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HEADER HYDROLASE 29-AUG-24 9JCB
TITLE CALA-LIKE LIPASE FROM KALMANOZYMA BRASILIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KALMANOZYMA BRASILIENSIS GHG001;
SOURCE 3 ORGANISM_TAXID: 1365824;
SOURCE 4 GENE: PSEUBRA_SCAF1G00196;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFAI2
KEYWDS ALPHA/BETA-HYDROLASES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.XUE,L.H.LING,X.JIA,W.S.YEW
REVDAT 1 02-APR-25 9JCB 0
JRNL AUTH L.H.LING,E.T.CHUA,B.XUE,X.JIA,J.Y.CHOW,R.L.YANG,Y.P.LIM,
JRNL AUTH 2 P.HAN,H.XIE,C.H.TAN,G.K.T.NGUYEN,W.S.YEW
JRNL TITL SUSTAINABLE BIOSYNTHESIS OF DIVERSE FATTY ACID ESTERS OF
JRNL TITL 2 HYDROXY FATTY ACIDS (FAHFAS) FOR INDUSTRIAL PRODUCTION
JRNL REF ACS SUSTAIN CHEM ENG V. 13 2830 2025
JRNL REFN ESSN 2168-0485
JRNL DOI 10.1021/ACSSUSCHEMENG.4C08793
REMARK 2
REMARK 2 RESOLUTION. 3.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 3.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 43684
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.360
REMARK 3 FREE R VALUE TEST SET COUNT : 2340
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 45.3600 - 8.8700 1.00 2467 162 0.1521 0.1890
REMARK 3 2 8.8700 - 7.0500 1.00 2482 129 0.1331 0.2171
REMARK 3 3 7.0500 - 6.1600 1.00 2492 105 0.1614 0.2450
REMARK 3 4 6.1600 - 5.6000 1.00 2473 123 0.1770 0.2785
REMARK 3 5 5.6000 - 5.2000 1.00 2440 144 0.1803 0.2563
REMARK 3 6 5.2000 - 4.8900 1.00 2434 167 0.1741 0.2534
REMARK 3 7 4.8900 - 4.6500 1.00 2451 131 0.1681 0.2090
REMARK 3 8 4.6400 - 4.4400 1.00 2399 168 0.1864 0.2604
REMARK 3 9 4.4400 - 4.2700 1.00 2456 143 0.1999 0.2506
REMARK 3 10 4.2700 - 4.1200 1.00 2396 164 0.2160 0.3945
REMARK 3 11 4.1200 - 4.0000 1.00 2483 103 0.2449 0.3213
REMARK 3 12 4.0000 - 3.8800 1.00 2451 121 0.2477 0.2801
REMARK 3 13 3.8800 - 3.7800 1.00 2455 112 0.2539 0.3292
REMARK 3 14 3.7800 - 3.6900 1.00 2440 149 0.2598 0.3182
REMARK 3 15 3.6900 - 3.6000 1.00 2379 191 0.2972 0.3420
REMARK 3 16 3.6000 - 3.5300 1.00 2468 105 0.3207 0.3398
REMARK 3 17 3.5300 - 3.4600 0.89 2178 123 0.3583 0.4110
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 89.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.13
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 11950
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 11950
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 11950
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN E
REMARK 3 ATOM PAIRS NUMBER : 11950
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN F
REMARK 3 ATOM PAIRS NUMBER : 11950
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9JCB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-24.
REMARK 100 THE DEPOSITION ID IS D_1300050879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95365
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44108
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.430
REMARK 200 RESOLUTION RANGE LOW (A) : 45.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.37800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 2.09500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% MPD: 5% PEG 4,000: 100 MM
REMARK 280 IMIDAZOLE: PH 8.0, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 89.15450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 VAL A 13
REMARK 465 MET A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 VAL A 21
REMARK 465 PRO A 22
REMARK 465 MET A 23
REMARK 465 GLN A 24
REMARK 465 LYS A 25
REMARK 465 ARG A 26
REMARK 465 ALA A 27
REMARK 465 VAL B 13
REMARK 465 MET B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 HIS B 19
REMARK 465 HIS B 20
REMARK 465 VAL B 21
REMARK 465 PRO B 22
REMARK 465 MET B 23
REMARK 465 GLN B 24
REMARK 465 LYS B 25
REMARK 465 ARG B 26
REMARK 465 ALA B 27
REMARK 465 VAL C 13
REMARK 465 MET C 14
REMARK 465 HIS C 15
REMARK 465 HIS C 16
REMARK 465 HIS C 17
REMARK 465 HIS C 18
REMARK 465 HIS C 19
REMARK 465 HIS C 20
REMARK 465 VAL C 21
REMARK 465 PRO C 22
REMARK 465 MET C 23
REMARK 465 GLN C 24
REMARK 465 LYS C 25
REMARK 465 ARG C 26
REMARK 465 ALA C 27
REMARK 465 VAL D 13
REMARK 465 MET D 14
REMARK 465 HIS D 15
REMARK 465 HIS D 16
REMARK 465 HIS D 17
REMARK 465 HIS D 18
REMARK 465 HIS D 19
REMARK 465 HIS D 20
REMARK 465 VAL D 21
REMARK 465 PRO D 22
REMARK 465 MET D 23
REMARK 465 GLN D 24
REMARK 465 LYS D 25
REMARK 465 ARG D 26
REMARK 465 ALA D 27
REMARK 465 VAL E 13
REMARK 465 MET E 14
REMARK 465 HIS E 15
REMARK 465 HIS E 16
REMARK 465 HIS E 17
REMARK 465 HIS E 18
REMARK 465 HIS E 19
REMARK 465 HIS E 20
REMARK 465 VAL E 21
REMARK 465 PRO E 22
REMARK 465 MET E 23
REMARK 465 GLN E 24
REMARK 465 LYS E 25
REMARK 465 ARG E 26
REMARK 465 ALA E 27
REMARK 465 VAL F 13
REMARK 465 MET F 14
REMARK 465 HIS F 15
REMARK 465 HIS F 16
REMARK 465 HIS F 17
REMARK 465 HIS F 18
REMARK 465 HIS F 19
REMARK 465 HIS F 20
REMARK 465 VAL F 21
REMARK 465 PRO F 22
REMARK 465 MET F 23
REMARK 465 GLN F 24
REMARK 465 LYS F 25
REMARK 465 ARG F 26
REMARK 465 ALA F 27
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 TRP A 397 OG1 THR A 400 2.05
REMARK 500 O TRP E 397 OG1 THR E 400 2.06
REMARK 500 NZ LYS E 446 OE2 GLU F 352 2.11
REMARK 500 O PRO E 140 OG SER E 144 2.16
REMARK 500 NH2 ARG B 343 OE1 GLN B 366 2.17
REMARK 500 NH2 ARG C 180 O TYR C 216 2.18
REMARK 500 OD2 ASP C 35 NH2 ARG C 56 2.18
REMARK 500 O PRO F 140 OG SER F 144 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 OD2 ASP A 428 OH TYR D 151 2655 2.03
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 ASP A 79 -160.73 -118.36
REMARK 500 THR A 113 61.23 -104.42
REMARK 500 THR A 137 -87.72 -82.85
REMARK 500 ASP A 157 69.15 -68.22
REMARK 500 PRO A 189 155.56 -47.87
REMARK 500 SER A 200 -128.77 60.25
REMARK 500 ALA A 217 60.61 -150.84
REMARK 500 ALA A 243 -3.02 63.58
REMARK 500 SER A 286 -178.49 -63.89
REMARK 500 ASP A 309 83.28 92.96
REMARK 500 HIS A 347 138.77 179.05
REMARK 500 GLU A 350 37.33 -86.29
REMARK 500 GLN A 405 44.62 -142.57
REMARK 500 PRO A 418 94.49 -66.15
REMARK 500 ASP B 79 -163.87 -118.22
REMARK 500 THR B 85 -161.37 -129.02
REMARK 500 THR B 113 59.70 -105.08
REMARK 500 THR B 137 -83.86 -76.70
REMARK 500 ASP B 157 72.96 -68.04
REMARK 500 ILE B 166 7.20 80.41
REMARK 500 SER B 200 -123.96 57.34
REMARK 500 ALA B 217 59.55 -151.58
REMARK 500 ALA B 243 -0.11 65.80
REMARK 500 GLU B 325 48.24 -97.65
REMARK 500 HIS B 347 141.66 176.65
REMARK 500 GLU B 350 39.12 -86.82
REMARK 500 ASN C 43 30.44 -84.64
REMARK 500 ASP C 79 -162.49 -120.93
REMARK 500 THR C 85 -161.04 -128.19
REMARK 500 THR C 113 66.94 -106.18
REMARK 500 THR C 137 -90.90 -80.44
REMARK 500 ASP C 157 72.01 -68.83
REMARK 500 ILE C 166 5.09 81.41
REMARK 500 SER C 200 -124.19 59.81
REMARK 500 ALA C 217 57.12 -148.68
REMARK 500 ALA C 243 -1.09 63.73
REMARK 500 ASP C 309 109.15 75.36
REMARK 500 GLU C 325 48.94 -97.29
REMARK 500 HIS C 347 142.90 179.32
REMARK 500 GLU C 350 36.63 -85.58
REMARK 500 ASP D 31 125.28 -39.88
REMARK 500 ASN D 43 30.85 -82.81
REMARK 500 ASP D 79 -165.14 -118.46
REMARK 500 THR D 137 -95.16 -83.41
REMARK 500 ILE D 166 5.57 81.31
REMARK 500 SER D 200 -126.70 57.83
REMARK 500 ALA D 217 59.02 -149.92
REMARK 500 ASP D 309 151.89 91.55
REMARK 500 GLU D 325 49.03 -95.02
REMARK 500 HIS D 347 140.80 176.54
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 162 0.08 SIDE CHAIN
REMARK 500 ARG B 162 0.21 SIDE CHAIN
REMARK 500 ARG C 162 0.22 SIDE CHAIN
REMARK 500 ARG D 162 0.19 SIDE CHAIN
REMARK 500 ARG E 162 0.19 SIDE CHAIN
REMARK 500 ARG F 162 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9JCB A 21 451 UNP V5F2U3 V5F2U3_KALBG 21 451
DBREF 9JCB B 21 451 UNP V5F2U3 V5F2U3_KALBG 21 451
DBREF 9JCB C 21 451 UNP V5F2U3 V5F2U3_KALBG 21 451
DBREF 9JCB D 21 451 UNP V5F2U3 V5F2U3_KALBG 21 451
DBREF 9JCB E 21 451 UNP V5F2U3 V5F2U3_KALBG 21 451
DBREF 9JCB F 21 451 UNP V5F2U3 V5F2U3_KALBG 21 451
SEQADV 9JCB VAL A 13 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB MET A 14 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS A 15 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS A 16 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS A 17 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS A 18 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS A 19 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS A 20 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB VAL B 13 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB MET B 14 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS B 15 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS B 16 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS B 17 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS B 18 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS B 19 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS B 20 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB VAL C 13 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB MET C 14 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS C 15 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS C 16 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS C 17 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS C 18 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS C 19 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS C 20 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB VAL D 13 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB MET D 14 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS D 15 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS D 16 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS D 17 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS D 18 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS D 19 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS D 20 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB VAL E 13 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB MET E 14 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS E 15 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS E 16 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS E 17 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS E 18 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS E 19 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS E 20 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB VAL F 13 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB MET F 14 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS F 15 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS F 16 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS F 17 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS F 18 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS F 19 UNP V5F2U3 EXPRESSION TAG
SEQADV 9JCB HIS F 20 UNP V5F2U3 EXPRESSION TAG
SEQRES 1 A 439 VAL MET HIS HIS HIS HIS HIS HIS VAL PRO MET GLN LYS
SEQRES 2 A 439 ARG ALA GLN TYR PRO ASP PRO ASN ASP ASP PRO PHE TYR
SEQRES 3 A 439 ARG VAL PRO ALA ASN ILE ASN THR TYR ALA ASN GLY GLN
SEQRES 4 A 439 VAL ILE GLN SER ARG SER ALA THR THR ASP ILE GLY THR
SEQRES 5 A 439 GLN ASN ASN ALA ALA SER PHE GLN LEU LEU TYR ARG THR
SEQRES 6 A 439 THR ASP THR GLN ASN ASN ALA THR ALA SER VAL ALA THR
SEQRES 7 A 439 VAL TRP ILE PRO SER LYS PRO ALA SER PRO PRO LYS ILE
SEQRES 8 A 439 PHE SER TYR GLN VAL TYR GLU ASP ALA THR GLN LEU ASP
SEQRES 9 A 439 CYS ALA PRO SER TYR ASN TYR LEU SER GLY PHE ASP GLN
SEQRES 10 A 439 PRO GLY LYS GLY THR VAL ILE THR ASP THR PRO ILE ALA
SEQRES 11 A 439 ILE SER TRP ALA LEU GLN GLN GLY TYR TYR ALA VAL SER
SEQRES 12 A 439 SER ASP HIS GLU GLY PHE ARG SER ALA PHE ILE ALA GLY
SEQRES 13 A 439 TYR GLU GLU GLY MET ALA ILE LEU ASP GLY VAL ARG ALA
SEQRES 14 A 439 LEU LYS ASN TYR LYS SER LEU PRO SER ASN SER ALA VAL
SEQRES 15 A 439 GLY PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY
SEQRES 16 A 439 TRP ALA VAL SER LEU SER GLY ALA TYR ALA SER ASP LEU
SEQRES 17 A 439 ASN ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER
SEQRES 18 A 439 ALA LYS ASP THR PHE LEU PHE LEU ASN ALA LYS SER PRO
SEQRES 19 A 439 PHE ALA GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA
SEQRES 20 A 439 LEU ALA HIS PRO ASP MET GLU ALA PHE ILE GLN PRO ARG
SEQRES 21 A 439 LEU ASN ALA ARG GLY ARG GLN VAL LEU GLN GLN ILE ARG
SEQRES 22 A 439 SER ARG GLY GLN CYS ILE GLY GLN VAL SER THR GLY TYR
SEQRES 23 A 439 PRO PHE LEU ASP THR PHE SER LEU VAL ASN ASP THR ASN
SEQRES 24 A 439 LEU LEU ASN GLU GLU PRO ILE VAL SER ILE LEU LYS ALA
SEQRES 25 A 439 GLU THR LEU VAL GLN SER GLU ALA GLY TYR THR VAL PRO
SEQRES 26 A 439 VAL PRO LYS PHE PRO ARG PHE MET TRP HIS ALA LEU GLU
SEQRES 27 A 439 ASP GLU ILE VAL PRO PHE GLN PRO ASP ALA GLN TYR VAL
SEQRES 28 A 439 LYS GLU GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN
SEQRES 29 A 439 ILE TYR PRO VAL ALA GLU HIS ILE SER ALA GLU LEU LEU
SEQRES 30 A 439 GLY LEU VAL PRO ALA LEU ALA TRP LEU GLU THR ALA TYR
SEQRES 31 A 439 ALA GLY GLN ALA PRO ARG VAL LEU CYS GLY VAL GLY VAL
SEQRES 32 A 439 PRO VAL PRO GLN PRO SER ALA PHE THR VAL LEU GLY ASP
SEQRES 33 A 439 LYS LEU ALA GLN GLN PHE LYS SER LEU ALA GLY GLN GLN
SEQRES 34 A 439 SER ALA PHE GLY LYS THR PHE PRO SER ILE
SEQRES 1 B 439 VAL MET HIS HIS HIS HIS HIS HIS VAL PRO MET GLN LYS
SEQRES 2 B 439 ARG ALA GLN TYR PRO ASP PRO ASN ASP ASP PRO PHE TYR
SEQRES 3 B 439 ARG VAL PRO ALA ASN ILE ASN THR TYR ALA ASN GLY GLN
SEQRES 4 B 439 VAL ILE GLN SER ARG SER ALA THR THR ASP ILE GLY THR
SEQRES 5 B 439 GLN ASN ASN ALA ALA SER PHE GLN LEU LEU TYR ARG THR
SEQRES 6 B 439 THR ASP THR GLN ASN ASN ALA THR ALA SER VAL ALA THR
SEQRES 7 B 439 VAL TRP ILE PRO SER LYS PRO ALA SER PRO PRO LYS ILE
SEQRES 8 B 439 PHE SER TYR GLN VAL TYR GLU ASP ALA THR GLN LEU ASP
SEQRES 9 B 439 CYS ALA PRO SER TYR ASN TYR LEU SER GLY PHE ASP GLN
SEQRES 10 B 439 PRO GLY LYS GLY THR VAL ILE THR ASP THR PRO ILE ALA
SEQRES 11 B 439 ILE SER TRP ALA LEU GLN GLN GLY TYR TYR ALA VAL SER
SEQRES 12 B 439 SER ASP HIS GLU GLY PHE ARG SER ALA PHE ILE ALA GLY
SEQRES 13 B 439 TYR GLU GLU GLY MET ALA ILE LEU ASP GLY VAL ARG ALA
SEQRES 14 B 439 LEU LYS ASN TYR LYS SER LEU PRO SER ASN SER ALA VAL
SEQRES 15 B 439 GLY PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY
SEQRES 16 B 439 TRP ALA VAL SER LEU SER GLY ALA TYR ALA SER ASP LEU
SEQRES 17 B 439 ASN ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER
SEQRES 18 B 439 ALA LYS ASP THR PHE LEU PHE LEU ASN ALA LYS SER PRO
SEQRES 19 B 439 PHE ALA GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA
SEQRES 20 B 439 LEU ALA HIS PRO ASP MET GLU ALA PHE ILE GLN PRO ARG
SEQRES 21 B 439 LEU ASN ALA ARG GLY ARG GLN VAL LEU GLN GLN ILE ARG
SEQRES 22 B 439 SER ARG GLY GLN CYS ILE GLY GLN VAL SER THR GLY TYR
SEQRES 23 B 439 PRO PHE LEU ASP THR PHE SER LEU VAL ASN ASP THR ASN
SEQRES 24 B 439 LEU LEU ASN GLU GLU PRO ILE VAL SER ILE LEU LYS ALA
SEQRES 25 B 439 GLU THR LEU VAL GLN SER GLU ALA GLY TYR THR VAL PRO
SEQRES 26 B 439 VAL PRO LYS PHE PRO ARG PHE MET TRP HIS ALA LEU GLU
SEQRES 27 B 439 ASP GLU ILE VAL PRO PHE GLN PRO ASP ALA GLN TYR VAL
SEQRES 28 B 439 LYS GLU GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN
SEQRES 29 B 439 ILE TYR PRO VAL ALA GLU HIS ILE SER ALA GLU LEU LEU
SEQRES 30 B 439 GLY LEU VAL PRO ALA LEU ALA TRP LEU GLU THR ALA TYR
SEQRES 31 B 439 ALA GLY GLN ALA PRO ARG VAL LEU CYS GLY VAL GLY VAL
SEQRES 32 B 439 PRO VAL PRO GLN PRO SER ALA PHE THR VAL LEU GLY ASP
SEQRES 33 B 439 LYS LEU ALA GLN GLN PHE LYS SER LEU ALA GLY GLN GLN
SEQRES 34 B 439 SER ALA PHE GLY LYS THR PHE PRO SER ILE
SEQRES 1 C 439 VAL MET HIS HIS HIS HIS HIS HIS VAL PRO MET GLN LYS
SEQRES 2 C 439 ARG ALA GLN TYR PRO ASP PRO ASN ASP ASP PRO PHE TYR
SEQRES 3 C 439 ARG VAL PRO ALA ASN ILE ASN THR TYR ALA ASN GLY GLN
SEQRES 4 C 439 VAL ILE GLN SER ARG SER ALA THR THR ASP ILE GLY THR
SEQRES 5 C 439 GLN ASN ASN ALA ALA SER PHE GLN LEU LEU TYR ARG THR
SEQRES 6 C 439 THR ASP THR GLN ASN ASN ALA THR ALA SER VAL ALA THR
SEQRES 7 C 439 VAL TRP ILE PRO SER LYS PRO ALA SER PRO PRO LYS ILE
SEQRES 8 C 439 PHE SER TYR GLN VAL TYR GLU ASP ALA THR GLN LEU ASP
SEQRES 9 C 439 CYS ALA PRO SER TYR ASN TYR LEU SER GLY PHE ASP GLN
SEQRES 10 C 439 PRO GLY LYS GLY THR VAL ILE THR ASP THR PRO ILE ALA
SEQRES 11 C 439 ILE SER TRP ALA LEU GLN GLN GLY TYR TYR ALA VAL SER
SEQRES 12 C 439 SER ASP HIS GLU GLY PHE ARG SER ALA PHE ILE ALA GLY
SEQRES 13 C 439 TYR GLU GLU GLY MET ALA ILE LEU ASP GLY VAL ARG ALA
SEQRES 14 C 439 LEU LYS ASN TYR LYS SER LEU PRO SER ASN SER ALA VAL
SEQRES 15 C 439 GLY PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY
SEQRES 16 C 439 TRP ALA VAL SER LEU SER GLY ALA TYR ALA SER ASP LEU
SEQRES 17 C 439 ASN ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER
SEQRES 18 C 439 ALA LYS ASP THR PHE LEU PHE LEU ASN ALA LYS SER PRO
SEQRES 19 C 439 PHE ALA GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA
SEQRES 20 C 439 LEU ALA HIS PRO ASP MET GLU ALA PHE ILE GLN PRO ARG
SEQRES 21 C 439 LEU ASN ALA ARG GLY ARG GLN VAL LEU GLN GLN ILE ARG
SEQRES 22 C 439 SER ARG GLY GLN CYS ILE GLY GLN VAL SER THR GLY TYR
SEQRES 23 C 439 PRO PHE LEU ASP THR PHE SER LEU VAL ASN ASP THR ASN
SEQRES 24 C 439 LEU LEU ASN GLU GLU PRO ILE VAL SER ILE LEU LYS ALA
SEQRES 25 C 439 GLU THR LEU VAL GLN SER GLU ALA GLY TYR THR VAL PRO
SEQRES 26 C 439 VAL PRO LYS PHE PRO ARG PHE MET TRP HIS ALA LEU GLU
SEQRES 27 C 439 ASP GLU ILE VAL PRO PHE GLN PRO ASP ALA GLN TYR VAL
SEQRES 28 C 439 LYS GLU GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN
SEQRES 29 C 439 ILE TYR PRO VAL ALA GLU HIS ILE SER ALA GLU LEU LEU
SEQRES 30 C 439 GLY LEU VAL PRO ALA LEU ALA TRP LEU GLU THR ALA TYR
SEQRES 31 C 439 ALA GLY GLN ALA PRO ARG VAL LEU CYS GLY VAL GLY VAL
SEQRES 32 C 439 PRO VAL PRO GLN PRO SER ALA PHE THR VAL LEU GLY ASP
SEQRES 33 C 439 LYS LEU ALA GLN GLN PHE LYS SER LEU ALA GLY GLN GLN
SEQRES 34 C 439 SER ALA PHE GLY LYS THR PHE PRO SER ILE
SEQRES 1 D 439 VAL MET HIS HIS HIS HIS HIS HIS VAL PRO MET GLN LYS
SEQRES 2 D 439 ARG ALA GLN TYR PRO ASP PRO ASN ASP ASP PRO PHE TYR
SEQRES 3 D 439 ARG VAL PRO ALA ASN ILE ASN THR TYR ALA ASN GLY GLN
SEQRES 4 D 439 VAL ILE GLN SER ARG SER ALA THR THR ASP ILE GLY THR
SEQRES 5 D 439 GLN ASN ASN ALA ALA SER PHE GLN LEU LEU TYR ARG THR
SEQRES 6 D 439 THR ASP THR GLN ASN ASN ALA THR ALA SER VAL ALA THR
SEQRES 7 D 439 VAL TRP ILE PRO SER LYS PRO ALA SER PRO PRO LYS ILE
SEQRES 8 D 439 PHE SER TYR GLN VAL TYR GLU ASP ALA THR GLN LEU ASP
SEQRES 9 D 439 CYS ALA PRO SER TYR ASN TYR LEU SER GLY PHE ASP GLN
SEQRES 10 D 439 PRO GLY LYS GLY THR VAL ILE THR ASP THR PRO ILE ALA
SEQRES 11 D 439 ILE SER TRP ALA LEU GLN GLN GLY TYR TYR ALA VAL SER
SEQRES 12 D 439 SER ASP HIS GLU GLY PHE ARG SER ALA PHE ILE ALA GLY
SEQRES 13 D 439 TYR GLU GLU GLY MET ALA ILE LEU ASP GLY VAL ARG ALA
SEQRES 14 D 439 LEU LYS ASN TYR LYS SER LEU PRO SER ASN SER ALA VAL
SEQRES 15 D 439 GLY PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY
SEQRES 16 D 439 TRP ALA VAL SER LEU SER GLY ALA TYR ALA SER ASP LEU
SEQRES 17 D 439 ASN ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER
SEQRES 18 D 439 ALA LYS ASP THR PHE LEU PHE LEU ASN ALA LYS SER PRO
SEQRES 19 D 439 PHE ALA GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA
SEQRES 20 D 439 LEU ALA HIS PRO ASP MET GLU ALA PHE ILE GLN PRO ARG
SEQRES 21 D 439 LEU ASN ALA ARG GLY ARG GLN VAL LEU GLN GLN ILE ARG
SEQRES 22 D 439 SER ARG GLY GLN CYS ILE GLY GLN VAL SER THR GLY TYR
SEQRES 23 D 439 PRO PHE LEU ASP THR PHE SER LEU VAL ASN ASP THR ASN
SEQRES 24 D 439 LEU LEU ASN GLU GLU PRO ILE VAL SER ILE LEU LYS ALA
SEQRES 25 D 439 GLU THR LEU VAL GLN SER GLU ALA GLY TYR THR VAL PRO
SEQRES 26 D 439 VAL PRO LYS PHE PRO ARG PHE MET TRP HIS ALA LEU GLU
SEQRES 27 D 439 ASP GLU ILE VAL PRO PHE GLN PRO ASP ALA GLN TYR VAL
SEQRES 28 D 439 LYS GLU GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN
SEQRES 29 D 439 ILE TYR PRO VAL ALA GLU HIS ILE SER ALA GLU LEU LEU
SEQRES 30 D 439 GLY LEU VAL PRO ALA LEU ALA TRP LEU GLU THR ALA TYR
SEQRES 31 D 439 ALA GLY GLN ALA PRO ARG VAL LEU CYS GLY VAL GLY VAL
SEQRES 32 D 439 PRO VAL PRO GLN PRO SER ALA PHE THR VAL LEU GLY ASP
SEQRES 33 D 439 LYS LEU ALA GLN GLN PHE LYS SER LEU ALA GLY GLN GLN
SEQRES 34 D 439 SER ALA PHE GLY LYS THR PHE PRO SER ILE
SEQRES 1 E 439 VAL MET HIS HIS HIS HIS HIS HIS VAL PRO MET GLN LYS
SEQRES 2 E 439 ARG ALA GLN TYR PRO ASP PRO ASN ASP ASP PRO PHE TYR
SEQRES 3 E 439 ARG VAL PRO ALA ASN ILE ASN THR TYR ALA ASN GLY GLN
SEQRES 4 E 439 VAL ILE GLN SER ARG SER ALA THR THR ASP ILE GLY THR
SEQRES 5 E 439 GLN ASN ASN ALA ALA SER PHE GLN LEU LEU TYR ARG THR
SEQRES 6 E 439 THR ASP THR GLN ASN ASN ALA THR ALA SER VAL ALA THR
SEQRES 7 E 439 VAL TRP ILE PRO SER LYS PRO ALA SER PRO PRO LYS ILE
SEQRES 8 E 439 PHE SER TYR GLN VAL TYR GLU ASP ALA THR GLN LEU ASP
SEQRES 9 E 439 CYS ALA PRO SER TYR ASN TYR LEU SER GLY PHE ASP GLN
SEQRES 10 E 439 PRO GLY LYS GLY THR VAL ILE THR ASP THR PRO ILE ALA
SEQRES 11 E 439 ILE SER TRP ALA LEU GLN GLN GLY TYR TYR ALA VAL SER
SEQRES 12 E 439 SER ASP HIS GLU GLY PHE ARG SER ALA PHE ILE ALA GLY
SEQRES 13 E 439 TYR GLU GLU GLY MET ALA ILE LEU ASP GLY VAL ARG ALA
SEQRES 14 E 439 LEU LYS ASN TYR LYS SER LEU PRO SER ASN SER ALA VAL
SEQRES 15 E 439 GLY PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY
SEQRES 16 E 439 TRP ALA VAL SER LEU SER GLY ALA TYR ALA SER ASP LEU
SEQRES 17 E 439 ASN ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER
SEQRES 18 E 439 ALA LYS ASP THR PHE LEU PHE LEU ASN ALA LYS SER PRO
SEQRES 19 E 439 PHE ALA GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA
SEQRES 20 E 439 LEU ALA HIS PRO ASP MET GLU ALA PHE ILE GLN PRO ARG
SEQRES 21 E 439 LEU ASN ALA ARG GLY ARG GLN VAL LEU GLN GLN ILE ARG
SEQRES 22 E 439 SER ARG GLY GLN CYS ILE GLY GLN VAL SER THR GLY TYR
SEQRES 23 E 439 PRO PHE LEU ASP THR PHE SER LEU VAL ASN ASP THR ASN
SEQRES 24 E 439 LEU LEU ASN GLU GLU PRO ILE VAL SER ILE LEU LYS ALA
SEQRES 25 E 439 GLU THR LEU VAL GLN SER GLU ALA GLY TYR THR VAL PRO
SEQRES 26 E 439 VAL PRO LYS PHE PRO ARG PHE MET TRP HIS ALA LEU GLU
SEQRES 27 E 439 ASP GLU ILE VAL PRO PHE GLN PRO ASP ALA GLN TYR VAL
SEQRES 28 E 439 LYS GLU GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN
SEQRES 29 E 439 ILE TYR PRO VAL ALA GLU HIS ILE SER ALA GLU LEU LEU
SEQRES 30 E 439 GLY LEU VAL PRO ALA LEU ALA TRP LEU GLU THR ALA TYR
SEQRES 31 E 439 ALA GLY GLN ALA PRO ARG VAL LEU CYS GLY VAL GLY VAL
SEQRES 32 E 439 PRO VAL PRO GLN PRO SER ALA PHE THR VAL LEU GLY ASP
SEQRES 33 E 439 LYS LEU ALA GLN GLN PHE LYS SER LEU ALA GLY GLN GLN
SEQRES 34 E 439 SER ALA PHE GLY LYS THR PHE PRO SER ILE
SEQRES 1 F 439 VAL MET HIS HIS HIS HIS HIS HIS VAL PRO MET GLN LYS
SEQRES 2 F 439 ARG ALA GLN TYR PRO ASP PRO ASN ASP ASP PRO PHE TYR
SEQRES 3 F 439 ARG VAL PRO ALA ASN ILE ASN THR TYR ALA ASN GLY GLN
SEQRES 4 F 439 VAL ILE GLN SER ARG SER ALA THR THR ASP ILE GLY THR
SEQRES 5 F 439 GLN ASN ASN ALA ALA SER PHE GLN LEU LEU TYR ARG THR
SEQRES 6 F 439 THR ASP THR GLN ASN ASN ALA THR ALA SER VAL ALA THR
SEQRES 7 F 439 VAL TRP ILE PRO SER LYS PRO ALA SER PRO PRO LYS ILE
SEQRES 8 F 439 PHE SER TYR GLN VAL TYR GLU ASP ALA THR GLN LEU ASP
SEQRES 9 F 439 CYS ALA PRO SER TYR ASN TYR LEU SER GLY PHE ASP GLN
SEQRES 10 F 439 PRO GLY LYS GLY THR VAL ILE THR ASP THR PRO ILE ALA
SEQRES 11 F 439 ILE SER TRP ALA LEU GLN GLN GLY TYR TYR ALA VAL SER
SEQRES 12 F 439 SER ASP HIS GLU GLY PHE ARG SER ALA PHE ILE ALA GLY
SEQRES 13 F 439 TYR GLU GLU GLY MET ALA ILE LEU ASP GLY VAL ARG ALA
SEQRES 14 F 439 LEU LYS ASN TYR LYS SER LEU PRO SER ASN SER ALA VAL
SEQRES 15 F 439 GLY PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR GLY
SEQRES 16 F 439 TRP ALA VAL SER LEU SER GLY ALA TYR ALA SER ASP LEU
SEQRES 17 F 439 ASN ILE ILE GLY ALA ALA TYR GLY GLY LEU PRO ALA SER
SEQRES 18 F 439 ALA LYS ASP THR PHE LEU PHE LEU ASN ALA LYS SER PRO
SEQRES 19 F 439 PHE ALA GLY PHE ALA ILE ALA GLY VAL SER GLY LEU ALA
SEQRES 20 F 439 LEU ALA HIS PRO ASP MET GLU ALA PHE ILE GLN PRO ARG
SEQRES 21 F 439 LEU ASN ALA ARG GLY ARG GLN VAL LEU GLN GLN ILE ARG
SEQRES 22 F 439 SER ARG GLY GLN CYS ILE GLY GLN VAL SER THR GLY TYR
SEQRES 23 F 439 PRO PHE LEU ASP THR PHE SER LEU VAL ASN ASP THR ASN
SEQRES 24 F 439 LEU LEU ASN GLU GLU PRO ILE VAL SER ILE LEU LYS ALA
SEQRES 25 F 439 GLU THR LEU VAL GLN SER GLU ALA GLY TYR THR VAL PRO
SEQRES 26 F 439 VAL PRO LYS PHE PRO ARG PHE MET TRP HIS ALA LEU GLU
SEQRES 27 F 439 ASP GLU ILE VAL PRO PHE GLN PRO ASP ALA GLN TYR VAL
SEQRES 28 F 439 LYS GLU GLN CYS SER LYS GLY ALA ASP ILE ASN TRP ASN
SEQRES 29 F 439 ILE TYR PRO VAL ALA GLU HIS ILE SER ALA GLU LEU LEU
SEQRES 30 F 439 GLY LEU VAL PRO ALA LEU ALA TRP LEU GLU THR ALA TYR
SEQRES 31 F 439 ALA GLY GLN ALA PRO ARG VAL LEU CYS GLY VAL GLY VAL
SEQRES 32 F 439 PRO VAL PRO GLN PRO SER ALA PHE THR VAL LEU GLY ASP
SEQRES 33 F 439 LYS LEU ALA GLN GLN PHE LYS SER LEU ALA GLY GLN GLN
SEQRES 34 F 439 SER ALA PHE GLY LYS THR PHE PRO SER ILE
HET NAG A 501 14
HET NAG B 501 14
HET NAG C 501 14
HET NAG D 501 14
HET NAG E 501 14
HET NAG F 501 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 7 NAG 6(C8 H15 N O6)
HELIX 1 AA1 ASN A 43 TYR A 47 5 5
HELIX 2 AA2 THR A 60 ASN A 67 1 8
HELIX 3 AA3 GLN A 114 CYS A 117 5 4
HELIX 4 AA4 ALA A 118 LEU A 124 1 7
HELIX 5 AA5 LYS A 132 ILE A 136 5 5
HELIX 6 AA6 ASP A 138 GLN A 149 1 12
HELIX 7 AA7 ALA A 167 SER A 187 1 21
HELIX 8 AA8 SER A 200 ALA A 217 1 18
HELIX 9 AA9 SER A 233 ASN A 242 1 10
HELIX 10 AB1 ALA A 248 HIS A 262 1 15
HELIX 11 AB2 HIS A 262 LEU A 273 1 12
HELIX 12 AB3 ASN A 274 SER A 286 1 13
HELIX 13 AB4 CYS A 290 TYR A 298 1 9
HELIX 14 AB5 ASP A 302 VAL A 307 1 6
HELIX 15 AB6 ASP A 309 ASN A 314 5 6
HELIX 16 AB7 PRO A 317 THR A 326 1 10
HELIX 17 AB8 PRO A 355 LYS A 369 1 15
HELIX 18 AB9 GLU A 382 GLY A 390 1 9
HELIX 19 AC1 GLY A 390 ALA A 403 1 14
HELIX 20 AC2 SER A 421 GLY A 427 1 7
HELIX 21 AC3 GLY A 427 ALA A 438 1 12
HELIX 22 AC4 ASN B 43 TYR B 47 5 5
HELIX 23 AC5 THR B 60 ASN B 67 1 8
HELIX 24 AC6 GLN B 114 CYS B 117 5 4
HELIX 25 AC7 ALA B 118 LEU B 124 1 7
HELIX 26 AC8 GLN B 129 ILE B 136 5 8
HELIX 27 AC9 ASP B 138 GLN B 149 1 12
HELIX 28 AD1 ALA B 167 SER B 187 1 21
HELIX 29 AD2 SER B 200 ALA B 217 1 18
HELIX 30 AD3 SER B 233 ASN B 242 1 10
HELIX 31 AD4 ALA B 248 HIS B 262 1 15
HELIX 32 AD5 HIS B 262 GLN B 270 1 9
HELIX 33 AD6 PRO B 271 LEU B 273 5 3
HELIX 34 AD7 ASN B 274 SER B 286 1 13
HELIX 35 AD8 CYS B 290 TYR B 298 1 9
HELIX 36 AD9 ASP B 302 LEU B 306 5 5
HELIX 37 AE1 ASP B 309 GLU B 315 5 7
HELIX 38 AE2 PRO B 317 GLU B 325 1 9
HELIX 39 AE3 PRO B 355 LYS B 369 1 15
HELIX 40 AE4 GLU B 382 GLY B 390 1 9
HELIX 41 AE5 GLY B 390 ALA B 403 1 14
HELIX 42 AE6 SER B 421 LEU B 426 1 6
HELIX 43 AE7 GLY B 427 SER B 436 1 10
HELIX 44 AE8 ASN C 43 TYR C 47 5 5
HELIX 45 AE9 THR C 60 ASN C 67 1 8
HELIX 46 AF1 GLN C 114 CYS C 117 5 4
HELIX 47 AF2 ALA C 118 LEU C 124 1 7
HELIX 48 AF3 ASP C 138 GLN C 149 1 12
HELIX 49 AF4 ALA C 167 SER C 187 1 21
HELIX 50 AF5 SER C 200 ALA C 217 1 18
HELIX 51 AF6 SER C 233 ASN C 242 1 10
HELIX 52 AF7 ALA C 248 HIS C 262 1 15
HELIX 53 AF8 HIS C 262 GLN C 270 1 9
HELIX 54 AF9 ASN C 274 SER C 286 1 13
HELIX 55 AG1 CYS C 290 TYR C 298 1 9
HELIX 56 AG2 ASP C 302 VAL C 307 1 6
HELIX 57 AG3 PRO C 317 GLU C 325 1 9
HELIX 58 AG4 PRO C 355 LYS C 369 1 15
HELIX 59 AG5 GLU C 382 GLY C 390 1 9
HELIX 60 AG6 GLY C 390 ALA C 403 1 14
HELIX 61 AG7 SER C 421 LEU C 426 1 6
HELIX 62 AG8 GLY C 427 SER C 436 1 10
HELIX 63 AG9 ASP D 31 ASP D 35 5 5
HELIX 64 AH1 PRO D 41 TYR D 47 5 7
HELIX 65 AH2 THR D 60 ASN D 67 1 8
HELIX 66 AH3 ALA D 118 LEU D 124 1 7
HELIX 67 AH4 LYS D 132 ILE D 136 5 5
HELIX 68 AH5 ASP D 138 GLY D 150 1 13
HELIX 69 AH6 ALA D 167 SER D 187 1 21
HELIX 70 AH7 SER D 200 ALA D 217 1 18
HELIX 71 AH8 SER D 233 ASN D 242 1 10
HELIX 72 AH9 ALA D 248 HIS D 262 1 15
HELIX 73 AI1 HIS D 262 LEU D 273 1 12
HELIX 74 AI2 ASN D 274 SER D 286 1 13
HELIX 75 AI3 CYS D 290 TYR D 298 1 9
HELIX 76 AI4 ASP D 302 VAL D 307 1 6
HELIX 77 AI5 PRO D 317 GLU D 325 1 9
HELIX 78 AI6 PRO D 355 LYS D 369 1 15
HELIX 79 AI7 GLU D 382 GLY D 390 1 9
HELIX 80 AI8 GLY D 390 ALA D 403 1 14
HELIX 81 AI9 SER D 421 LEU D 426 1 6
HELIX 82 AJ1 GLY D 427 SER D 436 1 10
HELIX 83 AJ2 ASN E 43 TYR E 47 5 5
HELIX 84 AJ3 THR E 60 ASN E 67 1 8
HELIX 85 AJ4 GLN E 114 CYS E 117 5 4
HELIX 86 AJ5 ALA E 118 LEU E 124 1 7
HELIX 87 AJ6 GLN E 129 ILE E 136 5 8
HELIX 88 AJ7 ASP E 138 GLN E 149 1 12
HELIX 89 AJ8 ALA E 167 SER E 187 1 21
HELIX 90 AJ9 SER E 200 ALA E 217 1 18
HELIX 91 AK1 SER E 233 ASN E 242 1 10
HELIX 92 AK2 ALA E 248 HIS E 262 1 15
HELIX 93 AK3 HIS E 262 GLN E 270 1 9
HELIX 94 AK4 PRO E 271 LEU E 273 5 3
HELIX 95 AK5 ASN E 274 SER E 286 1 13
HELIX 96 AK6 CYS E 290 TYR E 298 1 9
HELIX 97 AK7 ASP E 302 VAL E 307 1 6
HELIX 98 AK8 PRO E 317 GLU E 325 1 9
HELIX 99 AK9 PRO E 355 LYS E 369 1 15
HELIX 100 AL1 GLU E 382 GLY E 390 1 9
HELIX 101 AL2 GLY E 390 ALA E 403 1 14
HELIX 102 AL3 SER E 421 LEU E 426 1 6
HELIX 103 AL4 GLY E 427 SER E 436 1 10
HELIX 104 AL5 ASN F 43 TYR F 47 5 5
HELIX 105 AL6 THR F 60 ASN F 67 1 8
HELIX 106 AL7 GLN F 114 CYS F 117 5 4
HELIX 107 AL8 ALA F 118 TYR F 123 1 6
HELIX 108 AL9 ASP F 138 GLY F 150 1 13
HELIX 109 AM1 ALA F 167 SER F 187 1 21
HELIX 110 AM2 SER F 200 ALA F 217 1 18
HELIX 111 AM3 SER F 233 ASN F 242 1 10
HELIX 112 AM4 ALA F 248 HIS F 262 1 15
HELIX 113 AM5 HIS F 262 GLN F 270 1 9
HELIX 114 AM6 ASN F 274 SER F 286 1 13
HELIX 115 AM7 CYS F 290 TYR F 298 1 9
HELIX 116 AM8 ASP F 302 VAL F 307 1 6
HELIX 117 AM9 PRO F 317 GLU F 325 1 9
HELIX 118 AN1 PRO F 355 LYS F 369 1 15
HELIX 119 AN2 GLU F 382 GLY F 390 1 9
HELIX 120 AN3 GLY F 390 ALA F 403 1 14
HELIX 121 AN4 SER F 421 LEU F 426 1 6
HELIX 122 AN5 GLY F 427 SER F 436 1 10
SHEET 1 AA1 9 GLN A 51 ALA A 58 0
SHEET 2 AA1 9 ALA A 68 THR A 78 -1 O GLN A 72 N ARG A 56
SHEET 3 AA1 9 ALA A 84 PRO A 94 -1 O SER A 87 N TYR A 75
SHEET 4 AA1 9 TYR A 152 SER A 156 -1 O ALA A 153 N TRP A 92
SHEET 5 AA1 9 LYS A 102 GLN A 107 1 N PHE A 104 O TYR A 152
SHEET 6 AA1 9 ALA A 193 TYR A 199 1 O ALA A 193 N ILE A 103
SHEET 7 AA1 9 ASN A 221 GLY A 228 1 O ALA A 226 N PHE A 196
SHEET 8 AA1 9 ARG A 343 ALA A 348 1 O PHE A 344 N TYR A 227
SHEET 9 AA1 9 ILE A 373 TYR A 378 1 O ASN A 374 N ARG A 343
SHEET 1 AA2 9 GLN B 51 ALA B 58 0
SHEET 2 AA2 9 SER B 70 THR B 78 -1 O LEU B 74 N ILE B 53
SHEET 3 AA2 9 ALA B 84 TRP B 92 -1 O SER B 87 N TYR B 75
SHEET 4 AA2 9 TYR B 152 SER B 156 -1 O SER B 155 N THR B 90
SHEET 5 AA2 9 LYS B 102 GLN B 107 1 N PHE B 104 O TYR B 152
SHEET 6 AA2 9 ALA B 193 TYR B 199 1 O GLY B 195 N ILE B 103
SHEET 7 AA2 9 ASN B 221 GLY B 228 1 O ALA B 226 N PHE B 196
SHEET 8 AA2 9 ARG B 343 ALA B 348 1 O PHE B 344 N TYR B 227
SHEET 9 AA2 9 ILE B 373 TYR B 378 1 O ASN B 374 N MET B 345
SHEET 1 AA3 9 VAL C 52 ALA C 58 0
SHEET 2 AA3 9 ALA C 69 THR C 78 -1 O GLN C 72 N ARG C 56
SHEET 3 AA3 9 ALA C 84 ILE C 93 -1 O ILE C 93 N ALA C 69
SHEET 4 AA3 9 TYR C 152 SER C 156 -1 O ALA C 153 N TRP C 92
SHEET 5 AA3 9 LYS C 102 GLN C 107 1 N PHE C 104 O TYR C 152
SHEET 6 AA3 9 ALA C 193 TYR C 199 1 O ALA C 193 N ILE C 103
SHEET 7 AA3 9 ASN C 221 GLY C 228 1 O ALA C 226 N PHE C 196
SHEET 8 AA3 9 ARG C 343 ALA C 348 1 O PHE C 344 N TYR C 227
SHEET 9 AA3 9 ILE C 373 TYR C 378 1 O ASN C 374 N ARG C 343
SHEET 1 AA4 9 VAL D 52 ALA D 58 0
SHEET 2 AA4 9 SER D 70 THR D 78 -1 O SER D 70 N ALA D 58
SHEET 3 AA4 9 ALA D 84 TRP D 92 -1 O SER D 87 N TYR D 75
SHEET 4 AA4 9 TYR D 152 SER D 156 -1 O SER D 155 N THR D 90
SHEET 5 AA4 9 LYS D 102 GLN D 107 1 N PHE D 104 O TYR D 152
SHEET 6 AA4 9 ALA D 193 TYR D 199 1 O GLY D 195 N ILE D 103
SHEET 7 AA4 9 ASN D 221 GLY D 228 1 O ASN D 221 N VAL D 194
SHEET 8 AA4 9 PRO D 342 TRP D 346 1 O PHE D 344 N TYR D 227
SHEET 9 AA4 9 ASP D 372 TRP D 375 1 O ASN D 374 N ARG D 343
SHEET 1 AA5 9 GLN E 51 ALA E 58 0
SHEET 2 AA5 9 ALA E 69 THR E 78 -1 O LEU E 74 N ILE E 53
SHEET 3 AA5 9 ALA E 84 ILE E 93 -1 O SER E 87 N TYR E 75
SHEET 4 AA5 9 TYR E 152 SER E 156 -1 O ALA E 153 N TRP E 92
SHEET 5 AA5 9 LYS E 102 GLN E 107 1 N PHE E 104 O TYR E 152
SHEET 6 AA5 9 ALA E 193 TYR E 199 1 O GLY E 195 N ILE E 103
SHEET 7 AA5 9 ASN E 221 GLY E 228 1 O ASN E 221 N VAL E 194
SHEET 8 AA5 9 ARG E 343 ALA E 348 1 O PHE E 344 N TYR E 227
SHEET 9 AA5 9 ILE E 373 TYR E 378 1 O ASN E 374 N ARG E 343
SHEET 1 AA6 9 VAL F 52 SER F 57 0
SHEET 2 AA6 9 ALA F 69 THR F 78 -1 O LEU F 74 N ILE F 53
SHEET 3 AA6 9 ALA F 84 ILE F 93 -1 O ALA F 89 N LEU F 73
SHEET 4 AA6 9 TYR F 152 SER F 156 -1 O SER F 155 N THR F 90
SHEET 5 AA6 9 LYS F 102 GLN F 107 1 N PHE F 104 O TYR F 152
SHEET 6 AA6 9 ALA F 193 TYR F 199 1 O ALA F 193 N ILE F 103
SHEET 7 AA6 9 ASN F 221 GLY F 228 1 O ALA F 226 N PHE F 196
SHEET 8 AA6 9 PRO F 342 ALA F 348 1 O PHE F 344 N ALA F 225
SHEET 9 AA6 9 ASP F 372 TYR F 378 1 O ASN F 374 N ARG F 343
SSBOND 1 CYS A 117 CYS A 290 1555 1555 2.04
SSBOND 2 CYS B 117 CYS B 290 1555 1555 2.06
SSBOND 3 CYS C 117 CYS C 290 1555 1555 2.03
SSBOND 4 CYS D 117 CYS D 290 1555 1555 2.03
SSBOND 5 CYS E 117 CYS E 290 1555 1555 2.03
SSBOND 6 CYS F 117 CYS F 290 1555 1555 2.04
LINK ND2 ASN A 308 C1 NAG A 501 1555 1555 1.45
LINK ND2 ASN B 308 C1 NAG B 501 1555 1555 1.45
LINK ND2 ASN C 308 C1 NAG C 501 1555 1555 1.46
LINK ND2 ASN D 308 C1 NAG D 501 1555 1555 1.47
LINK ND2 ASN E 308 C1 NAG E 501 1555 1555 1.45
LINK ND2 ASN F 308 C1 NAG F 501 1555 1555 1.46
CISPEP 1 SER A 99 PRO A 100 0 0.21
CISPEP 2 GLU A 316 PRO A 317 0 7.78
CISPEP 3 SER B 99 PRO B 100 0 -0.88
CISPEP 4 GLU B 316 PRO B 317 0 4.49
CISPEP 5 SER C 99 PRO C 100 0 -0.08
CISPEP 6 GLU C 316 PRO C 317 0 2.67
CISPEP 7 SER D 99 PRO D 100 0 -0.46
CISPEP 8 GLU D 316 PRO D 317 0 14.91
CISPEP 9 SER E 99 PRO E 100 0 -2.74
CISPEP 10 GLU E 316 PRO E 317 0 4.17
CISPEP 11 SER F 99 PRO F 100 0 -3.80
CISPEP 12 GLU F 316 PRO F 317 0 5.19
CRYST1 104.372 178.309 105.386 90.00 119.24 90.00 P 1 21 1 12
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 0.009581 0.000000 0.005363 0.00000
SCALE2 0.000000 0.005608 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010875 0.00000
TER 3227 ILE A 451
TER 6454 ILE B 451
TER 9681 ILE C 451
TER 12908 ILE D 451
TER 16135 ILE E 451
TER 19362 ILE F 451
MASTER 461 0 6 122 54 0 0 619440 6 102 204
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