HEADER HYDROLASE 27-JAN-10 3LK6
TITLE BETA-N-HEXOSAMINIDASE N318D MUTANT (YBBD_N318D) FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN YBBD;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ORF1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: BSU01660, YBBD, YZBA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS BACILLUS SUBTILIS, HEXOSAMINIDASE, CELL MEMBRANE, GLYCOSIDASE,
KEYWDS 2 HYDROLASE, LIPOPROTEIN, MEMBRANE, PALMITATE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KRUG
REVDAT 3 06-SEP-23 3LK6 1 REMARK
REVDAT 2 13-OCT-21 3LK6 1 REMARK SEQADV LINK
REVDAT 1 25-MAY-11 3LK6 0
JRNL AUTH M.KRUG,S.FISCHER,K.DIEDERICHS,W.BOOS,C.MAYER
JRNL TITL BETA-N-HEXOSAMINIDASE N318D MUTANT (YBBD_N318D) FROM
JRNL TITL 2 BACILLUS SUBTILIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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) : 2.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 64427
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3261
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 48.9955 - 8.1751 0.94 2645 147 0.1564 0.1752
REMARK 3 2 8.1751 - 6.4936 0.95 2713 152 0.1440 0.1579
REMARK 3 3 6.4936 - 5.6742 0.97 2702 149 0.1374 0.1462
REMARK 3 4 5.6742 - 5.1560 0.96 2711 143 0.1238 0.1564
REMARK 3 5 5.1560 - 4.7868 0.96 2748 143 0.1186 0.1422
REMARK 3 6 4.7868 - 4.5048 0.96 2688 164 0.1126 0.1332
REMARK 3 7 4.5048 - 4.2793 0.95 2665 150 0.1241 0.1654
REMARK 3 8 4.2793 - 4.0931 0.95 2708 139 0.1424 0.1842
REMARK 3 9 4.0931 - 3.9356 0.95 2697 150 0.1542 0.1897
REMARK 3 10 3.9356 - 3.7998 0.95 2694 136 0.1559 0.1885
REMARK 3 11 3.7998 - 3.6811 0.95 2651 143 0.1653 0.2125
REMARK 3 12 3.6811 - 3.5759 0.96 2760 136 0.1691 0.1751
REMARK 3 13 3.5759 - 3.4818 0.95 2675 151 0.1564 0.1890
REMARK 3 14 3.4818 - 3.3968 0.95 2756 146 0.1743 0.1868
REMARK 3 15 3.3968 - 3.3196 0.95 2642 126 0.1821 0.1908
REMARK 3 16 3.3196 - 3.2490 0.96 2740 153 0.2061 0.2434
REMARK 3 17 3.2490 - 3.1840 0.96 2710 126 0.2088 0.2865
REMARK 3 18 3.1840 - 3.1240 0.96 2706 142 0.2364 0.2892
REMARK 3 19 3.1240 - 3.0682 0.96 2763 146 0.2623 0.3166
REMARK 3 20 3.0682 - 3.0162 0.97 2733 147 0.2541 0.3155
REMARK 3 21 3.0162 - 2.9675 0.96 2650 140 0.2501 0.2836
REMARK 3 22 2.9675 - 2.9219 0.95 2718 143 0.2616 0.2667
REMARK 3 23 2.9219 - 2.8800 0.58 1691 89 0.3176 0.4075
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 : 0.33
REMARK 3 B_SOL : 31.67
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.58
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 : 0.006 19470
REMARK 3 ANGLE : 0.961 26234
REMARK 3 CHIRALITY : 0.062 2965
REMARK 3 PLANARITY : 0.004 3394
REMARK 3 DIHEDRAL : 16.036 7413
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN D AND RESID 427:642)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3738 -10.2199 25.9673
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.0839
REMARK 3 T33: 0.0392 T12: -0.0723
REMARK 3 T13: -0.0380 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.0640 L22: 0.3175
REMARK 3 L33: 0.3466 L12: -0.2164
REMARK 3 L13: 0.0348 L23: -0.0487
REMARK 3 S TENSOR
REMARK 3 S11: -0.0496 S12: 0.0144 S13: 0.0157
REMARK 3 S21: -0.0811 S22: 0.0746 S23: 0.0968
REMARK 3 S31: -0.2087 S32: 0.1594 S33: -0.0211
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 31:321 OR RESSEQ
REMARK 3 323:642 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 31:321 OR RESSEQ
REMARK 3 323:642 )
REMARK 3 ATOM PAIRS NUMBER : 4721
REMARK 3 RMSD : 0.019
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 31:321 OR RESSEQ
REMARK 3 323:642 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 31:321 OR RESSEQ
REMARK 3 323:642 )
REMARK 3 ATOM PAIRS NUMBER : 4709
REMARK 3 RMSD : 0.020
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 31:321 OR RESSEQ
REMARK 3 323:642 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 31:321 OR RESSEQ
REMARK 3 323:642 )
REMARK 3 ATOM PAIRS NUMBER : 4721
REMARK 3 RMSD : 0.019
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057377.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI(111)MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64490
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880
REMARK 200 RESOLUTION RANGE LOW (A) : 48.988
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 1.880
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.66
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.740
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: PDB ENTRY 3BMX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.9 AND
REMARK 280 VARYING CONCENTRATIONS OF POLYETHYLENE GLYCOL 1000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 SER A 27
REMARK 465 SER B 27
REMARK 465 ALA B 28
REMARK 465 SER B 29
REMARK 465 LYS B 30
REMARK 465 SER D 27
REMARK 465 ALA D 28
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 PRO A 114 C - N - CA ANGL. DEV. = 12.4 DEGREES
REMARK 500 PRO B 114 C - N - CA ANGL. DEV. = 12.1 DEGREES
REMARK 500 PRO C 114 C - N - CA ANGL. DEV. = 12.5 DEGREES
REMARK 500 PRO D 114 C - N - CA ANGL. DEV. = 11.9 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 LYS A 61 177.28 -54.96
REMARK 500 ASP A 123 54.68 -98.51
REMARK 500 ARG A 131 -41.26 -130.62
REMARK 500 ARG A 148 -43.33 75.47
REMARK 500 ASN A 185 70.26 -161.38
REMARK 500 HIS A 222 46.43 79.27
REMARK 500 PRO A 224 32.67 -99.16
REMARK 500 VAL A 250 -92.38 -112.58
REMARK 500 LEU A 285 -22.25 -151.92
REMARK 500 GLN A 307 -73.02 -89.70
REMARK 500 MET A 348 77.45 47.67
REMARK 500 SER A 404 54.98 -161.43
REMARK 500 ILE A 417 -51.43 -120.31
REMARK 500 ASN A 440 66.56 -159.69
REMARK 500 SER A 493 -0.15 79.64
REMARK 500 VAL A 517 -76.63 -106.14
REMARK 500 ARG A 563 -106.19 -126.62
REMARK 500 PRO A 565 -0.87 -59.81
REMARK 500 LYS B 61 177.45 -55.31
REMARK 500 ASP B 123 54.53 -98.23
REMARK 500 ARG B 131 -40.94 -131.04
REMARK 500 ARG B 148 -44.27 76.70
REMARK 500 ASN B 185 69.11 -161.53
REMARK 500 HIS B 222 47.03 79.98
REMARK 500 PRO B 224 32.77 -99.32
REMARK 500 ASP B 228 36.45 -140.49
REMARK 500 VAL B 250 -92.31 -112.25
REMARK 500 LEU B 285 -22.18 -152.44
REMARK 500 GLN B 307 -73.71 -89.85
REMARK 500 MET B 348 76.76 48.23
REMARK 500 SER B 404 55.65 -161.19
REMARK 500 ILE B 417 -52.06 -120.22
REMARK 500 ASN B 440 67.41 -162.29
REMARK 500 SER B 493 -0.21 79.12
REMARK 500 VAL B 517 -76.13 -106.05
REMARK 500 ASP B 520 50.80 -112.61
REMARK 500 ARG B 563 -107.16 -128.08
REMARK 500 PRO B 565 -0.91 -59.89
REMARK 500 LYS C 61 177.91 -55.02
REMARK 500 ASP C 123 54.68 -98.47
REMARK 500 ARG C 131 -41.15 -131.18
REMARK 500 ARG C 148 -43.38 75.11
REMARK 500 ASN C 185 69.69 -161.57
REMARK 500 HIS C 222 47.46 79.67
REMARK 500 PRO C 224 33.73 -99.09
REMARK 500 ASP C 228 36.27 -140.37
REMARK 500 VAL C 250 -92.17 -112.33
REMARK 500 LEU C 285 -21.62 -152.85
REMARK 500 GLN C 307 -72.85 -90.77
REMARK 500 MET C 348 76.33 48.33
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 647 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 106 OG1
REMARK 620 2 ASP A 107 OD1 106.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 648 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 106 OG1
REMARK 620 2 ASP C 107 OD1 105.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 647 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 106 OG1
REMARK 620 2 ASP D 107 OD1 105.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 644
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 646
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 647
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 644
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 648
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 649
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 650
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 651
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 647
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 644
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 645
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 646
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 648
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 644
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 645
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 646
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 647
DBREF 3LK6 A 27 642 UNP P40406 YBBD_BACSU 27 642
DBREF 3LK6 B 27 642 UNP P40406 YBBD_BACSU 27 642
DBREF 3LK6 C 27 642 UNP P40406 YBBD_BACSU 27 642
DBREF 3LK6 D 27 642 UNP P40406 YBBD_BACSU 27 642
SEQADV 3LK6 ASN A 318 UNP P40406 ASP 318 ENGINEERED MUTATION
SEQADV 3LK6 ASN B 318 UNP P40406 ASP 318 ENGINEERED MUTATION
SEQADV 3LK6 ASN C 318 UNP P40406 ASP 318 ENGINEERED MUTATION
SEQADV 3LK6 ASN D 318 UNP P40406 ASP 318 ENGINEERED MUTATION
SEQRES 1 A 616 SER ALA SER LYS ARG ALA ILE ASP ALA ASN GLN ILE VAL
SEQRES 2 A 616 ASN ARG MET SER LEU ASP GLU LYS LEU GLY GLN MET LEU
SEQRES 3 A 616 MET PRO ASP PHE ARG ASN TRP GLN LYS GLU GLY GLU SER
SEQRES 4 A 616 SER PRO GLN ALA LEU THR LYS MET ASN ASP GLU VAL ALA
SEQRES 5 A 616 SER LEU VAL LYS LYS TYR GLN PHE GLY GLY ILE ILE LEU
SEQRES 6 A 616 PHE ALA GLU ASN VAL LYS THR THR LYS GLN THR VAL GLN
SEQRES 7 A 616 LEU THR ASP ASP TYR GLN LYS ALA SER PRO LYS ILE PRO
SEQRES 8 A 616 LEU MET LEU SER ILE ASP GLN GLU GLY GLY ILE VAL THR
SEQRES 9 A 616 ARG LEU GLY GLU GLY THR ASN PHE PRO GLY ASN MET ALA
SEQRES 10 A 616 LEU GLY ALA ALA ARG SER ARG ILE ASN ALA TYR GLN THR
SEQRES 11 A 616 GLY SER ILE ILE GLY LYS GLU LEU SER ALA LEU GLY ILE
SEQRES 12 A 616 ASN THR ASP PHE SER PRO VAL VAL ASP ILE ASN ASN ASN
SEQRES 13 A 616 PRO ASP ASN PRO VAL ILE GLY VAL ARG SER PHE SER SER
SEQRES 14 A 616 ASN ARG GLU LEU THR SER ARG LEU GLY LEU TYR THR MET
SEQRES 15 A 616 LYS GLY LEU GLN ARG GLN ASP ILE ALA SER ALA LEU LYS
SEQRES 16 A 616 HIS PHE PRO GLY HIS GLY ASP THR ASP VAL ASP SER HIS
SEQRES 17 A 616 TYR GLY LEU PRO LEU VAL SER HIS GLY GLN GLU ARG LEU
SEQRES 18 A 616 ARG GLU VAL GLU LEU TYR PRO PHE GLN LYS ALA ILE ASP
SEQRES 19 A 616 ALA GLY ALA ASP MET VAL MET THR ALA HIS VAL GLN PHE
SEQRES 20 A 616 PRO ALA PHE ASP ASP THR THR TYR LYS SER LYS LEU ASP
SEQRES 21 A 616 GLY SER ASP ILE LEU VAL PRO ALA THR LEU SER LYS LYS
SEQRES 22 A 616 VAL MET THR GLY LEU LEU ARG GLN GLU MET GLY PHE ASN
SEQRES 23 A 616 GLY VAL ILE VAL THR ASN ALA LEU ASN MET LYS ALA ILE
SEQRES 24 A 616 ALA ASP HIS PHE GLY GLN GLU GLU ALA VAL VAL MET ALA
SEQRES 25 A 616 VAL LYS ALA GLY VAL ASP ILE ALA LEU MET PRO ALA SER
SEQRES 26 A 616 VAL THR SER LEU LYS GLU GLU GLN LYS PHE ALA ARG VAL
SEQRES 27 A 616 ILE GLN ALA LEU LYS GLU ALA VAL LYS ASN GLY ASP ILE
SEQRES 28 A 616 PRO GLU GLN GLN ILE ASN ASN SER VAL GLU ARG ILE ILE
SEQRES 29 A 616 SER LEU LYS ILE LYS ARG GLY MET TYR PRO ALA ARG ASN
SEQRES 30 A 616 SER ASP SER THR LYS GLU LYS ILE ALA LYS ALA LYS LYS
SEQRES 31 A 616 ILE VAL GLY SER LYS GLN HIS LEU LYS ALA GLU LYS LYS
SEQRES 32 A 616 LEU ALA GLU LYS ALA VAL THR VAL LEU LYS ASN GLU GLN
SEQRES 33 A 616 HIS THR LEU PRO PHE LYS PRO LYS LYS GLY SER ARG ILE
SEQRES 34 A 616 LEU ILE VAL ALA PRO TYR GLU GLU GLN THR ALA SER ILE
SEQRES 35 A 616 GLU GLN THR ILE HIS ASP LEU ILE LYS ARG LYS LYS ILE
SEQRES 36 A 616 LYS PRO VAL SER LEU SER LYS MET ASN PHE ALA SER GLN
SEQRES 37 A 616 VAL PHE LYS THR GLU HIS GLU LYS GLN VAL LYS GLU ALA
SEQRES 38 A 616 ASP TYR ILE ILE THR GLY SER TYR VAL VAL LYS ASN ASP
SEQRES 39 A 616 PRO VAL VAL ASN ASP GLY VAL ILE ASP ASP THR ILE SER
SEQRES 40 A 616 ASP SER SER LYS TRP ALA THR VAL PHE PRO ARG ALA VAL
SEQRES 41 A 616 MET LYS ALA ALA LEU GLN HIS ASN LYS PRO PHE VAL LEU
SEQRES 42 A 616 MET SER LEU ARG ASN PRO TYR ASP ALA ALA ASN PHE GLU
SEQRES 43 A 616 GLU ALA LYS ALA LEU ILE ALA VAL TYR GLY PHE LYS GLY
SEQRES 44 A 616 TYR ALA ASN GLY ARG TYR LEU GLN PRO ASN ILE PRO ALA
SEQRES 45 A 616 GLY VAL MET ALA ILE PHE GLY GLN ALA LYS PRO LYS GLY
SEQRES 46 A 616 THR LEU PRO VAL ASP ILE PRO SER VAL THR LYS PRO GLY
SEQRES 47 A 616 ASN THR LEU TYR PRO LEU GLY TYR GLY LEU ASN ILE LYS
SEQRES 48 A 616 THR GLY ARG PRO LEU
SEQRES 1 B 616 SER ALA SER LYS ARG ALA ILE ASP ALA ASN GLN ILE VAL
SEQRES 2 B 616 ASN ARG MET SER LEU ASP GLU LYS LEU GLY GLN MET LEU
SEQRES 3 B 616 MET PRO ASP PHE ARG ASN TRP GLN LYS GLU GLY GLU SER
SEQRES 4 B 616 SER PRO GLN ALA LEU THR LYS MET ASN ASP GLU VAL ALA
SEQRES 5 B 616 SER LEU VAL LYS LYS TYR GLN PHE GLY GLY ILE ILE LEU
SEQRES 6 B 616 PHE ALA GLU ASN VAL LYS THR THR LYS GLN THR VAL GLN
SEQRES 7 B 616 LEU THR ASP ASP TYR GLN LYS ALA SER PRO LYS ILE PRO
SEQRES 8 B 616 LEU MET LEU SER ILE ASP GLN GLU GLY GLY ILE VAL THR
SEQRES 9 B 616 ARG LEU GLY GLU GLY THR ASN PHE PRO GLY ASN MET ALA
SEQRES 10 B 616 LEU GLY ALA ALA ARG SER ARG ILE ASN ALA TYR GLN THR
SEQRES 11 B 616 GLY SER ILE ILE GLY LYS GLU LEU SER ALA LEU GLY ILE
SEQRES 12 B 616 ASN THR ASP PHE SER PRO VAL VAL ASP ILE ASN ASN ASN
SEQRES 13 B 616 PRO ASP ASN PRO VAL ILE GLY VAL ARG SER PHE SER SER
SEQRES 14 B 616 ASN ARG GLU LEU THR SER ARG LEU GLY LEU TYR THR MET
SEQRES 15 B 616 LYS GLY LEU GLN ARG GLN ASP ILE ALA SER ALA LEU LYS
SEQRES 16 B 616 HIS PHE PRO GLY HIS GLY ASP THR ASP VAL ASP SER HIS
SEQRES 17 B 616 TYR GLY LEU PRO LEU VAL SER HIS GLY GLN GLU ARG LEU
SEQRES 18 B 616 ARG GLU VAL GLU LEU TYR PRO PHE GLN LYS ALA ILE ASP
SEQRES 19 B 616 ALA GLY ALA ASP MET VAL MET THR ALA HIS VAL GLN PHE
SEQRES 20 B 616 PRO ALA PHE ASP ASP THR THR TYR LYS SER LYS LEU ASP
SEQRES 21 B 616 GLY SER ASP ILE LEU VAL PRO ALA THR LEU SER LYS LYS
SEQRES 22 B 616 VAL MET THR GLY LEU LEU ARG GLN GLU MET GLY PHE ASN
SEQRES 23 B 616 GLY VAL ILE VAL THR ASN ALA LEU ASN MET LYS ALA ILE
SEQRES 24 B 616 ALA ASP HIS PHE GLY GLN GLU GLU ALA VAL VAL MET ALA
SEQRES 25 B 616 VAL LYS ALA GLY VAL ASP ILE ALA LEU MET PRO ALA SER
SEQRES 26 B 616 VAL THR SER LEU LYS GLU GLU GLN LYS PHE ALA ARG VAL
SEQRES 27 B 616 ILE GLN ALA LEU LYS GLU ALA VAL LYS ASN GLY ASP ILE
SEQRES 28 B 616 PRO GLU GLN GLN ILE ASN ASN SER VAL GLU ARG ILE ILE
SEQRES 29 B 616 SER LEU LYS ILE LYS ARG GLY MET TYR PRO ALA ARG ASN
SEQRES 30 B 616 SER ASP SER THR LYS GLU LYS ILE ALA LYS ALA LYS LYS
SEQRES 31 B 616 ILE VAL GLY SER LYS GLN HIS LEU LYS ALA GLU LYS LYS
SEQRES 32 B 616 LEU ALA GLU LYS ALA VAL THR VAL LEU LYS ASN GLU GLN
SEQRES 33 B 616 HIS THR LEU PRO PHE LYS PRO LYS LYS GLY SER ARG ILE
SEQRES 34 B 616 LEU ILE VAL ALA PRO TYR GLU GLU GLN THR ALA SER ILE
SEQRES 35 B 616 GLU GLN THR ILE HIS ASP LEU ILE LYS ARG LYS LYS ILE
SEQRES 36 B 616 LYS PRO VAL SER LEU SER LYS MET ASN PHE ALA SER GLN
SEQRES 37 B 616 VAL PHE LYS THR GLU HIS GLU LYS GLN VAL LYS GLU ALA
SEQRES 38 B 616 ASP TYR ILE ILE THR GLY SER TYR VAL VAL LYS ASN ASP
SEQRES 39 B 616 PRO VAL VAL ASN ASP GLY VAL ILE ASP ASP THR ILE SER
SEQRES 40 B 616 ASP SER SER LYS TRP ALA THR VAL PHE PRO ARG ALA VAL
SEQRES 41 B 616 MET LYS ALA ALA LEU GLN HIS ASN LYS PRO PHE VAL LEU
SEQRES 42 B 616 MET SER LEU ARG ASN PRO TYR ASP ALA ALA ASN PHE GLU
SEQRES 43 B 616 GLU ALA LYS ALA LEU ILE ALA VAL TYR GLY PHE LYS GLY
SEQRES 44 B 616 TYR ALA ASN GLY ARG TYR LEU GLN PRO ASN ILE PRO ALA
SEQRES 45 B 616 GLY VAL MET ALA ILE PHE GLY GLN ALA LYS PRO LYS GLY
SEQRES 46 B 616 THR LEU PRO VAL ASP ILE PRO SER VAL THR LYS PRO GLY
SEQRES 47 B 616 ASN THR LEU TYR PRO LEU GLY TYR GLY LEU ASN ILE LYS
SEQRES 48 B 616 THR GLY ARG PRO LEU
SEQRES 1 C 616 SER ALA SER LYS ARG ALA ILE ASP ALA ASN GLN ILE VAL
SEQRES 2 C 616 ASN ARG MET SER LEU ASP GLU LYS LEU GLY GLN MET LEU
SEQRES 3 C 616 MET PRO ASP PHE ARG ASN TRP GLN LYS GLU GLY GLU SER
SEQRES 4 C 616 SER PRO GLN ALA LEU THR LYS MET ASN ASP GLU VAL ALA
SEQRES 5 C 616 SER LEU VAL LYS LYS TYR GLN PHE GLY GLY ILE ILE LEU
SEQRES 6 C 616 PHE ALA GLU ASN VAL LYS THR THR LYS GLN THR VAL GLN
SEQRES 7 C 616 LEU THR ASP ASP TYR GLN LYS ALA SER PRO LYS ILE PRO
SEQRES 8 C 616 LEU MET LEU SER ILE ASP GLN GLU GLY GLY ILE VAL THR
SEQRES 9 C 616 ARG LEU GLY GLU GLY THR ASN PHE PRO GLY ASN MET ALA
SEQRES 10 C 616 LEU GLY ALA ALA ARG SER ARG ILE ASN ALA TYR GLN THR
SEQRES 11 C 616 GLY SER ILE ILE GLY LYS GLU LEU SER ALA LEU GLY ILE
SEQRES 12 C 616 ASN THR ASP PHE SER PRO VAL VAL ASP ILE ASN ASN ASN
SEQRES 13 C 616 PRO ASP ASN PRO VAL ILE GLY VAL ARG SER PHE SER SER
SEQRES 14 C 616 ASN ARG GLU LEU THR SER ARG LEU GLY LEU TYR THR MET
SEQRES 15 C 616 LYS GLY LEU GLN ARG GLN ASP ILE ALA SER ALA LEU LYS
SEQRES 16 C 616 HIS PHE PRO GLY HIS GLY ASP THR ASP VAL ASP SER HIS
SEQRES 17 C 616 TYR GLY LEU PRO LEU VAL SER HIS GLY GLN GLU ARG LEU
SEQRES 18 C 616 ARG GLU VAL GLU LEU TYR PRO PHE GLN LYS ALA ILE ASP
SEQRES 19 C 616 ALA GLY ALA ASP MET VAL MET THR ALA HIS VAL GLN PHE
SEQRES 20 C 616 PRO ALA PHE ASP ASP THR THR TYR LYS SER LYS LEU ASP
SEQRES 21 C 616 GLY SER ASP ILE LEU VAL PRO ALA THR LEU SER LYS LYS
SEQRES 22 C 616 VAL MET THR GLY LEU LEU ARG GLN GLU MET GLY PHE ASN
SEQRES 23 C 616 GLY VAL ILE VAL THR ASN ALA LEU ASN MET LYS ALA ILE
SEQRES 24 C 616 ALA ASP HIS PHE GLY GLN GLU GLU ALA VAL VAL MET ALA
SEQRES 25 C 616 VAL LYS ALA GLY VAL ASP ILE ALA LEU MET PRO ALA SER
SEQRES 26 C 616 VAL THR SER LEU LYS GLU GLU GLN LYS PHE ALA ARG VAL
SEQRES 27 C 616 ILE GLN ALA LEU LYS GLU ALA VAL LYS ASN GLY ASP ILE
SEQRES 28 C 616 PRO GLU GLN GLN ILE ASN ASN SER VAL GLU ARG ILE ILE
SEQRES 29 C 616 SER LEU LYS ILE LYS ARG GLY MET TYR PRO ALA ARG ASN
SEQRES 30 C 616 SER ASP SER THR LYS GLU LYS ILE ALA LYS ALA LYS LYS
SEQRES 31 C 616 ILE VAL GLY SER LYS GLN HIS LEU LYS ALA GLU LYS LYS
SEQRES 32 C 616 LEU ALA GLU LYS ALA VAL THR VAL LEU LYS ASN GLU GLN
SEQRES 33 C 616 HIS THR LEU PRO PHE LYS PRO LYS LYS GLY SER ARG ILE
SEQRES 34 C 616 LEU ILE VAL ALA PRO TYR GLU GLU GLN THR ALA SER ILE
SEQRES 35 C 616 GLU GLN THR ILE HIS ASP LEU ILE LYS ARG LYS LYS ILE
SEQRES 36 C 616 LYS PRO VAL SER LEU SER LYS MET ASN PHE ALA SER GLN
SEQRES 37 C 616 VAL PHE LYS THR GLU HIS GLU LYS GLN VAL LYS GLU ALA
SEQRES 38 C 616 ASP TYR ILE ILE THR GLY SER TYR VAL VAL LYS ASN ASP
SEQRES 39 C 616 PRO VAL VAL ASN ASP GLY VAL ILE ASP ASP THR ILE SER
SEQRES 40 C 616 ASP SER SER LYS TRP ALA THR VAL PHE PRO ARG ALA VAL
SEQRES 41 C 616 MET LYS ALA ALA LEU GLN HIS ASN LYS PRO PHE VAL LEU
SEQRES 42 C 616 MET SER LEU ARG ASN PRO TYR ASP ALA ALA ASN PHE GLU
SEQRES 43 C 616 GLU ALA LYS ALA LEU ILE ALA VAL TYR GLY PHE LYS GLY
SEQRES 44 C 616 TYR ALA ASN GLY ARG TYR LEU GLN PRO ASN ILE PRO ALA
SEQRES 45 C 616 GLY VAL MET ALA ILE PHE GLY GLN ALA LYS PRO LYS GLY
SEQRES 46 C 616 THR LEU PRO VAL ASP ILE PRO SER VAL THR LYS PRO GLY
SEQRES 47 C 616 ASN THR LEU TYR PRO LEU GLY TYR GLY LEU ASN ILE LYS
SEQRES 48 C 616 THR GLY ARG PRO LEU
SEQRES 1 D 616 SER ALA SER LYS ARG ALA ILE ASP ALA ASN GLN ILE VAL
SEQRES 2 D 616 ASN ARG MET SER LEU ASP GLU LYS LEU GLY GLN MET LEU
SEQRES 3 D 616 MET PRO ASP PHE ARG ASN TRP GLN LYS GLU GLY GLU SER
SEQRES 4 D 616 SER PRO GLN ALA LEU THR LYS MET ASN ASP GLU VAL ALA
SEQRES 5 D 616 SER LEU VAL LYS LYS TYR GLN PHE GLY GLY ILE ILE LEU
SEQRES 6 D 616 PHE ALA GLU ASN VAL LYS THR THR LYS GLN THR VAL GLN
SEQRES 7 D 616 LEU THR ASP ASP TYR GLN LYS ALA SER PRO LYS ILE PRO
SEQRES 8 D 616 LEU MET LEU SER ILE ASP GLN GLU GLY GLY ILE VAL THR
SEQRES 9 D 616 ARG LEU GLY GLU GLY THR ASN PHE PRO GLY ASN MET ALA
SEQRES 10 D 616 LEU GLY ALA ALA ARG SER ARG ILE ASN ALA TYR GLN THR
SEQRES 11 D 616 GLY SER ILE ILE GLY LYS GLU LEU SER ALA LEU GLY ILE
SEQRES 12 D 616 ASN THR ASP PHE SER PRO VAL VAL ASP ILE ASN ASN ASN
SEQRES 13 D 616 PRO ASP ASN PRO VAL ILE GLY VAL ARG SER PHE SER SER
SEQRES 14 D 616 ASN ARG GLU LEU THR SER ARG LEU GLY LEU TYR THR MET
SEQRES 15 D 616 LYS GLY LEU GLN ARG GLN ASP ILE ALA SER ALA LEU LYS
SEQRES 16 D 616 HIS PHE PRO GLY HIS GLY ASP THR ASP VAL ASP SER HIS
SEQRES 17 D 616 TYR GLY LEU PRO LEU VAL SER HIS GLY GLN GLU ARG LEU
SEQRES 18 D 616 ARG GLU VAL GLU LEU TYR PRO PHE GLN LYS ALA ILE ASP
SEQRES 19 D 616 ALA GLY ALA ASP MET VAL MET THR ALA HIS VAL GLN PHE
SEQRES 20 D 616 PRO ALA PHE ASP ASP THR THR TYR LYS SER LYS LEU ASP
SEQRES 21 D 616 GLY SER ASP ILE LEU VAL PRO ALA THR LEU SER LYS LYS
SEQRES 22 D 616 VAL MET THR GLY LEU LEU ARG GLN GLU MET GLY PHE ASN
SEQRES 23 D 616 GLY VAL ILE VAL THR ASN ALA LEU ASN MET LYS ALA ILE
SEQRES 24 D 616 ALA ASP HIS PHE GLY GLN GLU GLU ALA VAL VAL MET ALA
SEQRES 25 D 616 VAL LYS ALA GLY VAL ASP ILE ALA LEU MET PRO ALA SER
SEQRES 26 D 616 VAL THR SER LEU LYS GLU GLU GLN LYS PHE ALA ARG VAL
SEQRES 27 D 616 ILE GLN ALA LEU LYS GLU ALA VAL LYS ASN GLY ASP ILE
SEQRES 28 D 616 PRO GLU GLN GLN ILE ASN ASN SER VAL GLU ARG ILE ILE
SEQRES 29 D 616 SER LEU LYS ILE LYS ARG GLY MET TYR PRO ALA ARG ASN
SEQRES 30 D 616 SER ASP SER THR LYS GLU LYS ILE ALA LYS ALA LYS LYS
SEQRES 31 D 616 ILE VAL GLY SER LYS GLN HIS LEU LYS ALA GLU LYS LYS
SEQRES 32 D 616 LEU ALA GLU LYS ALA VAL THR VAL LEU LYS ASN GLU GLN
SEQRES 33 D 616 HIS THR LEU PRO PHE LYS PRO LYS LYS GLY SER ARG ILE
SEQRES 34 D 616 LEU ILE VAL ALA PRO TYR GLU GLU GLN THR ALA SER ILE
SEQRES 35 D 616 GLU GLN THR ILE HIS ASP LEU ILE LYS ARG LYS LYS ILE
SEQRES 36 D 616 LYS PRO VAL SER LEU SER LYS MET ASN PHE ALA SER GLN
SEQRES 37 D 616 VAL PHE LYS THR GLU HIS GLU LYS GLN VAL LYS GLU ALA
SEQRES 38 D 616 ASP TYR ILE ILE THR GLY SER TYR VAL VAL LYS ASN ASP
SEQRES 39 D 616 PRO VAL VAL ASN ASP GLY VAL ILE ASP ASP THR ILE SER
SEQRES 40 D 616 ASP SER SER LYS TRP ALA THR VAL PHE PRO ARG ALA VAL
SEQRES 41 D 616 MET LYS ALA ALA LEU GLN HIS ASN LYS PRO PHE VAL LEU
SEQRES 42 D 616 MET SER LEU ARG ASN PRO TYR ASP ALA ALA ASN PHE GLU
SEQRES 43 D 616 GLU ALA LYS ALA LEU ILE ALA VAL TYR GLY PHE LYS GLY
SEQRES 44 D 616 TYR ALA ASN GLY ARG TYR LEU GLN PRO ASN ILE PRO ALA
SEQRES 45 D 616 GLY VAL MET ALA ILE PHE GLY GLN ALA LYS PRO LYS GLY
SEQRES 46 D 616 THR LEU PRO VAL ASP ILE PRO SER VAL THR LYS PRO GLY
SEQRES 47 D 616 ASN THR LEU TYR PRO LEU GLY TYR GLY LEU ASN ILE LYS
SEQRES 48 D 616 THR GLY ARG PRO LEU
HET PEG A 643 15
HET PEG A 644 17
HET PEG A 645 17
HET PEG A 646 17
HET NA A 647 1
HET PEG B 643 17
HET PEG B 644 17
HET PEG B 645 17
HET PEG B 648 17
HET PEG B 649 17
HET PEG B 650 17
HET NA B 651 1
HET PEG C 647 17
HET PEG C 643 17
HET PEG C 644 17
HET PEG C 645 17
HET PEG C 646 17
HET NA C 648 1
HET PEG D 643 17
HET PEG D 644 17
HET PEG D 645 17
HET PEG D 646 17
HET NA D 647 1
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NA SODIUM ION
FORMUL 5 PEG 19(C4 H10 O3)
FORMUL 9 NA 4(NA 1+)
FORMUL 28 HOH *75(H2 O)
HELIX 1 1 ALA A 28 ASN A 40 1 13
HELIX 2 2 SER A 43 GLN A 50 1 8
HELIX 3 3 ASN A 74 GLN A 85 1 12
HELIX 4 4 THR A 98 SER A 113 1 16
HELIX 5 5 GLY A 140 ARG A 148 1 9
HELIX 6 6 SER A 149 GLY A 168 1 20
HELIX 7 7 ILE A 188 SER A 192 5 5
HELIX 8 8 ASN A 196 GLN A 214 1 19
HELIX 9 9 GLY A 225 THR A 229 5 5
HELIX 10 10 GLY A 243 VAL A 250 1 8
HELIX 11 11 GLU A 251 ALA A 261 1 11
HELIX 12 12 PRO A 293 LEU A 296 5 4
HELIX 13 13 SER A 297 THR A 302 1 6
HELIX 14 14 MET A 322 GLY A 330 1 9
HELIX 15 15 GLY A 330 GLY A 342 1 13
HELIX 16 16 GLU A 358 ASN A 374 1 17
HELIX 17 17 PRO A 378 ARG A 396 1 19
HELIX 18 18 SER A 406 LYS A 416 1 11
HELIX 19 19 SER A 420 VAL A 435 1 16
HELIX 20 20 GLN A 442 THR A 444 5 3
HELIX 21 21 TYR A 461 ARG A 478 1 18
HELIX 22 22 LYS A 497 ALA A 507 1 11
HELIX 23 23 ASP A 534 SER A 536 5 3
HELIX 24 24 LYS A 537 HIS A 553 1 17
HELIX 25 25 ASN A 564 PHE A 571 5 8
HELIX 26 26 PRO A 594 PHE A 604 1 11
HELIX 27 27 ARG B 31 ASN B 40 1 10
HELIX 28 28 SER B 43 GLN B 50 1 8
HELIX 29 29 ASN B 74 GLN B 85 1 12
HELIX 30 30 THR B 98 SER B 113 1 16
HELIX 31 31 GLY B 140 ARG B 148 1 9
HELIX 32 32 SER B 149 GLY B 168 1 20
HELIX 33 33 ILE B 188 SER B 192 5 5
HELIX 34 34 ASN B 196 GLN B 214 1 19
HELIX 35 35 GLY B 225 THR B 229 5 5
HELIX 36 36 GLY B 243 VAL B 250 1 8
HELIX 37 37 GLU B 251 ALA B 261 1 11
HELIX 38 38 PRO B 293 LEU B 296 5 4
HELIX 39 39 SER B 297 THR B 302 1 6
HELIX 40 40 MET B 322 GLY B 330 1 9
HELIX 41 41 GLY B 330 GLY B 342 1 13
HELIX 42 42 GLU B 358 ASN B 374 1 17
HELIX 43 43 PRO B 378 ARG B 396 1 19
HELIX 44 44 SER B 406 LYS B 416 1 11
HELIX 45 45 SER B 420 VAL B 435 1 16
HELIX 46 46 GLN B 442 THR B 444 5 3
HELIX 47 47 TYR B 461 ARG B 478 1 18
HELIX 48 48 LYS B 497 ALA B 507 1 11
HELIX 49 49 ASP B 534 SER B 536 5 3
HELIX 50 50 LYS B 537 HIS B 553 1 17
HELIX 51 51 ASN B 564 PHE B 571 5 8
HELIX 52 52 PRO B 594 PHE B 604 1 11
HELIX 53 53 SER C 27 ASN C 40 1 14
HELIX 54 54 SER C 43 GLN C 50 1 8
HELIX 55 55 ASN C 74 GLN C 85 1 12
HELIX 56 56 THR C 98 SER C 113 1 16
HELIX 57 57 GLY C 140 ARG C 148 1 9
HELIX 58 58 SER C 149 GLY C 168 1 20
HELIX 59 59 ILE C 188 SER C 192 5 5
HELIX 60 60 ASN C 196 GLN C 214 1 19
HELIX 61 61 GLY C 225 THR C 229 5 5
HELIX 62 62 GLY C 243 VAL C 250 1 8
HELIX 63 63 GLU C 251 ALA C 261 1 11
HELIX 64 64 PRO C 293 LEU C 296 5 4
HELIX 65 65 SER C 297 THR C 302 1 6
HELIX 66 66 MET C 322 GLY C 330 1 9
HELIX 67 67 GLY C 330 GLY C 342 1 13
HELIX 68 68 GLU C 358 ASN C 374 1 17
HELIX 69 69 PRO C 378 ARG C 396 1 19
HELIX 70 70 SER C 406 LYS C 416 1 11
HELIX 71 71 SER C 420 VAL C 435 1 16
HELIX 72 72 GLN C 442 THR C 444 5 3
HELIX 73 73 TYR C 461 ARG C 478 1 18
HELIX 74 74 LYS C 497 ALA C 507 1 11
HELIX 75 75 ASP C 534 SER C 536 5 3
HELIX 76 76 LYS C 537 HIS C 553 1 17
HELIX 77 77 ASN C 564 PHE C 571 5 8
HELIX 78 78 PRO C 594 PHE C 604 1 11
HELIX 79 79 LYS D 30 ASN D 40 1 11
HELIX 80 80 SER D 43 GLN D 50 1 8
HELIX 81 81 ASN D 74 GLN D 85 1 12
HELIX 82 82 THR D 98 SER D 113 1 16
HELIX 83 83 GLY D 140 ARG D 148 1 9
HELIX 84 84 SER D 149 GLY D 168 1 20
HELIX 85 85 ILE D 188 SER D 192 5 5
HELIX 86 86 ASN D 196 GLN D 214 1 19
HELIX 87 87 GLY D 225 THR D 229 5 5
HELIX 88 88 GLY D 243 VAL D 250 1 8
HELIX 89 89 GLU D 251 ALA D 261 1 11
HELIX 90 90 PRO D 293 LEU D 296 5 4
HELIX 91 91 SER D 297 THR D 302 1 6
HELIX 92 92 MET D 322 GLY D 330 1 9
HELIX 93 93 GLY D 330 GLY D 342 1 13
HELIX 94 94 GLU D 358 ASN D 374 1 17
HELIX 95 95 PRO D 378 ARG D 396 1 19
HELIX 96 96 SER D 406 LYS D 416 1 11
HELIX 97 97 SER D 420 VAL D 435 1 16
HELIX 98 98 GLN D 442 THR D 444 5 3
HELIX 99 99 TYR D 461 ARG D 478 1 18
HELIX 100 100 LYS D 497 ALA D 507 1 11
HELIX 101 101 ASP D 534 SER D 536 5 3
HELIX 102 102 LYS D 537 HIS D 553 1 17
HELIX 103 103 ASN D 564 PHE D 571 5 8
HELIX 104 104 PRO D 594 PHE D 604 1 11
SHEET 1 A 2 LEU A 52 MET A 53 0
SHEET 2 A 2 ALA A 346 LEU A 347 1 O ALA A 346 N MET A 53
SHEET 1 B 2 ASN A 58 TRP A 59 0
SHEET 2 B 2 GLN A 68 ALA A 69 -1 O GLN A 68 N TRP A 59
SHEET 1 C 6 GLY A 88 ILE A 90 0
SHEET 2 C 6 MET A 119 ILE A 122 1 O SER A 121 N ILE A 89
SHEET 3 C 6 THR A 171 ASP A 172 1 O THR A 171 N LEU A 120
SHEET 4 C 6 ALA A 217 PHE A 223 1 O ALA A 217 N ASP A 172
SHEET 5 C 6 MET A 265 THR A 268 1 O MET A 267 N PHE A 223
SHEET 6 C 6 VAL A 314 THR A 317 1 O VAL A 316 N VAL A 266
SHEET 1 D 2 ASP A 230 ASP A 232 0
SHEET 2 D 2 LEU A 237 LEU A 239 -1 O LEU A 237 N ASP A 232
SHEET 1 E 2 THR A 280 LYS A 282 0
SHEET 2 E 2 ASP A 289 LEU A 291 -1 O ILE A 290 N TYR A 281
SHEET 1 F 6 THR A 436 ASN A 440 0
SHEET 2 F 6 ALA A 576 ALA A 579 -1 O LEU A 577 N LEU A 438
SHEET 3 F 6 PHE A 557 SER A 561 1 N LEU A 559 O ILE A 578
SHEET 4 F 6 TYR A 509 SER A 514 1 N THR A 512 O MET A 560
SHEET 5 F 6 ARG A 454 ALA A 459 1 N LEU A 456 O TYR A 509
SHEET 6 F 6 SER A 485 ASN A 490 1 O SER A 485 N ILE A 455
SHEET 1 G 2 VAL A 523 ASN A 524 0
SHEET 2 G 2 VAL A 527 ILE A 528 -1 O VAL A 527 N ASN A 524
SHEET 1 H 2 TYR A 586 ALA A 587 0
SHEET 2 H 2 ARG A 590 TYR A 591 -1 O ARG A 590 N ALA A 587
SHEET 1 I 2 ILE A 617 PRO A 618 0
SHEET 2 I 2 THR A 626 TYR A 628 -1 O LEU A 627 N ILE A 617
SHEET 1 J 2 LEU B 52 MET B 53 0
SHEET 2 J 2 ALA B 346 LEU B 347 1 O ALA B 346 N MET B 53
SHEET 1 K 2 ASN B 58 TRP B 59 0
SHEET 2 K 2 GLN B 68 ALA B 69 -1 O GLN B 68 N TRP B 59
SHEET 1 L 6 GLY B 88 ILE B 90 0
SHEET 2 L 6 MET B 119 ILE B 122 1 O SER B 121 N ILE B 89
SHEET 3 L 6 THR B 171 ASP B 172 1 O THR B 171 N LEU B 120
SHEET 4 L 6 ALA B 217 PHE B 223 1 O ALA B 217 N ASP B 172
SHEET 5 L 6 MET B 265 THR B 268 1 O MET B 267 N PHE B 223
SHEET 6 L 6 VAL B 314 THR B 317 1 O VAL B 316 N VAL B 266
SHEET 1 M 2 ASP B 230 ASP B 232 0
SHEET 2 M 2 LEU B 237 LEU B 239 -1 O LEU B 239 N ASP B 230
SHEET 1 N 2 THR B 280 LYS B 282 0
SHEET 2 N 2 ASP B 289 LEU B 291 -1 O ILE B 290 N TYR B 281
SHEET 1 O 6 THR B 436 ASN B 440 0
SHEET 2 O 6 ALA B 576 ALA B 579 -1 O LEU B 577 N LEU B 438
SHEET 3 O 6 PHE B 557 SER B 561 1 N LEU B 559 O ILE B 578
SHEET 4 O 6 TYR B 509 SER B 514 1 N THR B 512 O MET B 560
SHEET 5 O 6 ARG B 454 ALA B 459 1 N LEU B 456 O TYR B 509
SHEET 6 O 6 SER B 485 ASN B 490 1 O SER B 485 N ILE B 455
SHEET 1 P 2 VAL B 523 ASN B 524 0
SHEET 2 P 2 VAL B 527 ILE B 528 -1 O VAL B 527 N ASN B 524
SHEET 1 Q 2 TYR B 586 ALA B 587 0
SHEET 2 Q 2 ARG B 590 TYR B 591 -1 O ARG B 590 N ALA B 587
SHEET 1 R 2 ILE B 617 PRO B 618 0
SHEET 2 R 2 THR B 626 TYR B 628 -1 O LEU B 627 N ILE B 617
SHEET 1 S 2 LEU C 52 MET C 53 0
SHEET 2 S 2 ALA C 346 LEU C 347 1 O ALA C 346 N MET C 53
SHEET 1 T 2 ASN C 58 TRP C 59 0
SHEET 2 T 2 GLN C 68 ALA C 69 -1 O GLN C 68 N TRP C 59
SHEET 1 U 6 GLY C 88 ILE C 90 0
SHEET 2 U 6 MET C 119 ILE C 122 1 O SER C 121 N ILE C 89
SHEET 3 U 6 THR C 171 ASP C 172 1 O THR C 171 N LEU C 120
SHEET 4 U 6 ALA C 217 PHE C 223 1 O ALA C 217 N ASP C 172
SHEET 5 U 6 MET C 265 THR C 268 1 O MET C 267 N PHE C 223
SHEET 6 U 6 VAL C 314 THR C 317 1 O VAL C 316 N VAL C 266
SHEET 1 V 2 ASP C 230 ASP C 232 0
SHEET 2 V 2 LEU C 237 LEU C 239 -1 O LEU C 239 N ASP C 230
SHEET 1 W 2 THR C 280 LYS C 282 0
SHEET 2 W 2 ASP C 289 LEU C 291 -1 O ILE C 290 N TYR C 281
SHEET 1 X 6 THR C 436 ASN C 440 0
SHEET 2 X 6 ALA C 576 ALA C 579 -1 O LEU C 577 N LEU C 438
SHEET 3 X 6 PHE C 557 SER C 561 1 N LEU C 559 O ILE C 578
SHEET 4 X 6 TYR C 509 SER C 514 1 N THR C 512 O MET C 560
SHEET 5 X 6 ARG C 454 ALA C 459 1 N LEU C 456 O TYR C 509
SHEET 6 X 6 SER C 485 ASN C 490 1 O SER C 485 N ILE C 455
SHEET 1 Y 2 VAL C 523 ASN C 524 0
SHEET 2 Y 2 VAL C 527 ILE C 528 -1 O VAL C 527 N ASN C 524
SHEET 1 Z 2 TYR C 586 ALA C 587 0
SHEET 2 Z 2 ARG C 590 TYR C 591 -1 O ARG C 590 N ALA C 587
SHEET 1 AA 2 ILE C 617 PRO C 618 0
SHEET 2 AA 2 THR C 626 TYR C 628 -1 O LEU C 627 N ILE C 617
SHEET 1 AB 2 LEU D 52 MET D 53 0
SHEET 2 AB 2 ALA D 346 LEU D 347 1 O ALA D 346 N MET D 53
SHEET 1 AC 2 ASN D 58 TRP D 59 0
SHEET 2 AC 2 GLN D 68 ALA D 69 -1 O GLN D 68 N TRP D 59
SHEET 1 AD 5 SER D 121 ILE D 122 0
SHEET 2 AD 5 THR D 171 ASP D 172 1 O THR D 171 N ILE D 122
SHEET 3 AD 5 ALA D 217 PHE D 223 1 O ALA D 217 N ASP D 172
SHEET 4 AD 5 MET D 265 THR D 268 1 O MET D 267 N PHE D 223
SHEET 5 AD 5 VAL D 314 THR D 317 1 O VAL D 316 N VAL D 266
SHEET 1 AE 2 ASP D 230 ASP D 232 0
SHEET 2 AE 2 LEU D 237 LEU D 239 -1 O LEU D 237 N ASP D 232
SHEET 1 AF 2 THR D 280 LYS D 282 0
SHEET 2 AF 2 ASP D 289 LEU D 291 -1 O ILE D 290 N TYR D 281
SHEET 1 AG 6 THR D 436 ASN D 440 0
SHEET 2 AG 6 ALA D 576 ALA D 579 -1 O LEU D 577 N LEU D 438
SHEET 3 AG 6 PHE D 557 SER D 561 1 N LEU D 559 O ILE D 578
SHEET 4 AG 6 TYR D 509 SER D 514 1 N THR D 512 O MET D 560
SHEET 5 AG 6 ARG D 454 ALA D 459 1 N LEU D 456 O TYR D 509
SHEET 6 AG 6 SER D 485 ASN D 490 1 O SER D 485 N ILE D 455
SHEET 1 AH 2 VAL D 523 ASN D 524 0
SHEET 2 AH 2 VAL D 527 ILE D 528 -1 O VAL D 527 N ASN D 524
SHEET 1 AI 2 TYR D 586 ALA D 587 0
SHEET 2 AI 2 ARG D 590 TYR D 591 -1 O ARG D 590 N ALA D 587
SHEET 1 AJ 2 ILE D 617 PRO D 618 0
SHEET 2 AJ 2 THR D 626 TYR D 628 -1 O LEU D 627 N ILE D 617
LINK OG1 THR A 106 NA NA A 647 1555 1555 3.12
LINK OD1 ASP A 107 NA NA A 647 1555 1555 3.11
LINK OG1 THR B 106 NA NA B 651 1555 1555 3.18
LINK OG1 THR C 106 NA NA C 648 1555 1555 3.18
LINK OD1 ASP C 107 NA NA C 648 1555 1555 3.11
LINK OG1 THR D 106 NA NA D 647 1555 1555 3.16
LINK OD1 ASP D 107 NA NA D 647 1555 1555 3.12
CISPEP 1 SER A 174 PRO A 175 0 2.87
CISPEP 2 PHE A 223 PRO A 224 0 8.12
CISPEP 3 TYR A 399 PRO A 400 0 -1.89
CISPEP 4 LEU A 445 PRO A 446 0 -2.22
CISPEP 5 SER B 174 PRO B 175 0 5.04
CISPEP 6 PHE B 223 PRO B 224 0 9.21
CISPEP 7 TYR B 399 PRO B 400 0 -2.09
CISPEP 8 LEU B 445 PRO B 446 0 -2.92
CISPEP 9 SER C 174 PRO C 175 0 4.43
CISPEP 10 PHE C 223 PRO C 224 0 8.27
CISPEP 11 TYR C 399 PRO C 400 0 -2.69
CISPEP 12 LEU C 445 PRO C 446 0 -2.20
CISPEP 13 SER D 174 PRO D 175 0 4.64
CISPEP 14 PHE D 223 PRO D 224 0 8.39
CISPEP 15 TYR D 399 PRO D 400 0 -2.09
CISPEP 16 LEU D 445 PRO D 446 0 -1.74
SITE 1 AC1 3 LYS A 479 ILE A 481 LYS A 482
SITE 1 AC2 4 ASN A 152 GLN A 155 LYS A 429 LYS A 433
SITE 1 AC3 2 HIS A 222 ASN A 318
SITE 1 AC4 4 ARG A 148 SER A 149 ARG A 150 ILE A 151
SITE 1 AC5 5 THR A 106 ASP A 107 LEU A 167 GLY A 168
SITE 2 AC5 5 LYS A 410
SITE 1 AC6 3 LYS B 479 ILE B 481 LYS B 482
SITE 1 AC7 5 ARG B 148 SER B 149 ARG B 150 ILE B 151
SITE 2 AC7 5 ARG B 202
SITE 1 AC8 1 ILE B 151
SITE 1 AC9 2 HIS B 222 ASN B 318
SITE 1 BC1 3 ASN B 182 ASP B 184 ASP B 230
SITE 1 BC2 4 ASN B 152 GLN B 155 LYS B 429 LYS B 433
SITE 1 BC3 5 THR B 106 ASP B 107 LEU B 167 GLY B 168
SITE 2 BC3 5 LYS B 410
SITE 1 BC4 1 THR C 280
SITE 1 BC5 3 LYS C 479 ILE C 481 LYS C 482
SITE 1 BC6 5 ARG C 148 SER C 149 ARG C 150 ILE C 151
SITE 2 BC6 5 ARG C 202
SITE 1 BC7 5 ASN C 152 GLN C 155 ALA C 426 LYS C 429
SITE 2 BC7 5 LYS C 433
SITE 1 BC8 1 HIS C 222
SITE 1 BC9 4 THR C 106 ASP C 107 GLY C 168 LYS C 410
SITE 1 CC1 2 HIS D 222 HIS D 226
SITE 1 CC2 4 ASN D 152 GLN D 155 LYS D 429 LYS D 433
SITE 1 CC3 5 ARG D 148 SER D 149 ARG D 150 ILE D 151
SITE 2 CC3 5 ARG D 202
SITE 1 CC4 2 LYS D 479 LYS D 482
SITE 1 CC5 5 THR D 106 ASP D 107 LEU D 167 GLY D 168
SITE 2 CC5 5 LYS D 410
CRYST1 56.315 99.149 139.861 90.11 90.05 89.94 P 1 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 0.017757 -0.000018 0.000014 0.00000
SCALE2 0.000000 0.010086 0.000020 0.00000
SCALE3 0.000000 0.000000 0.007150 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
