| 6k5e-pdb | HEADER HYDROLASE 28-MAY-19 6K5E
TITLE CRYSTAL STRUCTURE OF BIOH FROM KLEBSIELLA PNEUMONIA
CAVEAT 6K5E THE DISTANCE BETWEEN LEU221 AND ASP219 IS 1.34 FOR A/B/C/D
CAVEAT 2 6K5E CHAINS DUE TO THE POOR ELECTRON DENSITY OF ASP220.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PIMELOYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: BIOTIN SYNTHESIS PROTEIN BIOH,CARBOXYLESTERASE BIOH;
COMPND 5 EC: 3.1.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 GENE: BIOH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K-12
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.WANG,Y.CHEN
REVDAT 1 17-JUL-19 6K5E 0
JRNL AUTH L.WANG,Y.CHEN
JRNL TITL CRYSTAL STRUCTURE OF BIOH FROM KLEBSIELLA PNEUMONIA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.15.2_3472: ???)
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.540
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.8
REMARK 3 NUMBER OF REFLECTIONS : 67403
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810
REMARK 3 FREE R VALUE TEST SET COUNT : 3245
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 36.7411 - 6.4077 0.99 3537 181 0.1928 0.2575
REMARK 3 2 6.4077 - 5.0903 0.98 3401 171 0.1911 0.2362
REMARK 3 3 5.0903 - 4.4481 0.94 3230 156 0.1477 0.1920
REMARK 3 4 4.4481 - 4.0420 0.92 3108 141 0.1506 0.2371
REMARK 3 5 4.0420 - 3.7526 0.91 3140 141 0.1694 0.2654
REMARK 3 6 3.7526 - 3.5315 0.92 3104 143 0.1793 0.2641
REMARK 3 7 3.5315 - 3.3548 0.91 3062 169 0.1962 0.3356
REMARK 3 8 3.3548 - 3.2088 0.91 3044 170 0.1985 0.2615
REMARK 3 9 3.2088 - 3.0854 0.92 3114 154 0.2014 0.2954
REMARK 3 10 3.0854 - 2.9790 0.91 3057 170 0.2032 0.2763
REMARK 3 11 2.9790 - 2.8858 0.92 3131 130 0.2001 0.2889
REMARK 3 12 2.8858 - 2.8034 0.91 3077 153 0.2019 0.3260
REMARK 3 13 2.8034 - 2.7296 0.91 3024 160 0.2135 0.3227
REMARK 3 14 2.7296 - 2.6630 0.90 2997 172 0.2244 0.3101
REMARK 3 15 2.6630 - 2.6025 0.89 3006 151 0.2184 0.3165
REMARK 3 16 2.6025 - 2.5471 0.86 2841 143 0.2318 0.3421
REMARK 3 17 2.5471 - 2.4962 0.84 2831 143 0.2237 0.3115
REMARK 3 18 2.4962 - 2.4491 0.80 2655 142 0.2148 0.3286
REMARK 3 19 2.4491 - 2.4054 0.73 2392 129 0.2142 0.3042
REMARK 3 20 2.4054 - 2.3646 0.65 2183 115 0.2130 0.3025
REMARK 3 21 2.3646 - 2.3265 0.56 1857 94 0.2106 0.3017
REMARK 3 22 2.3265 - 2.2907 0.47 1604 80 0.2186 0.3096
REMARK 3 23 2.2907 - 2.2570 0.23 763 37 0.2259 0.3241
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 11987
REMARK 3 ANGLE : 1.017 16372
REMARK 3 CHIRALITY : 0.054 1836
REMARK 3 PLANARITY : 0.007 2128
REMARK 3 DIHEDRAL : 4.289 9722
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 6K5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1300012296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979617
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73488
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.257
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09100
REMARK 200 FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30100
REMARK 200 FOR SHELL : 2.360
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 1.5% PGE400,
REMARK 280 0.1 M HEPES (PH 7.5), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 146.42850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 146.42850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 53.82100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.76550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.82100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.76550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 146.42850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 53.82100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.76550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 146.42850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 53.82100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.76550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: A, B, E
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 APPLY THE FOLLOWING TO CHAINS: C, D, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 343 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 LYS A 213
REMARK 465 ASP A 220
REMARK 465 LEU A 221
REMARK 465 MET B 1
REMARK 465 LYS B 213
REMARK 465 ASP B 220
REMARK 465 LEU B 221
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 ASP C 115
REMARK 465 GLN C 130
REMARK 465 GLN C 131
REMARK 465 LEU C 132
REMARK 465 SER C 133
REMARK 465 GLN C 137
REMARK 465 ARG C 138
REMARK 465 ARG C 142
REMARK 465 ILE C 214
REMARK 465 ASP C 220
REMARK 465 LEU C 221
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 ASP D 115
REMARK 465 ASP D 220
REMARK 465 LEU D 221
REMARK 465 ASP E 115
REMARK 465 ASP E 116
REMARK 465 ARG E 194
REMARK 465 ASP E 220
REMARK 465 LEU E 221
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 SER F 133
REMARK 465 ASP F 134
REMARK 465 ASP F 135
REMARK 465 ARG F 138
REMARK 465 GLU F 141
REMARK 465 ARG F 142
REMARK 465 GLN F 190
REMARK 465 ALA F 191
REMARK 465 LEU F 192
REMARK 465 VAL F 193
REMARK 465 ARG F 194
REMARK 465 LEU F 195
REMARK 465 ARG F 212
REMARK 465 ASP F 220
REMARK 465 LEU F 221
REMARK 465 TRP F 222
REMARK 465 PRO F 223
REMARK 465 GLU F 224
REMARK 465 SER F 225
REMARK 465 GLY F 257
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 GLU B 226 CG CD OE1 OE2
REMARK 470 LYS C 121 CG CD CE NZ
REMARK 470 GLN D 35 CG CD OE1 NE2
REMARK 470 LYS D 121 CG CD CE NZ
REMARK 470 LYS E 121 CG CD CE NZ
REMARK 470 ARG E 142 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 121 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 303 O HOH B 349 1.90
REMARK 500 O ARG D 189 O HOH D 301 1.98
REMARK 500 O ASP E 219 N TRP E 222 2.02
REMARK 500 O GLN F 75 O HOH F 301 2.05
REMARK 500 OG SER B 38 O HOH B 301 2.06
REMARK 500 O HOH D 378 O HOH D 398 2.06
REMARK 500 O HOH A 377 O HOH A 392 2.11
REMARK 500 O HOH D 401 O HOH D 407 2.12
REMARK 500 OG SER E 82 O HOH E 301 2.12
REMARK 500 OG SER B 82 O HOH B 302 2.12
REMARK 500 O HOH B 412 O HOH E 361 2.12
REMARK 500 NE1 TRP D 222 O HOH D 301 2.13
REMARK 500 OG SER E 82 O HOH E 302 2.14
REMARK 500 O HOH A 395 O HOH E 334 2.14
REMARK 500 O HOH A 317 O HOH A 331 2.16
REMARK 500 O PRO B 48 O HOH B 303 2.16
REMARK 500 O HOH B 316 O HOH B 349 2.16
REMARK 500 O HOH D 337 O HOH D 351 2.16
REMARK 500 O HOH A 331 O HOH A 375 2.17
REMARK 500 O ALA A 112 O HOH A 301 2.17
REMARK 500 OD2 ASP E 134 O HOH E 303 2.18
REMARK 500 N ARG C 194 O HOH C 301 2.18
REMARK 500 NE2 GLN A 100 O HOH A 302 2.19
REMARK 500 OE2 GLU B 11 O HOH B 304 2.19
REMARK 500 OE1 GLN E 100 O HOH E 304 2.19
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 GLU A 11 72.47 -158.63
REMARK 500 LEU A 24 -156.27 -117.12
REMARK 500 SER A 82 -124.10 59.72
REMARK 500 CYS A 110 88.36 -158.26
REMARK 500 SER A 153 5.12 178.89
REMARK 500 ALA A 234 -134.27 -106.72
REMARK 500 ALA A 234 -133.94 -106.72
REMARK 500 LEU B 24 -154.00 -110.62
REMARK 500 SER B 82 -117.66 55.84
REMARK 500 ASP B 116 17.96 59.25
REMARK 500 ASP B 135 70.07 -155.36
REMARK 500 ALA B 234 -125.77 -110.81
REMARK 500 LEU C 24 -157.43 -100.94
REMARK 500 SER C 53 47.88 -99.54
REMARK 500 SER C 82 -124.40 57.80
REMARK 500 ALA C 234 -127.53 -109.23
REMARK 500 ALA C 234 -127.74 -109.28
REMARK 500 GLU D 11 -62.56 108.38
REMARK 500 LEU D 24 -156.06 -112.20
REMARK 500 LEU D 24 -155.48 -106.41
REMARK 500 SER D 82 -114.19 56.63
REMARK 500 ARG D 212 22.95 -72.21
REMARK 500 ARG D 212 24.14 -72.21
REMARK 500 ALA D 234 -117.03 -110.08
REMARK 500 GLU E 11 31.49 -144.41
REMARK 500 ASP E 13 -1.74 42.51
REMARK 500 HIS E 20 -169.59 -75.57
REMARK 500 SER E 53 50.76 -106.79
REMARK 500 MET E 59 149.40 -172.52
REMARK 500 SER E 82 -128.41 57.73
REMARK 500 ARG E 95 68.89 -154.69
REMARK 500 ALA E 101 145.62 -174.98
REMARK 500 ASP E 135 87.94 -154.86
REMARK 500 PRO E 211 -108.09 -70.39
REMARK 500 PRO E 211 -107.18 -70.39
REMARK 500 ARG E 212 44.61 -145.47
REMARK 500 ARG E 212 46.55 -147.94
REMARK 500 LYS E 213 7.35 -69.33
REMARK 500 ALA E 234 -128.12 -105.81
REMARK 500 LEU F 24 -143.98 -114.18
REMARK 500 ASN F 25 -178.29 -172.77
REMARK 500 SER F 53 40.43 -103.23
REMARK 500 PRO F 73 152.67 -49.25
REMARK 500 SER F 82 -131.01 53.28
REMARK 500 ALA F 101 142.14 -179.33
REMARK 500 GLN F 131 0.07 -67.71
REMARK 500 SER F 153 44.01 -92.82
REMARK 500 SER F 167 11.26 58.39
REMARK 500 ASP F 207 -83.95 -40.89
REMARK 500 ALA F 234 -132.87 -112.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 409 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH B 429 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH E 380 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH F 355 DISTANCE = 5.84 ANGSTROMS
DBREF1 6K5E A 1 257 UNP A0A0S4G6Z4_KLEPN
DBREF2 6K5E A A0A0S4G6Z4 1 257
DBREF1 6K5E B 1 257 UNP A0A0S4G6Z4_KLEPN
DBREF2 6K5E B A0A0S4G6Z4 1 257
DBREF1 6K5E C 1 257 UNP A0A0S4G6Z4_KLEPN
DBREF2 6K5E C A0A0S4G6Z4 1 257
DBREF1 6K5E D 1 257 UNP A0A0S4G6Z4_KLEPN
DBREF2 6K5E D A0A0S4G6Z4 1 257
DBREF1 6K5E E 1 257 UNP A0A0S4G6Z4_KLEPN
DBREF2 6K5E E A0A0S4G6Z4 1 257
DBREF1 6K5E F 1 257 UNP A0A0S4G6Z4_KLEPN
DBREF2 6K5E F A0A0S4G6Z4 1 257
SEQRES 1 A 257 MET ASN ASP ILE TRP TRP GLN THR ILE GLY GLU GLY ASP
SEQRES 2 A 257 CYS HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 A 257 GLN VAL TRP ASP CYS ILE THR PRO GLN LEU ALA SER HIS
SEQRES 4 A 257 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY TYR GLY ARG
SEQRES 5 A 257 SER GLY GLY PHE GLY ALA MET SER LEU GLU ALA MET ALA
SEQRES 6 A 257 GLN ARG VAL LEU GLU GLN ALA PRO PRO GLN ALA VAL TRP
SEQRES 7 A 257 LEU GLY TRP SER LEU GLY GLY LEU VAL ALA SER GLN VAL
SEQRES 8 A 257 ALA ILE MET ARG PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 A 257 VAL ALA SER SER PRO CYS PHE ALA ALA ARG ASP ASP TRP
SEQRES 10 A 257 PRO GLY ILE LYS PRO GLU VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 A 257 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 A 257 LEU ALA LEU GLN THR MET GLY THR GLU SER ALA ARG GLN
SEQRES 13 A 257 ASP ALA ARG ALA LEU LYS GLN ALA VAL LEU SER LEU PRO
SEQRES 14 A 257 MET PRO SER ALA GLU ALA LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 A 257 LEU ARG THR VAL ASP LEU ARG GLN ALA LEU VAL ARG LEU
SEQRES 16 A 257 PRO MET PRO PHE LEU ARG LEU TYR GLY ARG LEU ASP GLY
SEQRES 17 A 257 LEU VAL PRO ARG LYS ILE VAL PRO LEU LEU ASP ASP LEU
SEQRES 18 A 257 TRP PRO GLU SER GLU SER ILE LEU PHE ASP LYS ALA ALA
SEQRES 19 A 257 HIS ALA PRO PHE VAL SER HIS PRO ALA ALA PHE CYS GLU
SEQRES 20 A 257 PRO LEU LEU ALA LEU LYS THR ARG LEU GLY
SEQRES 1 B 257 MET ASN ASP ILE TRP TRP GLN THR ILE GLY GLU GLY ASP
SEQRES 2 B 257 CYS HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 B 257 GLN VAL TRP ASP CYS ILE THR PRO GLN LEU ALA SER HIS
SEQRES 4 B 257 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY TYR GLY ARG
SEQRES 5 B 257 SER GLY GLY PHE GLY ALA MET SER LEU GLU ALA MET ALA
SEQRES 6 B 257 GLN ARG VAL LEU GLU GLN ALA PRO PRO GLN ALA VAL TRP
SEQRES 7 B 257 LEU GLY TRP SER LEU GLY GLY LEU VAL ALA SER GLN VAL
SEQRES 8 B 257 ALA ILE MET ARG PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 B 257 VAL ALA SER SER PRO CYS PHE ALA ALA ARG ASP ASP TRP
SEQRES 10 B 257 PRO GLY ILE LYS PRO GLU VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 B 257 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 B 257 LEU ALA LEU GLN THR MET GLY THR GLU SER ALA ARG GLN
SEQRES 13 B 257 ASP ALA ARG ALA LEU LYS GLN ALA VAL LEU SER LEU PRO
SEQRES 14 B 257 MET PRO SER ALA GLU ALA LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 B 257 LEU ARG THR VAL ASP LEU ARG GLN ALA LEU VAL ARG LEU
SEQRES 16 B 257 PRO MET PRO PHE LEU ARG LEU TYR GLY ARG LEU ASP GLY
SEQRES 17 B 257 LEU VAL PRO ARG LYS ILE VAL PRO LEU LEU ASP ASP LEU
SEQRES 18 B 257 TRP PRO GLU SER GLU SER ILE LEU PHE ASP LYS ALA ALA
SEQRES 19 B 257 HIS ALA PRO PHE VAL SER HIS PRO ALA ALA PHE CYS GLU
SEQRES 20 B 257 PRO LEU LEU ALA LEU LYS THR ARG LEU GLY
SEQRES 1 C 257 MET ASN ASP ILE TRP TRP GLN THR ILE GLY GLU GLY ASP
SEQRES 2 C 257 CYS HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 C 257 GLN VAL TRP ASP CYS ILE THR PRO GLN LEU ALA SER HIS
SEQRES 4 C 257 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY TYR GLY ARG
SEQRES 5 C 257 SER GLY GLY PHE GLY ALA MET SER LEU GLU ALA MET ALA
SEQRES 6 C 257 GLN ARG VAL LEU GLU GLN ALA PRO PRO GLN ALA VAL TRP
SEQRES 7 C 257 LEU GLY TRP SER LEU GLY GLY LEU VAL ALA SER GLN VAL
SEQRES 8 C 257 ALA ILE MET ARG PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 C 257 VAL ALA SER SER PRO CYS PHE ALA ALA ARG ASP ASP TRP
SEQRES 10 C 257 PRO GLY ILE LYS PRO GLU VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 C 257 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 C 257 LEU ALA LEU GLN THR MET GLY THR GLU SER ALA ARG GLN
SEQRES 13 C 257 ASP ALA ARG ALA LEU LYS GLN ALA VAL LEU SER LEU PRO
SEQRES 14 C 257 MET PRO SER ALA GLU ALA LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 C 257 LEU ARG THR VAL ASP LEU ARG GLN ALA LEU VAL ARG LEU
SEQRES 16 C 257 PRO MET PRO PHE LEU ARG LEU TYR GLY ARG LEU ASP GLY
SEQRES 17 C 257 LEU VAL PRO ARG LYS ILE VAL PRO LEU LEU ASP ASP LEU
SEQRES 18 C 257 TRP PRO GLU SER GLU SER ILE LEU PHE ASP LYS ALA ALA
SEQRES 19 C 257 HIS ALA PRO PHE VAL SER HIS PRO ALA ALA PHE CYS GLU
SEQRES 20 C 257 PRO LEU LEU ALA LEU LYS THR ARG LEU GLY
SEQRES 1 D 257 MET ASN ASP ILE TRP TRP GLN THR ILE GLY GLU GLY ASP
SEQRES 2 D 257 CYS HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 D 257 GLN VAL TRP ASP CYS ILE THR PRO GLN LEU ALA SER HIS
SEQRES 4 D 257 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY TYR GLY ARG
SEQRES 5 D 257 SER GLY GLY PHE GLY ALA MET SER LEU GLU ALA MET ALA
SEQRES 6 D 257 GLN ARG VAL LEU GLU GLN ALA PRO PRO GLN ALA VAL TRP
SEQRES 7 D 257 LEU GLY TRP SER LEU GLY GLY LEU VAL ALA SER GLN VAL
SEQRES 8 D 257 ALA ILE MET ARG PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 D 257 VAL ALA SER SER PRO CYS PHE ALA ALA ARG ASP ASP TRP
SEQRES 10 D 257 PRO GLY ILE LYS PRO GLU VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 D 257 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 D 257 LEU ALA LEU GLN THR MET GLY THR GLU SER ALA ARG GLN
SEQRES 13 D 257 ASP ALA ARG ALA LEU LYS GLN ALA VAL LEU SER LEU PRO
SEQRES 14 D 257 MET PRO SER ALA GLU ALA LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 D 257 LEU ARG THR VAL ASP LEU ARG GLN ALA LEU VAL ARG LEU
SEQRES 16 D 257 PRO MET PRO PHE LEU ARG LEU TYR GLY ARG LEU ASP GLY
SEQRES 17 D 257 LEU VAL PRO ARG LYS ILE VAL PRO LEU LEU ASP ASP LEU
SEQRES 18 D 257 TRP PRO GLU SER GLU SER ILE LEU PHE ASP LYS ALA ALA
SEQRES 19 D 257 HIS ALA PRO PHE VAL SER HIS PRO ALA ALA PHE CYS GLU
SEQRES 20 D 257 PRO LEU LEU ALA LEU LYS THR ARG LEU GLY
SEQRES 1 E 257 MET ASN ASP ILE TRP TRP GLN THR ILE GLY GLU GLY ASP
SEQRES 2 E 257 CYS HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 E 257 GLN VAL TRP ASP CYS ILE THR PRO GLN LEU ALA SER HIS
SEQRES 4 E 257 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY TYR GLY ARG
SEQRES 5 E 257 SER GLY GLY PHE GLY ALA MET SER LEU GLU ALA MET ALA
SEQRES 6 E 257 GLN ARG VAL LEU GLU GLN ALA PRO PRO GLN ALA VAL TRP
SEQRES 7 E 257 LEU GLY TRP SER LEU GLY GLY LEU VAL ALA SER GLN VAL
SEQRES 8 E 257 ALA ILE MET ARG PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 E 257 VAL ALA SER SER PRO CYS PHE ALA ALA ARG ASP ASP TRP
SEQRES 10 E 257 PRO GLY ILE LYS PRO GLU VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 E 257 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 E 257 LEU ALA LEU GLN THR MET GLY THR GLU SER ALA ARG GLN
SEQRES 13 E 257 ASP ALA ARG ALA LEU LYS GLN ALA VAL LEU SER LEU PRO
SEQRES 14 E 257 MET PRO SER ALA GLU ALA LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 E 257 LEU ARG THR VAL ASP LEU ARG GLN ALA LEU VAL ARG LEU
SEQRES 16 E 257 PRO MET PRO PHE LEU ARG LEU TYR GLY ARG LEU ASP GLY
SEQRES 17 E 257 LEU VAL PRO ARG LYS ILE VAL PRO LEU LEU ASP ASP LEU
SEQRES 18 E 257 TRP PRO GLU SER GLU SER ILE LEU PHE ASP LYS ALA ALA
SEQRES 19 E 257 HIS ALA PRO PHE VAL SER HIS PRO ALA ALA PHE CYS GLU
SEQRES 20 E 257 PRO LEU LEU ALA LEU LYS THR ARG LEU GLY
SEQRES 1 F 257 MET ASN ASP ILE TRP TRP GLN THR ILE GLY GLU GLY ASP
SEQRES 2 F 257 CYS HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 F 257 GLN VAL TRP ASP CYS ILE THR PRO GLN LEU ALA SER HIS
SEQRES 4 F 257 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY TYR GLY ARG
SEQRES 5 F 257 SER GLY GLY PHE GLY ALA MET SER LEU GLU ALA MET ALA
SEQRES 6 F 257 GLN ARG VAL LEU GLU GLN ALA PRO PRO GLN ALA VAL TRP
SEQRES 7 F 257 LEU GLY TRP SER LEU GLY GLY LEU VAL ALA SER GLN VAL
SEQRES 8 F 257 ALA ILE MET ARG PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 F 257 VAL ALA SER SER PRO CYS PHE ALA ALA ARG ASP ASP TRP
SEQRES 10 F 257 PRO GLY ILE LYS PRO GLU VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 F 257 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 F 257 LEU ALA LEU GLN THR MET GLY THR GLU SER ALA ARG GLN
SEQRES 13 F 257 ASP ALA ARG ALA LEU LYS GLN ALA VAL LEU SER LEU PRO
SEQRES 14 F 257 MET PRO SER ALA GLU ALA LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 F 257 LEU ARG THR VAL ASP LEU ARG GLN ALA LEU VAL ARG LEU
SEQRES 16 F 257 PRO MET PRO PHE LEU ARG LEU TYR GLY ARG LEU ASP GLY
SEQRES 17 F 257 LEU VAL PRO ARG LYS ILE VAL PRO LEU LEU ASP ASP LEU
SEQRES 18 F 257 TRP PRO GLU SER GLU SER ILE LEU PHE ASP LYS ALA ALA
SEQRES 19 F 257 HIS ALA PRO PHE VAL SER HIS PRO ALA ALA PHE CYS GLU
SEQRES 20 F 257 PRO LEU LEU ALA LEU LYS THR ARG LEU GLY
FORMUL 7 HOH *584(H2 O)
HELIX 1 AA1 ASN A 25 ASP A 30 5 6
HELIX 2 AA2 ILE A 32 ALA A 37 1 6
HELIX 3 AA3 TYR A 50 GLY A 54 5 5
HELIX 4 AA4 SER A 60 GLU A 70 1 11
HELIX 5 AA5 SER A 82 ARG A 95 1 14
HELIX 6 AA6 LYS A 121 ASP A 135 1 15
HELIX 7 AA7 ASP A 135 LEU A 146 1 12
HELIX 8 AA8 SER A 153 SER A 167 1 15
HELIX 9 AA9 SER A 172 VAL A 186 1 15
HELIX 10 AB1 VAL A 215 ASP A 219 1 5
HELIX 11 AB2 ALA A 236 HIS A 241 1 6
HELIX 12 AB3 HIS A 241 GLY A 257 1 17
HELIX 13 AB4 ASN B 25 ASP B 30 5 6
HELIX 14 AB5 ILE B 32 ALA B 37 1 6
HELIX 15 AB6 SER B 60 GLN B 71 1 12
HELIX 16 AB7 SER B 82 ARG B 95 1 14
HELIX 17 AB8 LYS B 121 ASP B 135 1 15
HELIX 18 AB9 ASP B 135 MET B 149 1 15
HELIX 19 AC1 SER B 153 SER B 167 1 15
HELIX 20 AC2 SER B 172 VAL B 186 1 15
HELIX 21 AC3 ARG B 189 VAL B 193 5 5
HELIX 22 AC4 VAL B 215 ASP B 219 1 5
HELIX 23 AC5 ALA B 236 HIS B 241 1 6
HELIX 24 AC6 HIS B 241 GLY B 257 1 17
HELIX 25 AC7 ASN C 25 ASP C 30 5 6
HELIX 26 AC8 ILE C 32 ALA C 37 1 6
HELIX 27 AC9 SER C 60 GLU C 70 1 11
HELIX 28 AD1 SER C 82 ARG C 95 1 14
HELIX 29 AD2 LYS C 121 GLN C 129 1 9
HELIX 30 AD3 VAL C 140 GLU C 141 5 2
HELIX 31 AD4 PHE C 143 THR C 148 5 6
HELIX 32 AD5 SER C 153 SER C 167 1 15
HELIX 33 AD6 SER C 172 VAL C 186 1 15
HELIX 34 AD7 ARG C 189 VAL C 193 5 5
HELIX 35 AD8 ALA C 236 HIS C 241 1 6
HELIX 36 AD9 HIS C 241 GLY C 257 1 17
HELIX 37 AE1 ASN D 25 CYS D 31 5 7
HELIX 38 AE2 ILE D 32 SER D 38 1 7
HELIX 39 AE3 SER D 60 GLN D 71 1 12
HELIX 40 AE4 SER D 82 ARG D 95 1 14
HELIX 41 AE5 LYS D 121 ASP D 135 1 15
HELIX 42 AE6 ASP D 135 MET D 149 1 15
HELIX 43 AE7 SER D 153 SER D 167 1 15
HELIX 44 AE8 SER D 172 VAL D 186 1 15
HELIX 45 AE9 LYS D 213 ASP D 219 1 7
HELIX 46 AF1 ALA D 236 HIS D 241 1 6
HELIX 47 AF2 HIS D 241 GLY D 257 1 17
HELIX 48 AF3 ASN E 25 ASP E 30 5 6
HELIX 49 AF4 ILE E 32 ALA E 37 1 6
HELIX 50 AF5 SER E 60 GLU E 70 1 11
HELIX 51 AF6 SER E 82 ARG E 95 1 14
HELIX 52 AF7 LYS E 121 ASP E 135 1 15
HELIX 53 AF8 ASP E 135 GLN E 147 1 13
HELIX 54 AF9 SER E 153 SER E 167 1 15
HELIX 55 AG1 SER E 172 VAL E 186 1 15
HELIX 56 AG2 ARG E 189 VAL E 193 5 5
HELIX 57 AG3 LYS E 213 LEU E 218 1 6
HELIX 58 AG4 ALA E 236 HIS E 241 1 6
HELIX 59 AG5 HIS E 241 LEU E 256 1 16
HELIX 60 AG6 ASN F 25 ASP F 30 5 6
HELIX 61 AG7 ILE F 32 ALA F 37 1 6
HELIX 62 AG8 TYR F 50 GLY F 54 5 5
HELIX 63 AG9 SER F 60 GLU F 70 1 11
HELIX 64 AH1 SER F 82 ARG F 95 1 14
HELIX 65 AH2 LYS F 121 LEU F 132 1 12
HELIX 66 AH3 LEU F 144 MET F 149 1 6
HELIX 67 AH4 SER F 153 VAL F 165 1 13
HELIX 68 AH5 SER F 172 VAL F 186 1 15
HELIX 69 AH6 ILE F 214 ASP F 219 1 6
HELIX 70 AH7 ALA F 236 HIS F 241 1 6
HELIX 71 AH8 HIS F 241 LEU F 256 1 16
SHEET 1 AA1 7 TRP A 6 ILE A 9 0
SHEET 2 AA1 7 THR A 41 VAL A 45 -1 O LEU A 44 N GLN A 7
SHEET 3 AA1 7 HIS A 15 LEU A 19 1 N LEU A 16 O HIS A 43
SHEET 4 AA1 7 ALA A 76 TRP A 81 1 O LEU A 79 N VAL A 17
SHEET 5 AA1 7 VAL A 99 VAL A 105 1 O VAL A 103 N TRP A 78
SHEET 6 AA1 7 PHE A 199 GLY A 204 1 O LEU A 200 N LEU A 102
SHEET 7 AA1 7 GLU A 226 PHE A 230 1 O GLU A 226 N ARG A 201
SHEET 1 AA2 7 TRP B 6 ILE B 9 0
SHEET 2 AA2 7 PHE B 40 VAL B 45 -1 O LEU B 44 N GLN B 7
SHEET 3 AA2 7 CYS B 14 LEU B 19 1 N LEU B 16 O HIS B 43
SHEET 4 AA2 7 ALA B 76 TRP B 81 1 O VAL B 77 N VAL B 17
SHEET 5 AA2 7 VAL B 99 VAL B 105 1 O GLN B 100 N ALA B 76
SHEET 6 AA2 7 PHE B 199 GLY B 204 1 O LEU B 202 N THR B 104
SHEET 7 AA2 7 GLU B 226 PHE B 230 1 O PHE B 230 N TYR B 203
SHEET 1 AA3 7 TRP C 6 ILE C 9 0
SHEET 2 AA3 7 THR C 41 VAL C 45 -1 O LEU C 44 N GLN C 7
SHEET 3 AA3 7 HIS C 15 LEU C 19 1 N LEU C 18 O HIS C 43
SHEET 4 AA3 7 ALA C 76 TRP C 81 1 O VAL C 77 N HIS C 15
SHEET 5 AA3 7 VAL C 99 VAL C 105 1 O VAL C 103 N GLY C 80
SHEET 6 AA3 7 PHE C 199 GLY C 204 1 O LEU C 202 N THR C 104
SHEET 7 AA3 7 GLU C 226 PHE C 230 1 O PHE C 230 N TYR C 203
SHEET 1 AA4 7 TRP D 6 ILE D 9 0
SHEET 2 AA4 7 PHE D 40 VAL D 45 -1 O LEU D 44 N GLN D 7
SHEET 3 AA4 7 CYS D 14 LEU D 19 1 N LEU D 16 O HIS D 43
SHEET 4 AA4 7 ALA D 76 TRP D 81 1 O LEU D 79 N VAL D 17
SHEET 5 AA4 7 VAL D 99 VAL D 105 1 O GLN D 100 N ALA D 76
SHEET 6 AA4 7 PHE D 199 GLY D 204 1 O LEU D 202 N THR D 104
SHEET 7 AA4 7 GLU D 226 PHE D 230 1 O GLU D 226 N ARG D 201
SHEET 1 AA5 7 TRP E 6 ILE E 9 0
SHEET 2 AA5 7 THR E 41 VAL E 45 -1 O LEU E 42 N ILE E 9
SHEET 3 AA5 7 HIS E 15 LEU E 19 1 N LEU E 16 O HIS E 43
SHEET 4 AA5 7 ALA E 76 TRP E 81 1 O VAL E 77 N VAL E 17
SHEET 5 AA5 7 VAL E 99 VAL E 105 1 O VAL E 103 N TRP E 78
SHEET 6 AA5 7 PHE E 199 GLY E 204 1 O LEU E 200 N LEU E 102
SHEET 7 AA5 7 GLU E 226 PHE E 230 1 O PHE E 230 N TYR E 203
SHEET 1 AA6 7 TRP F 6 ILE F 9 0
SHEET 2 AA6 7 PHE F 40 VAL F 45 -1 O LEU F 44 N GLN F 7
SHEET 3 AA6 7 CYS F 14 LEU F 19 1 N LEU F 16 O THR F 41
SHEET 4 AA6 7 ALA F 76 TRP F 81 1 O VAL F 77 N VAL F 17
SHEET 5 AA6 7 VAL F 99 VAL F 105 1 O GLN F 100 N ALA F 76
SHEET 6 AA6 7 PHE F 199 GLY F 204 1 O LEU F 200 N LEU F 102
SHEET 7 AA6 7 SER F 227 PHE F 230 1 O ILE F 228 N ARG F 201
SSBOND 1 CYS A 31 CYS E 31 1555 1555 2.00
SSBOND 2 CYS C 31 CYS F 31 1555 1555 2.08
CRYST1 107.642 109.531 292.857 90.00 90.00 90.00 C 2 2 21 48
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 0.009290 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009130 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003415 0.00000
TER 1967 GLY A 257
TER 3917 GLY B 257
TER 5798 GLY C 257
TER 7778 GLY D 257
TER 9736 GLY E 257
TER 11548 LEU F 256
MASTER 434 0 0 71 42 0 0 612034 6 4 120
END
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