HEADER HYDROLASE INHIBITOR 24-JUL-14 4U59
TITLE CRYSTAL STRUCTURE OF SALMONELLA ALPHA-2-MACROGLOBULIN REACTED WITH
TITLE 2 METHYLAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-2-MACROGLOBULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 90371;
SOURCE 4 GENE: CY43_13515;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MACROGLOBULIN, THIOESTER, PROTEASE INHIBITOR, METHYLAMINE, HYDROLASE
KEYWDS 2 INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.WONG,A.DESSEN
REVDAT 3 20-DEC-23 4U59 1 REMARK
REVDAT 2 01-OCT-14 4U59 1 JRNL
REVDAT 1 17-SEP-14 4U59 0
JRNL AUTH S.G.WONG,A.DESSEN
JRNL TITL STRUCTURE OF A BACTERIAL ALPHA 2-MACROGLOBULIN REVEALS
JRNL TITL 2 MIMICRY OF EUKARYOTIC INNATE IMMUNITY.
JRNL REF NAT COMMUN V. 5 4917 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25221932
JRNL DOI 10.1038/NCOMMS5917
REMARK 2
REMARK 2 RESOLUTION. 3.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 3.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 38986
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1951
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 50.7390 - 7.4403 1.00 2839 150 0.2233 0.2824
REMARK 3 2 7.4403 - 5.9085 1.00 2707 143 0.2574 0.2776
REMARK 3 3 5.9085 - 5.1624 1.00 2672 140 0.2094 0.2339
REMARK 3 4 5.1624 - 4.6908 1.00 2672 141 0.1854 0.2526
REMARK 3 5 4.6908 - 4.3548 1.00 2636 139 0.1903 0.2321
REMARK 3 6 4.3548 - 4.0981 1.00 2630 138 0.2048 0.2483
REMARK 3 7 4.0981 - 3.8930 1.00 2613 138 0.2353 0.2762
REMARK 3 8 3.8930 - 3.7236 1.00 2644 139 0.2441 0.3170
REMARK 3 9 3.7236 - 3.5803 1.00 2586 136 0.2451 0.2830
REMARK 3 10 3.5803 - 3.4567 1.00 2638 139 0.2461 0.2822
REMARK 3 11 3.4567 - 3.3487 1.00 2608 137 0.2783 0.3821
REMARK 3 12 3.3487 - 3.2530 1.00 2600 136 0.2756 0.3741
REMARK 3 13 3.2530 - 3.1673 1.00 2575 136 0.3068 0.3599
REMARK 3 14 3.1673 - 3.0901 1.00 2615 139 0.3486 0.3993
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 75.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.11
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 : 0.003 12123
REMARK 3 ANGLE : 0.684 16517
REMARK 3 CHIRALITY : 0.028 1865
REMARK 3 PLANARITY : 0.003 2189
REMARK 3 DIHEDRAL : 10.410 4464
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 4U59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202759.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-13
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39003
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.090
REMARK 200 RESOLUTION RANGE LOW (A) : 50.732
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.13500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.13200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.050
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: 4U48
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 4000, 0.1 M SODIUM ACETATE PH
REMARK 280 5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 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 127.48000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 127.48000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.11500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 SER A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 VAL A 12
REMARK 465 PRO A 13
REMARK 465 ARG A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 HIS A 17
REMARK 465 MET A 18
REMARK 465 ASP A 19
REMARK 465 ASN A 20
REMARK 465 ASN A 21
REMARK 465 ASP A 22
REMARK 465 LYS A 23
REMARK 465 THR A 24
REMARK 465 ALA A 25
REMARK 465 PRO A 26
REMARK 465 THR A 27
REMARK 465 THR A 28
REMARK 465 LYS A 29
REMARK 465 SER A 30
REMARK 465 GLU A 31
REMARK 465 ALA A 32
REMARK 465 PRO A 33
REMARK 465 ALA A 34
REMARK 465 VAL A 35
REMARK 465 ALA A 36
REMARK 465 GLN A 37
REMARK 465 PRO A 38
REMARK 465 SER A 39
REMARK 465 PRO A 40
REMARK 465 ALA A 41
REMARK 465 GLN A 42
REMARK 465 ASP A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 GLN A 46
REMARK 465 LEU A 47
REMARK 465 GLN A 48
REMARK 465 LYS A 49
REMARK 465 ARG A 209
REMARK 465 SER A 210
REMARK 465 SER A 211
REMARK 465 LEU A 212
REMARK 465 SER A 213
REMARK 465 ASN A 214
REMARK 465 TRP A 215
REMARK 465 GLU A 216
REMARK 465 SER A 217
REMARK 465 ASP A 218
REMARK 465 ASN A 219
REMARK 465 LEU A 220
REMARK 465 LEU A 221
REMARK 465 LYS A 222
REMARK 465 GLN A 266
REMARK 465 ALA A 267
REMARK 465 GLY A 268
REMARK 465 HIS A 269
REMARK 465 TYR A 270
REMARK 465 ASN A 271
REMARK 465 TYR A 272
REMARK 465 GLN A 736
REMARK 465 ASP A 737
REMARK 465 ASN A 738
REMARK 465 SER A 739
REMARK 465 ASP A 740
REMARK 465 GLY A 741
REMARK 465 SER A 742
REMARK 465 GLY A 743
REMARK 465 ALA A 744
REMARK 465 ALA A 745
REMARK 465 ARG A 746
REMARK 465 PHE A 939
REMARK 465 GLY A 940
REMARK 465 GLY A 941
REMARK 465 ASP A 942
REMARK 465 GLY A 943
REMARK 465 ASP A 944
REMARK 465 ASP A 945
REMARK 465 LEU A 946
REMARK 465 LYS A 947
REMARK 465 ARG A 948
REMARK 465 GLY A 949
REMARK 465 GLY A 950
REMARK 465 LYS A 951
REMARK 465 PRO A 952
REMARK 465 PRO A 953
REMARK 465 VAL A 954
REMARK 465 ASN A 955
REMARK 465 ASP A 1555
REMARK 465 SER A 1556
REMARK 465 SER A 1557
REMARK 465 ALA A 1558
REMARK 465 SER A 1559
REMARK 465 LEU A 1560
REMARK 465 PRO A 1561
REMARK 465 GLU A 1562
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 ALA A 134 H LYS A 136 1.49
REMARK 500 OE2 GLU A 1241 HH TYR A 1278 1.53
REMARK 500 OD2 ASP A 922 H TYR A 924 1.55
REMARK 500 OE2 GLU A 1241 OH TYR A 1278 2.18
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 OE2 GLU A 124 HG SER A 466 2555 1.48
REMARK 500 OG SER A 102 OD2 ASP A 339 2555 2.10
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 58 -169.82 -79.76
REMARK 500 GLN A 87 92.05 -65.47
REMARK 500 SER A 90 -40.81 -178.34
REMARK 500 VAL A 92 -43.13 -136.93
REMARK 500 ALA A 99 -59.86 -131.03
REMARK 500 HIS A 120 86.47 63.05
REMARK 500 ALA A 134 -92.39 -159.46
REMARK 500 VAL A 135 -32.62 46.67
REMARK 500 LYS A 136 -57.28 72.34
REMARK 500 ALA A 137 -173.47 65.50
REMARK 500 ASN A 139 38.27 -92.83
REMARK 500 ASN A 140 44.03 31.99
REMARK 500 THR A 142 139.38 71.35
REMARK 500 LYS A 145 -155.28 -118.03
REMARK 500 ARG A 154 157.13 62.71
REMARK 500 ILE A 173 -40.66 -141.13
REMARK 500 ALA A 174 71.93 52.34
REMARK 500 GLU A 207 -60.27 68.97
REMARK 500 ASP A 225 -157.29 -75.84
REMARK 500 THR A 229 -66.89 -129.80
REMARK 500 ARG A 231 81.08 54.92
REMARK 500 ASP A 250 36.90 -95.33
REMARK 500 LEU A 254 -22.84 -164.16
REMARK 500 MET A 264 -110.91 -84.93
REMARK 500 ASN A 293 6.57 -155.42
REMARK 500 GLU A 303 -81.48 -88.30
REMARK 500 ALA A 307 117.65 65.07
REMARK 500 SER A 309 -150.84 -96.51
REMARK 500 ASP A 318 -61.69 58.90
REMARK 500 ASP A 339 -126.84 -104.10
REMARK 500 ALA A 341 -37.86 67.70
REMARK 500 ALA A 342 86.51 -57.14
REMARK 500 ALA A 343 -89.07 -91.99
REMARK 500 GLU A 350 -100.14 61.56
REMARK 500 PRO A 476 176.07 -58.99
REMARK 500 ARG A 478 17.54 47.22
REMARK 500 ALA A 485 -158.39 -128.81
REMARK 500 LYS A 487 -78.13 60.66
REMARK 500 LEU A 548 -151.53 -112.05
REMARK 500 LEU A 555 -50.89 76.17
REMARK 500 ASP A 556 -71.88 59.80
REMARK 500 GLN A 570 -49.54 -146.74
REMARK 500 GLU A 586 -67.87 -102.13
REMARK 500 SER A 587 28.91 -143.96
REMARK 500 ARG A 590 87.98 58.34
REMARK 500 ASP A 635 72.39 55.42
REMARK 500 ALA A 647 -72.49 -55.82
REMARK 500 LYS A 651 107.42 63.82
REMARK 500 GLU A 709 -87.13 -115.69
REMARK 500 ASN A 758 132.42 70.37
REMARK 500
REMARK 500 THIS ENTRY HAS 101 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4U59 A 19 1644 UNP Q8ZN46 Q8ZN46_SALTY 19 1644
SEQADV 4U59 MET A -2 UNP Q8ZN46 INITIATING METHIONINE
SEQADV 4U59 GLY A -1 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 SER A 0 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 SER A 1 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 HIS A 2 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 HIS A 3 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 HIS A 4 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 HIS A 5 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 HIS A 6 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 HIS A 7 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 SER A 8 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 SER A 9 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 GLY A 10 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 LEU A 11 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 VAL A 12 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 PRO A 13 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 ARG A 14 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 GLY A 15 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 SER A 16 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 HIS A 17 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 MET A 18 UNP Q8ZN46 EXPRESSION TAG
SEQADV 4U59 ALA A 98 UNP Q8ZN46 LYS 98 ENGINEERED MUTATION
SEQADV 4U59 ALA A 99 UNP Q8ZN46 LYS 99 ENGINEERED MUTATION
SEQRES 1 A 1647 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 1647 LEU VAL PRO ARG GLY SER HIS MET ASP ASN ASN ASP LYS
SEQRES 3 A 1647 THR ALA PRO THR THR LYS SER GLU ALA PRO ALA VAL ALA
SEQRES 4 A 1647 GLN PRO SER PRO ALA GLN ASP PRO ALA GLN LEU GLN LYS
SEQRES 5 A 1647 LEU ALA GLN GLN SER GLN GLY LYS ALA LEU THR LEU LEU
SEQRES 6 A 1647 ASP ALA SER GLU ALA GLN LEU ASP GLY ALA ALA THR LEU
SEQRES 7 A 1647 VAL LEU THR PHE SER ILE PRO LEU ASP PRO GLU GLN ASP
SEQRES 8 A 1647 PHE SER ARG VAL VAL HIS VAL VAL ASP ALA ALA SER GLY
SEQRES 9 A 1647 SER VAL ASP GLY ALA TRP GLU LEU ALA PRO ASN LEU LYS
SEQRES 10 A 1647 GLU LEU ARG LEU ARG HIS LEU GLU PRO GLU ARG VAL LEU
SEQRES 11 A 1647 VAL VAL THR VAL ASP PRO ALA VAL LYS ALA LEU ASN ASN
SEQRES 12 A 1647 ALA THR PHE GLY LYS SER TYR GLU LYS THR ILE THR THR
SEQRES 13 A 1647 ARG ASP VAL GLN PRO SER VAL GLY PHE ALA SER ARG GLY
SEQRES 14 A 1647 SER LEU LEU PRO GLY LYS ILE ALA GLU GLY LEU PRO VAL
SEQRES 15 A 1647 MET ALA LEU ASN VAL ASN HIS VAL ASP VAL ASN PHE PHE
SEQRES 16 A 1647 ARG VAL LYS PRO GLY SER LEU ALA SER PHE VAL SER GLN
SEQRES 17 A 1647 TRP GLU TYR ARG SER SER LEU SER ASN TRP GLU SER ASP
SEQRES 18 A 1647 ASN LEU LEU LYS MET ALA ASP LEU VAL TYR THR GLY ARG
SEQRES 19 A 1647 PHE ASP LEU ASN PRO ALA ARG ASN THR ARG GLU LYS LEU
SEQRES 20 A 1647 LEU LEU PRO LEU SER ASP ILE LYS PRO LEU GLN GLN ALA
SEQRES 21 A 1647 GLY VAL TYR VAL ALA VAL MET ASN GLN ALA GLY HIS TYR
SEQRES 22 A 1647 ASN TYR SER ASN ALA ALA THR LEU PHE THR LEU SER ASP
SEQRES 23 A 1647 ILE GLY VAL SER ALA HIS ARG TYR HIS ASN ARG LEU ASP
SEQRES 24 A 1647 ILE PHE THR GLN SER LEU GLU ASN GLY ALA ALA GLN SER
SEQRES 25 A 1647 GLY ILE GLU ILE VAL LEU LEU ASN ASP LYS GLY GLN THR
SEQRES 26 A 1647 LEU ALA GLN ALA THR SER ASP ALA GLN GLY HIS VAL GLN
SEQRES 27 A 1647 LEU GLU ALA ASP LYS ALA ALA ALA LEU LEU LEU ALA ARG
SEQRES 28 A 1647 LYS GLU GLU GLN THR THR LEU LEU ASP LEU THR LEU PRO
SEQRES 29 A 1647 ALA LEU ASP LEU SER GLU PHE ASN VAL ALA GLY ALA PRO
SEQRES 30 A 1647 GLY TYR SER LYS GLN PHE PHE MET PHE GLY PRO ARG ASP
SEQRES 31 A 1647 LEU TYR ARG PRO GLY GLU THR VAL ILE LEU ASN GLY LEU
SEQRES 32 A 1647 LEU ARG ASP SER ASP GLY LYS THR LEU PRO ASP GLN PRO
SEQRES 33 A 1647 VAL LYS LEU GLU VAL VAL LYS PRO ASP GLY GLN VAL MET
SEQRES 34 A 1647 ARG THR VAL VAL SER GLN PRO GLU ASN GLY LEU TYR ARG
SEQRES 35 A 1647 LEU ASN TYR PRO LEU ASP ILE ASN ALA PRO THR GLY LEU
SEQRES 36 A 1647 TRP HIS VAL ARG ALA ASN THR GLY ASP ASN LEU LEU ARG
SEQRES 37 A 1647 SER TRP ASP PHE HIS VAL GLU ASP PHE MET PRO GLU ARG
SEQRES 38 A 1647 MET ALA LEU ASN LEU THR ALA GLN LYS THR PRO LEU ALA
SEQRES 39 A 1647 PRO ALA ASP GLU VAL LYS PHE SER VAL VAL GLY TYR TYR
SEQRES 40 A 1647 LEU TYR GLY ALA PRO ALA ASN GLY ASN THR LEU GLN GLY
SEQRES 41 A 1647 GLN LEU PHE LEU ARG PRO LEU ARG ASP ALA VAL ALA ALA
SEQRES 42 A 1647 LEU PRO GLY PHE GLN PHE GLY ASN ILE ALA GLU GLU ASN
SEQRES 43 A 1647 LEU SER ARG SER LEU ASP GLU VAL GLN LEU THR LEU ASP
SEQRES 44 A 1647 LYS GLY GLY ARG GLY GLU VAL SER ALA ALA SER GLN TRP
SEQRES 45 A 1647 GLN GLU ALA HIS SER PRO LEU GLN VAL ILE LEU GLN ALA
SEQRES 46 A 1647 SER LEU LEU GLU SER GLY GLY ARG PRO VAL THR ARG ARG
SEQRES 47 A 1647 VAL GLU GLN ALA ILE TRP PRO ALA ASP THR LEU PRO GLY
SEQRES 48 A 1647 ILE ARG PRO GLN PHE ALA ALA LYS ALA VAL TYR ASP TYR
SEQRES 49 A 1647 ARG THR ASP THR THR VAL ASN GLN PRO ILE VAL ASP GLU
SEQRES 50 A 1647 ASP SER ASN ALA ALA PHE ASP ILE VAL TYR ALA ASN ALA
SEQRES 51 A 1647 GLN GLY GLU LYS LYS ALA VAL SER GLY LEU GLN VAL ARG
SEQRES 52 A 1647 LEU ILE ARG GLU ARG ARG ASP TYR TYR TRP ASN TRP SER
SEQRES 53 A 1647 GLU SER GLU GLY TRP GLN SER GLN PHE ASP GLN LYS ASP
SEQRES 54 A 1647 LEU VAL GLU GLY GLU GLN THR LEU ASP LEU ASN ALA ASP
SEQRES 55 A 1647 GLU THR GLY LYS VAL SER PHE PRO VAL GLU TRP GLY ALA
SEQRES 56 A 1647 TYR ARG LEU GLU VAL LYS ALA PRO ASN GLU THR VAL SER
SEQRES 57 A 1647 SER VAL ARG PHE TRP ALA GLY TYR SER TRP GLN ASP ASN
SEQRES 58 A 1647 SER ASP GLY SER GLY ALA ALA ARG PRO ASP ARG VAL THR
SEQRES 59 A 1647 LEU LYS LEU ASP LYS ALA ASN TYR ARG PRO GLY ASP THR
SEQRES 60 A 1647 MET LYS LEU HIS ILE ALA ALA PRO VAL ALA GLY LYS GLY
SEQRES 61 A 1647 TYR ALA MET VAL GLU SER SER ASP GLY PRO LEU TRP TRP
SEQRES 62 A 1647 GLN ALA ILE ASP VAL PRO ALA GLN GLY LEU GLU LEU THR
SEQRES 63 A 1647 ILE PRO VAL ASP LYS THR TRP ASN ARG HIS ASP LEU TYR
SEQRES 64 A 1647 LEU SER THR LEU VAL VAL ARG PRO GLY ASP LYS SER ARG
SEQRES 65 A 1647 SER ALA THR PRO LYS ARG ALA VAL GLY LEU LEU HIS LEU
SEQRES 66 A 1647 PRO LEU GLY ASP ASP ASN ARG ARG LEU ASP LEU ALA LEU
SEQRES 67 A 1647 GLU SER PRO ALA LYS MET ARG PRO ASN GLN PRO LEU THR
SEQRES 68 A 1647 VAL ARG VAL LYS ALA SER VAL LYS HIS GLY GLU MET PRO
SEQRES 69 A 1647 LYS GLN ILE ASN VAL LEU VAL SER ALA VAL ASP SER GLY
SEQRES 70 A 1647 VAL LEU ASN ILE THR ASP TYR ALA THR PRO ASP PRO TRP
SEQRES 71 A 1647 GLN ALA PHE PHE GLY GLN LYS ARG TYR GLY ALA ASP ILE
SEQRES 72 A 1647 TYR ASP ILE TYR GLY GLN VAL ILE GLU GLY GLN GLY ARG
SEQRES 73 A 1647 LEU ALA ALA LEU ARG PHE GLY GLY ASP GLY ASP ASP LEU
SEQRES 74 A 1647 LYS ARG GLY GLY LYS PRO PRO VAL ASN HIS VAL ASN ILE
SEQRES 75 A 1647 ILE ALA GLN GLN ALA GLN PRO ILE THR LEU ASN GLU GLN
SEQRES 76 A 1647 GLY GLU GLY VAL VAL THR LEU PRO ILE GLY ASP PHE ASN
SEQRES 77 A 1647 GLY GLU LEU ARG VAL MET ALA GLN ALA TRP THR ALA ASP
SEQRES 78 A 1647 ASP PHE GLY ARG GLY GLU SER LYS VAL VAL VAL ALA ALA
SEQRES 79 A 1647 PRO VAL ILE ALA GLU LEU ASN MET PRO ARG PHE LEU ALA
SEQRES 80 A 1647 GLY GLY ASP VAL SER ARG LEU VAL LEU ASP VAL THR ASN
SEQRES 81 A 1647 LEU THR ASP ARG PRO GLN THR LEU ASN ILE ALA LEU ALA
SEQRES 82 A 1647 ALA SER GLY LEU LEU GLU LEU LEU SER GLN GLN PRO GLN
SEQRES 83 A 1647 PRO VAL ASN LEU ALA PRO GLY VAL ARG THR THR LEU PHE
SEQRES 84 A 1647 VAL PRO VAL ARG ALA LEU GLU GLY PHE GLY GLU GLY GLU
SEQRES 85 A 1647 ILE GLN ALA THR ILE SER GLY LEU ASN LEU PRO GLY GLU
SEQRES 86 A 1647 THR LEU ASP ALA GLN HIS LYS GLN TRP GLN ILE GLY VAL
SEQRES 87 A 1647 ARG PRO ALA TRP PRO ALA GLN THR VAL ASN SER GLY ILE
SEQRES 88 A 1647 ALA LEU ALA PRO GLY GLU SER TRP HIS VAL PRO GLU GLN
SEQRES 89 A 1647 HIS LEU ALA ASN ILE SER PRO ALA THR LEU GLN GLY GLN
SEQRES 90 A 1647 LEU LEU LEU SER GLY LYS PRO PRO LEU ASN LEU ALA ARG
SEQRES 91 A 1647 TYR ILE ARG GLU LEU LYS ALA TYR PRO TYR GLY CYS LEU
SEQRES 92 A 1647 GLU MEQ THR THR SER GLY LEU PHE PRO ALA LEU TYR THR
SEQRES 93 A 1647 ASN ALA ALA GLN LEU GLN SER LEU GLY ILE THR GLY ASP
SEQRES 94 A 1647 SER ASP GLU LYS ARG ARG ALA ALA VAL ASP ILE GLY ILE
SEQRES 95 A 1647 SER ARG ILE LEU GLN MET GLN ARG ASP ASN GLY GLY PHE
SEQRES 96 A 1647 ALA LEU TRP ASP GLU ASN GLY ALA GLU GLU PRO TRP LEU
SEQRES 97 A 1647 THR ALA TYR ALA MET ASP PHE LEU ILE ARG ALA GLY GLU
SEQRES 98 A 1647 GLN GLY TYR SER VAL PRO PRO GLU ALA ILE ASN ARG GLY
SEQRES 99 A 1647 ASN GLU ARG LEU LEU ARG TYR LEU GLN ASP PRO GLY THR
SEQRES 100 A 1647 MET LEU ILE ARG TYR SER ASP ASN THR GLN ALA SER THR
SEQRES 101 A 1647 PHE ALA ALA GLN ALA TYR ALA ALA LEU VAL LEU ALA ARG
SEQRES 102 A 1647 GLN GLN LYS ALA PRO LEU GLY THR LEU ARG GLU ILE TRP
SEQRES 103 A 1647 GLU ARG ARG SER GLN ALA ALA SER GLY LEU PRO LEU MET
SEQRES 104 A 1647 GLN LEU GLY ILE ALA LEU ASN THR MET GLY ASP ALA ARG
SEQRES 105 A 1647 ARG GLY GLU GLU ALA ILE THR LEU ALA LEU ASN THR PRO
SEQRES 106 A 1647 ARG GLN ASP GLU ARG GLN TRP ILE ALA ASP TYR GLY SER
SEQRES 107 A 1647 SER LEU ARG ASP ASN ALA LEU MET LEU SER LEU LEU GLU
SEQRES 108 A 1647 GLU ASN ASN LEU ARG PRO ASP ALA GLN ASN ALA LEU LEU
SEQRES 109 A 1647 SER SER LEU SER GLU GLN ALA PHE GLY GLN ARG TRP LEU
SEQRES 110 A 1647 SER THR GLN GLU ASN ASN ALA LEU PHE LEU ALA ALA HIS
SEQRES 111 A 1647 SER ARG GLN ALA SER ALA GLY ALA TRP GLN VAL GLN THR
SEQRES 112 A 1647 SER LEU GLU ALA GLN PRO LEU SER GLY ASP LYS ALA LEU
SEQRES 113 A 1647 THR ARG ASN LEU ASP ALA ASP GLN LEU ALA ALA LEU GLU
SEQRES 114 A 1647 VAL THR ASN THR GLY SER GLN PRO LEU TRP LEU ARG LEU
SEQRES 115 A 1647 ASP SER SER GLY TYR PRO SER SER ALA PRO GLU PRO ALA
SEQRES 116 A 1647 SER ASN VAL LEU GLN ILE GLU ARG GLN ILE LEU GLY THR
SEQRES 117 A 1647 ASP GLY GLN ARG LYS SER LEU SER SER LEU ARG SER GLY
SEQRES 118 A 1647 GLU LEU VAL LEU VAL TRP LEU THR VAL VAL ALA ASP ARG
SEQRES 119 A 1647 ASN VAL PRO ASP ALA LEU VAL VAL ASP LEU LEU PRO ALA
SEQRES 120 A 1647 GLY LEU GLU LEU GLU ASN GLN ASN LEU ALA ASP SER SER
SEQRES 121 A 1647 ALA SER LEU PRO GLU SER GLY SER GLU VAL GLN ASN LEU
SEQRES 122 A 1647 LEU ASN GLN MET GLN GLN ALA ASP ILE GLN TYR MET GLU
SEQRES 123 A 1647 PHE ARG ASP ASP ARG PHE VAL ALA ALA VAL VAL VAL ASN
SEQRES 124 A 1647 GLU GLY GLN PRO VAL THR LEU VAL TYR LEU ALA ARG ALA
SEQRES 125 A 1647 VAL THR PRO GLY THR TYR GLN LEU ALA GLN PRO GLN VAL
SEQRES 126 A 1647 GLU SER MET TYR ALA PRO GLN TRP ARG ALA THR GLY ALA
SEQRES 127 A 1647 SER GLU GLY LEU LEU ILE VAL THR PRO
MODRES 4U59 MEQ A 1182 GLN MODIFIED RESIDUE
HET MEQ A1182 20
HETNAM MEQ N5-METHYLGLUTAMINE
FORMUL 1 MEQ C6 H12 N2 O3
HELIX 1 AA1 ALA A 51 GLN A 55 5 5
HELIX 2 AA2 SER A 198 TRP A 206 1 9
HELIX 3 AA3 ASP A 846 ASN A 848 5 3
HELIX 4 AA4 SER A 893 ASP A 900 1 8
HELIX 5 AA5 ASP A 905 GLY A 912 1 8
HELIX 6 AA6 PRO A 1139 LEU A 1143 5 5
HELIX 7 AA7 ASN A 1164 LEU A 1172 1 9
HELIX 8 AA8 CYS A 1179 GLY A 1186 1 8
HELIX 9 AA9 GLY A 1186 THR A 1193 1 8
HELIX 10 AB1 ASN A 1194 SER A 1200 1 7
HELIX 11 AB2 ASP A 1208 GLN A 1224 1 17
HELIX 12 AB3 GLU A 1242 GLN A 1259 1 18
HELIX 13 AB4 PRO A 1264 ASP A 1281 1 18
HELIX 14 AB5 PRO A 1282 MET A 1285 5 4
HELIX 15 AB6 ASN A 1292 GLN A 1311 1 20
HELIX 16 AB7 PRO A 1315 GLU A 1324 1 10
HELIX 17 AB8 ARG A 1325 ALA A 1329 5 5
HELIX 18 AB9 SER A 1331 MET A 1345 1 15
HELIX 19 AC1 ASP A 1347 LEU A 1359 1 13
HELIX 20 AC2 SER A 1375 ASN A 1391 1 17
HELIX 21 AC3 ARG A 1393 ALA A 1408 1 16
HELIX 22 AC4 SER A 1415 SER A 1428 1 14
HELIX 23 AC5 ASP A 1458 ALA A 1464 1 7
HELIX 24 AC6 GLY A 1564 GLU A 1566 5 3
HELIX 25 AC7 VAL A 1567 GLN A 1576 1 10
SHEET 1 AA1 4 LEU A 61 LEU A 69 0
SHEET 2 AA1 4 ALA A 72 PHE A 79 -1 O VAL A 76 N SER A 65
SHEET 3 AA1 4 GLU A 115 ARG A 119 -1 O LEU A 116 N LEU A 77
SHEET 4 AA1 4 GLU A 108 LEU A 109 -1 N GLU A 108 O ARG A 117
SHEET 1 AA2 3 VAL A 93 ASP A 97 0
SHEET 2 AA2 3 VAL A 126 VAL A 131 -1 O THR A 130 N HIS A 94
SHEET 3 AA2 3 TYR A 147 THR A 152 -1 O LYS A 149 N VAL A 129
SHEET 1 AA3 2 LEU A 177 ALA A 181 0
SHEET 2 AA3 2 GLU A 242 LEU A 246 -1 O LEU A 244 N VAL A 179
SHEET 1 AA4 3 ASN A 190 ARG A 193 0
SHEET 2 AA4 3 GLY A 258 VAL A 263 -1 O VAL A 263 N ASN A 190
SHEET 3 AA4 3 ALA A 276 LEU A 281 -1 O LEU A 281 N GLY A 258
SHEET 1 AA5 4 HIS A 333 GLU A 337 0
SHEET 2 AA5 4 ARG A 294 SER A 301 -1 N LEU A 295 O LEU A 336
SHEET 3 AA5 4 ILE A 284 ARG A 290 -1 N HIS A 289 O ASP A 296
SHEET 4 AA5 4 ASP A 919 ASP A 922 -1 O TYR A 921 N ALA A 288
SHEET 1 AA6 4 THR A 322 THR A 327 0
SHEET 2 AA6 4 ILE A 311 LEU A 315 -1 N GLU A 312 O ALA A 326
SHEET 3 AA6 4 LEU A 344 LYS A 349 -1 O LEU A 344 N LEU A 315
SHEET 4 AA6 4 GLN A 352 ASP A 357 -1 O THR A 354 N ALA A 347
SHEET 1 AA7 3 GLN A 379 PHE A 383 0
SHEET 2 AA7 3 THR A 394 ARG A 402 -1 O LEU A 400 N PHE A 381
SHEET 3 AA7 3 TYR A 438 PRO A 443 -1 O TYR A 442 N VAL A 395
SHEET 1 AA8 5 LEU A 388 TYR A 389 0
SHEET 2 AA8 5 ARG A 465 VAL A 471 1 O HIS A 470 N TYR A 389
SHEET 3 AA8 5 GLY A 451 ASN A 458 -1 N ALA A 457 O ARG A 465
SHEET 4 AA8 5 VAL A 414 VAL A 419 -1 N VAL A 419 O HIS A 454
SHEET 5 AA8 5 VAL A 425 SER A 431 -1 O MET A 426 N VAL A 418
SHEET 1 AA9 3 MET A 479 THR A 484 0
SHEET 2 AA9 3 VAL A 496 TYR A 504 -1 O SER A 499 N THR A 484
SHEET 3 AA9 3 ALA A 508 PRO A 509 -1 O ALA A 508 N TYR A 504
SHEET 1 AB1 3 MET A 479 THR A 484 0
SHEET 2 AB1 3 VAL A 496 TYR A 504 -1 O SER A 499 N THR A 484
SHEET 3 AB1 3 ARG A 560 ALA A 565 -1 O GLY A 561 N VAL A 500
SHEET 1 AB2 4 ARG A 546 LEU A 553 0
SHEET 2 AB2 4 LEU A 515 PRO A 523 -1 N LEU A 515 O LEU A 553
SHEET 3 AB2 4 LEU A 576 LEU A 584 -1 O GLN A 577 N ARG A 522
SHEET 4 AB2 4 VAL A 592 ILE A 600 -1 O VAL A 596 N LEU A 580
SHEET 1 AB3 3 LEU A 606 PRO A 611 0
SHEET 2 AB3 3 SER A 636 ALA A 645 -1 O ALA A 645 N LEU A 606
SHEET 3 AB3 3 GLY A 702 VAL A 708 -1 O PHE A 706 N ALA A 638
SHEET 1 AB4 2 ALA A 615 TYR A 619 0
SHEET 2 AB4 2 THR A 626 PRO A 630 -1 O VAL A 627 N VAL A 618
SHEET 1 AB5 4 GLN A 679 LEU A 696 0
SHEET 2 AB5 4 VAL A 654 ASN A 671 -1 N ARG A 663 O LEU A 687
SHEET 3 AB5 4 ALA A 712 ALA A 719 -1 O GLU A 716 N ARG A 660
SHEET 4 AB5 4 THR A 723 TRP A 730 -1 O PHE A 729 N TYR A 713
SHEET 1 AB6 3 THR A 751 LEU A 754 0
SHEET 2 AB6 3 THR A 764 ALA A 770 -1 O HIS A 768 N LYS A 753
SHEET 3 AB6 3 LEU A 800 PRO A 805 -1 O LEU A 800 N ILE A 769
SHEET 1 AB7 4 PRO A 787 VAL A 795 0
SHEET 2 AB7 4 GLY A 775 GLU A 782 -1 N ALA A 779 O GLN A 791
SHEET 3 AB7 4 TYR A 816 VAL A 822 -1 O TYR A 816 N GLU A 782
SHEET 4 AB7 4 ARG A 835 HIS A 841 -1 O ALA A 836 N VAL A 821
SHEET 1 AB8 5 LYS A 860 MET A 861 0
SHEET 2 AB8 5 PHE A1000 VAL A1009 1 O VAL A1008 N MET A 861
SHEET 3 AB8 5 GLY A 986 TRP A 995 -1 N LEU A 988 O VAL A1007
SHEET 4 AB8 5 ASN A 885 ASP A 892 -1 N SER A 889 O MET A 991
SHEET 5 AB8 5 ILE A 967 THR A 968 -1 O ILE A 967 N VAL A 886
SHEET 1 AB9 7 ALA A 961 GLN A 963 0
SHEET 2 AB9 7 ASN A 885 ASP A 892 -1 N ALA A 890 O GLN A 962
SHEET 3 AB9 7 GLY A 986 TRP A 995 -1 O MET A 991 N SER A 889
SHEET 4 AB9 7 PHE A1000 VAL A1009 -1 O VAL A1007 N LEU A 988
SHEET 5 AB9 7 ARG A 850 GLU A 856 1 N LEU A 851 O PHE A1000
SHEET 6 AB9 7 GLN A 865 SER A 874 -1 O ARG A 870 N GLU A 856
SHEET 7 AB9 7 GLU A 974 ILE A 981 -1 O VAL A 977 N VAL A 869
SHEET 1 AC1 4 VAL A1013 ASN A1018 0
SHEET 2 AC1 4 VAL A1028 ASN A1037 -1 O VAL A1032 N ASN A1018
SHEET 3 AC1 4 ARG A1072 ALA A1081 -1 O LEU A1075 N LEU A1033
SHEET 4 AC1 4 LEU A1055 LEU A1057 -1 N GLU A1056 O ARG A1080
SHEET 1 AC2 5 VAL A1013 ASN A1018 0
SHEET 2 AC2 5 VAL A1028 ASN A1037 -1 O VAL A1032 N ASN A1018
SHEET 3 AC2 5 GLY A1613 GLN A1616 -1 O THR A1614 N VAL A1028
SHEET 4 AC2 5 LEU A1639 THR A1643 -1 O VAL A1642 N GLY A1613
SHEET 5 AC2 5 LEU A1515 ARG A1516 1 N LEU A1515 O THR A1643
SHEET 1 AC3 5 PHE A1022 ALA A1024 0
SHEET 2 AC3 5 GLN A1107 ARG A1116 1 O GLY A1114 N LEU A1023
SHEET 3 AC3 5 GLY A1086 SER A1095 -1 N GLY A1086 O VAL A1115
SHEET 4 AC3 5 GLN A1043 GLY A1053 -1 N ASN A1046 O SER A1095
SHEET 5 AC3 5 VAL A1065 LEU A1067 -1 O LEU A1067 N GLN A1043
SHEET 1 AC4 4 GLN A1122 LEU A1130 0
SHEET 2 AC4 4 LEU A1475 GLY A1483 -1 O GLY A1483 N GLN A1122
SHEET 3 AC4 4 GLN A1152 SER A1158 -1 N LEU A1156 O ARG A1478
SHEET 4 AC4 4 LEU A1453 ASN A1456 -1 O ARG A1455 N LEU A1155
SHEET 1 AC5 4 SER A1135 HIS A1137 0
SHEET 2 AC5 4 GLU A1466 ASN A1469 -1 O VAL A1467 N TRP A1136
SHEET 3 AC5 4 TRP A1436 THR A1440 -1 N GLN A1439 O THR A1468
SHEET 4 AC5 4 LEU A1447 GLY A1449 -1 O LEU A1447 N VAL A1438
SHEET 1 AC6 4 LEU A1496 LEU A1503 0
SHEET 2 AC6 4 LEU A1520 ALA A1529 -1 O LEU A1522 N LEU A1503
SHEET 3 AC6 4 VAL A1601 ALA A1609 -1 O LEU A1603 N LEU A1525
SHEET 4 AC6 4 LEU A1546 LEU A1548 -1 N GLU A1547 O ARG A1608
SHEET 1 AC7 5 ILE A1579 PHE A1584 0
SHEET 2 AC7 5 ARG A1588 VAL A1595 -1 O ALA A1592 N TYR A1581
SHEET 3 AC7 5 VAL A1533 LEU A1541 -1 N VAL A1533 O VAL A1595
SHEET 4 AC7 5 GLN A1621 SER A1624 -1 O GLN A1621 N VAL A1539
SHEET 5 AC7 5 ARG A1631 THR A1633 -1 O ALA A1632 N VAL A1622
LINK C GLU A1181 N MEQ A1182 1555 1555 1.33
LINK C MEQ A1182 N THR A1183 1555 1555 1.33
CRYST1 254.960 82.230 98.920 90.00 90.00 90.00 P 21 21 2 4
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 0.003922 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012161 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010109 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
