27 B 705 LEU LYS PRO VAL ARG ILE TRP HIS ALA THR GLY LEU LEU
SEQRES 28 B 705 GLN GLY CYS GLU ARG GLN ALA LYS ARG LEU ILE CYS ALA
SEQRES 29 B 705 GLN GLU SER ALA LEU GLN PRO ARG ARG LEU VAL THR LEU
SEQRES 30 B 705 ASN LEU THR SER GLY GLN MET SER PRO LEU TYR ASP PRO
SEQRES 31 B 705 ASN PRO ASP LEU SER ARG TYR ARG LEU PRO LYS VAL GLU
SEQRES 32 B 705 ARG LEU THR LEU ARG ASN ARG ASN GLY ILE GLU VAL PHE
SEQRES 33 B 705 SER ASP LEU VAL LEU PRO PRO ASP TYR GLN LEU GLY THR
SEQRES 34 B 705 ARG LEU PRO LEU VAL ILE VAL GLN TYR SER SER ARG GLY
SEQRES 35 B 705 PHE LEU ARG GLY GLY THR GLY ASP GLU ASN PRO ILE LEU
SEQRES 36 B 705 PRO LEU ALA THR ALA GLY PHE ALA VAL LEU SER PHE HIS
SEQRES 37 B 705 SER PRO ARG SER GLU ALA SER TYR GLN ARG PHE THR SER
SEQRES 38 B 705 PRO ILE ALA GLN SER LYS ALA GLU TYR SER ASN TRP ARG
SEQRES 39 B 705 ASN ARG TRP ASN ILE LEU HIS THR LEU GLU ASP LEU ILE
SEQRES 40 B 705 ASP ASP LEU ASP ARG ARG GLY VAL ILE ASP PRO ALA ARG
SEQRES 41 B 705 VAL GLY LEU THR GLY LEU SER ASP GLY ALA THR THR VAL
SEQRES 42 B 705 HIS PHE GLY LEU ILE ASN SER HIS ARG PHE ALA ALA ALA
SEQRES 43 B 705 VAL THR SER SER CYS CYS THR ASP SER PHE THR ALA SER
SEQRES 44 B 705 VAL MET ASN GLY PRO ARG ILE SER GLY ALA LEU LYS ALA
SEQRES 45 B 705 TYR GLY ILE GLU THR ASP GLN ALA ASP ASP GLY PRO PHE
SEQRES 46 B 705 TRP ALA ALA THR SER PHE VAL VAL ASN ALA SER ARG LEU
SEQRES 47 B 705 ASP THR PRO LEU LEU ILE GLN SER ALA ASP GLU GLU TYR
SEQRES 48 B 705 LEU GLY ALA LEU PRO GLY PHE THR ALA LEU GLN GLN ALA
SEQRES 49 B 705 ARG LYS PRO VAL GLU LEU ILE ILE TYR PRO ASN GLU HIS
SEQRES 50 B 705 HIS VAL LYS TRP GLN PRO ALA HIS ARG LEU ALA VAL TYR
SEQRES 51 B 705 ASN ARG THR ILE ASP TRP PHE ARG PHE TRP LEU MET ASP
SEQRES 52 B 705 GLN SER ASP PRO ALA PRO ASP LYS ALA ALA GLN TYR ASP
SEQRES 53 B 705 ARG TRP ARG ALA LEU ARG ALA LEU ARG GLN LYS SER PRO
SEQRES 54 B 705 SER PRO THR PRO ALA PRO GLY SER ARG SER HIS HIS HIS
SEQRES 55 B 705 HIS HIS HIS
FORMUL 3 HOH *565(H2 O)
HELIX 1 AA1 THR A 39 ARG A 45 1 7
HELIX 2 AA2 ARG A 189 GLY A 203 1 15
HELIX 3 AA3 ARG A 204 GLY A 206 5 3
HELIX 4 AA4 HIS A 214 GLY A 218 5 5
HELIX 5 AA5 THR A 245 GLU A 254 1 10
HELIX 6 AA6 GLU A 298 GLN A 302 5 5
HELIX 7 AA7 GLY A 323 SER A 326 5 4
HELIX 8 AA8 ASP A 393 TYR A 397 5 5
HELIX 9 AA9 PRO A 453 ALA A 460 1 8
HELIX 10 AB1 SER A 472 GLN A 477 5 6
HELIX 11 AB2 SER A 481 SER A 491 1 11
HELIX 12 AB3 TRP A 493 ARG A 513 1 21
HELIX 13 AB4 SER A 527 ASN A 539 1 13
HELIX 14 AB5 ASP A 554 SER A 559 1 6
HELIX 15 AB6 ASN A 562 LYS A 571 1 10
HELIX 16 AB7 ALA A 572 GLY A 574 5 3
HELIX 17 AB8 PHE A 585 THR A 589 5 5
HELIX 18 AB9 SER A 590 ALA A 595 1 6
HELIX 19 AC1 SER A 596 LEU A 598 5 3
HELIX 20 AC2 GLU A 609 GLY A 613 5 5
HELIX 21 AC3 ALA A 614 ALA A 624 1 11
HELIX 22 AC4 GLN A 642 ASP A 663 1 22
HELIX 23 AC5 ALA A 668 ASP A 670 5 3
HELIX 24 AC6 LYS A 671 LEU A 684 1 14
HELIX 25 AC7 THR B 39 LEU B 46 1 8
HELIX 26 AC8 ARG B 189 GLY B 203 1 15
HELIX 27 AC9 ARG B 204 GLY B 206 5 3
HELIX 28 AD1 HIS B 214 GLY B 218 5 5
HELIX 29 AD2 THR B 245 GLU B 254 1 10
HELIX 30 AD3 GLU B 298 GLN B 302 5 5
HELIX 31 AD4 GLY B 323 ASN B 327 5 5
HELIX 32 AD5 ASP B 393 TYR B 397 5 5
HELIX 33 AD6 PRO B 453 ALA B 460 1 8
HELIX 34 AD7 SER B 472 GLN B 477 5 6
HELIX 35 AD8 SER B 481 SER B 491 1 11
HELIX 36 AD9 TRP B 493 ARG B 513 1 21
HELIX 37 AE1 SER B 527 SER B 540 1 14
HELIX 38 AE2 ASP B 554 SER B 559 1 6
HELIX 39 AE3 ASN B 562 LYS B 571 1 10
HELIX 40 AE4 ALA B 572 GLY B 574 5 3
HELIX 41 AE5 PHE B 585 THR B 589 5 5
HELIX 42 AE6 SER B 590 ALA B 595 1 6
HELIX 43 AE7 SER B 596 LEU B 598 5 3
HELIX 44 AE8 ASP B 608 LEU B 612 1 5
HELIX 45 AE9 ALA B 614 ALA B 624 1 11
HELIX 46 AF1 GLN B 642 ASP B 663 1 22
HELIX 47 AF2 ALA B 668 ASP B 670 5 3
HELIX 48 AF3 LYS B 671 ARG B 685 1 15
SHEET 1 AA1 3 ASP A 48 ILE A 49 0
SHEET 2 AA1 3 TYR A 69 ASP A 78 -1 O ARG A 75 N ASP A 48
SHEET 3 AA1 3 LEU A 61 LEU A 63 -1 N SER A 62 O ALA A 71
SHEET 1 AA2 4 ASP A 48 ILE A 49 0
SHEET 2 AA2 4 TYR A 69 ASP A 78 -1 O ARG A 75 N ASP A 48
SHEET 3 AA2 4 LEU A 83 ALA A 92 -1 O VAL A 85 N GLN A 76
SHEET 4 AA2 4 ILE A 100 VAL A 104 -1 O VAL A 102 N MET A 88
SHEET 1 AA3 4 ARG A 133 TRP A 134 0
SHEET 2 AA3 4 HIS A 140 ASP A 147 -1 O ALA A 142 N ARG A 133
SHEET 3 AA3 4 ARG A 150 SER A 157 -1 O ARG A 152 N ARG A 145
SHEET 4 AA3 4 PRO A 165 ILE A 167 -1 O VAL A 166 N VAL A 153
SHEET 1 AA4 4 ASP A 175 ASP A 180 0
SHEET 2 AA4 4 THR A 183 GLY A 188 -1 O ILE A 185 N GLN A 177
SHEET 3 AA4 4 VAL A 230 ASP A 235 -1 O LEU A 234 N LEU A 184
SHEET 4 AA4 4 ARG A 241 ALA A 243 -1 O ARG A 242 N VAL A 233
SHEET 1 AA5 9 TRP A 207 VAL A 208 0
SHEET 2 AA5 9 VAL B 628 TYR B 633 -1 O ILE B 632 N TRP A 207
SHEET 3 AA5 9 LEU B 602 ALA B 607 1 N ILE B 604 O ILE B 631
SHEET 4 AA5 9 ALA B 545 THR B 548 1 N THR B 548 O LEU B 603
SHEET 5 AA5 9 ILE B 516 GLY B 525 1 N LEU B 523 O VAL B 547
SHEET 6 AA5 9 LEU B 431 GLN B 437 1 N LEU B 433 O GLY B 522
SHEET 7 AA5 9 ALA B 463 PHE B 467 1 O LEU B 465 N VAL B 436
SHEET 8 AA5 9 GLU B 414 LEU B 421 -1 N ASP B 418 O SER B 466
SHEET 9 AA5 9 LYS B 401 ARG B 408 -1 N LEU B 407 O VAL B 415
SHEET 1 AA6 4 ALA A 261 VAL A 263 0
SHEET 2 AA6 4 THR A 266 SER A 271 -1 O PHE A 268 N ALA A 261
SHEET 3 AA6 4 THR A 283 ARG A 288 -1 O VAL A 285 N SER A 269
SHEET 4 AA6 4 VAL A 294 ARG A 295 -1 O VAL A 294 N ALA A 286
SHEET 1 AA7 4 ILE A 304 ASP A 310 0
SHEET 2 AA7 4 VAL A 315 GLU A 322 -1 O TYR A 317 N TRP A 308
SHEET 3 AA7 4 GLU A 328 PRO A 335 -1 O TYR A 332 N PHE A 318
SHEET 4 AA7 4 VAL A 342 THR A 348 -1 O ALA A 347 N MET A 329
SHEET 1 AA8 4 LEU A 350 GLN A 357 0
SHEET 2 AA8 4 ARG A 360 SER A 367 -1 O ALA A 364 N GLN A 352
SHEET 3 AA8 4 GLN A 370 ASN A 378 -1 O ARG A 373 N GLN A 365
SHEET 4 AA8 4 MET A 384 TYR A 388 -1 O TYR A 388 N LEU A 374
SHEET 1 AA9 9 LYS A 401 ARG A 408 0
SHEET 2 AA9 9 GLU A 414 LEU A 421 -1 O SER A 417 N LEU A 405
SHEET 3 AA9 9 ALA A 463 PHE A 467 -1 O VAL A 464 N VAL A 420
SHEET 4 AA9 9 LEU A 431 GLN A 437 1 N PRO A 432 O ALA A 463
SHEET 5 AA9 9 ILE A 516 GLY A 525 1 O GLY A 522 N LEU A 433
SHEET 6 AA9 9 ALA A 545 THR A 548 1 O VAL A 547 N LEU A 523
SHEET 7 AA9 9 LEU A 602 ALA A 607 1 O LEU A 603 N THR A 548
SHEET 8 AA9 9 VAL A 628 TYR A 633 1 O ILE A 631 N ILE A 604
SHEET 9 AA9 9 TRP B 207 VAL B 208 -1 O TRP B 207 N ILE A 632
SHEET 1 AB1 3 ASP B 48 ILE B 49 0
SHEET 2 AB1 3 TYR B 69 ALA B 77 -1 O ARG B 75 N ASP B 48
SHEET 3 AB1 3 SER B 62 LEU B 63 -1 N SER B 62 O ALA B 71
SHEET 1 AB2 4 ASP B 48 ILE B 49 0
SHEET 2 AB2 4 TYR B 69 ALA B 77 -1 O ARG B 75 N ASP B 48
SHEET 3 AB2 4 ASN B 84 ALA B 92 -1 O VAL B 85 N GLN B 76
SHEET 4 AB2 4 ILE B 100 VAL B 104 -1 O ASP B 103 N MET B 88
SHEET 1 AB3 4 ARG B 133 TRP B 134 0
SHEET 2 AB3 4 HIS B 140 ASP B 147 -1 O ALA B 142 N ARG B 133
SHEET 3 AB3 4 ARG B 150 SER B 157 -1 O ARG B 152 N ARG B 145
SHEET 4 AB3 4 PRO B 165 ILE B 167 -1 O VAL B 166 N VAL B 153
SHEET 1 AB4 4 ASP B 175 ASP B 180 0
SHEET 2 AB4 4 THR B 183 GLY B 188 -1 O ILE B 185 N GLN B 177
SHEET 3 AB4 4 VAL B 230 ASP B 235 -1 O VAL B 230 N GLY B 188
SHEET 4 AB4 4 ARG B 241 ALA B 243 -1 O ARG B 242 N VAL B 233
SHEET 1 AB5 4 ALA B 261 VAL B 263 0
SHEET 2 AB5 4 THR B 266 SER B 271 -1 O PHE B 268 N ALA B 261
SHEET 3 AB5 4 THR B 283 ARG B 288 -1 O ARG B 287 N THR B 267
SHEET 4 AB5 4 PRO B 293 ARG B 295 -1 O VAL B 294 N ALA B 286
SHEET 1 AB6 4 ILE B 304 ASP B 310 0
SHEET 2 AB6 4 VAL B 315 GLU B 322 -1 O LEU B 319 N ARG B 306
SHEET 3 AB6 4 GLU B 328 PRO B 335 -1 O GLU B 328 N GLU B 322
SHEET 4 AB6 4 VAL B 342 ALA B 347 -1 O ALA B 347 N MET B 329
SHEET 1 AB7 4 LEU B 350 ARG B 356 0
SHEET 2 AB7 4 ARG B 360 SER B 367 -1 O ALA B 364 N GLN B 352
SHEET 3 AB7 4 GLN B 370 ASN B 378 -1 O ARG B 373 N GLN B 365
SHEET 4 AB7 4 MET B 384 TYR B 388 -1 O TYR B 388 N LEU B 374
SSBOND 1 CYS A 296 CYS A 301 1555 1555 2.08
SSBOND 2 CYS A 354 CYS A 363 1555 1555 2.07
SSBOND 3 CYS A 551 CYS A 552 1555 1555 2.08
SSBOND 4 CYS B 296 CYS B 301 1555 1555 2.07
SSBOND 5 CYS B 354 CYS B 363 1555 1555 2.05
SSBOND 6 CYS B 551 CYS B 552 1555 1555 2.05
CISPEP 1 GLU A 225 PRO A 226 0 5.11
CISPEP 2 GLU B 225 PRO B 226 0 3.06
CRYST1 150.492 201.742 109.131 90.00 90.00 90.00 C 2 2 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006645 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009163 0.00000
TER 5159 GLN A 686
TER 10318 GLN B 686
MASTER 544 0 0 48 72 0 0 610881 2 12 110
END |