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HEADER SERINE HYDROLASE 04-FEB-98 1JKM
TITLE BREFELDIN A ESTERASE, A BACTERIAL HOMOLOGUE OF HUMAN
TITLE 2 HORMONE SENSITIVE LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BREFELDIN A ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS SERINE HYDROLASE, DEGRADATION OF BREFELDIN A, ALPHA/BETA
KEYWDS 2 HYDROLASE FAMILY
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WEI,A.J.CARRERAS,P.SHEFFIELD,T.OSTERLUND,U.DEREWENDA,
AUTHOR 2 U.O.MATERN,Z.S.DEREWENDA
REVDAT 1 16-FEB-99 1JKM 0
JRNL AUTH Y.WEI,A.J.CARRERAS,P.SHEFFIELD,T.OSTERLUND,
JRNL AUTH 2 U.DEREWENDA,U.O.MATERN,Z.S.DEREWENDA
JRNL TITL CRYSTAL STRUCTURE OF BREFELDIN A ESTERASE, A
JRNL TITL 2 BACTERIAL HORMOLOGUE OF THE HUMAN HORMONE SENSITIVE
JRNL TITL 3 LIPASE
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 8.0
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 1.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 62664
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5012
REMARK 3 NUCLEIC ACID ATOMS : NULL
REMARK 3 HETEROGEN ATOMS : NULL
REMARK 3 SOLVENT ATOMS : 524
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.1 (MAIN CHAIN),
REMARK 3 23.4 (SIDE CHAIN)
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.013 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.028 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.033 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 9.2 ; 7.0
REMARK 3 STAGGERED (DEGREES) : 21.0 ; 15.0
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.301 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.390 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.846 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.216 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JKM COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 20
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DESY-EMBL,HAMBURG
REMARK 200 BEAMLINE : WB7, X31
REMARK 200 X-RAY GENERATOR MODEL : SIEMENS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : MULTIWIRE AND IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : SIEMENS AND MAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN AND DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, CCP4 SUITE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62664
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.85
REMARK 200 RESOLUTION RANGE LOW (A) : 20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86
REMARK 200 DATA REDUNDANCY : 1.8
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.108
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHELX90, CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE AS MAJOR
REMARK 280 PRECIPITANT AT PH=6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 70.35317
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.29842
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.35317
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.29842
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 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 CA ALA B 48 CD ARG A 217 2656 0.12
REMARK 500 C VAL B 337 NH1 ARG A 295 2656 0.17
REMARK 500 CE1 PHE B 259 CA GLY A 296 2656 0.34
REMARK 500 O HOH 408 CB HIS B 346 2656 0.36
REMARK 500 NH1 ARG B 15 O PHE A 288 2656 0.37
REMARK 500 CB ASP B 43 CD1 LEU A 321 2656 0.37
REMARK 500 O HOH 516 N GLU B 261 2656 0.41
REMARK 500 CA ARG B 218 CA ALA B 215 2655 0.41
REMARK 500 CA PRO B 83 CB ASP B 81 2656 0.42
REMARK 500 C ALA B 38 N PHE A 300 2656 0.43
REMARK 500 CG PRO B 83 N ASP B 81 2656 0.46
REMARK 500 CD1 LEU B 42 C LEU A 297 2656 0.48
REMARK 500 C VAL B 34 CG2 VAL A 328 2656 0.51
REMARK 500 CG MET B 33 O ALA A 322 2656 0.52
REMARK 500 O HOH 507 OD2 ASP B 26 2656 0.52
REMARK 500 CD2 LEU B 37 CG2 VAL A 326 2656 0.53
REMARK 500 CG1 VAL B 337 CA ALA A 324 2656 0.58
REMARK 500 CD PRO B 309 OD1 ASP A 292 2656 0.58
REMARK 500 O HOH 495 CG PRO B 27 2656 0.58
REMARK 500 N ALA B 351 OE2 GLU B 35 2656 0.59
REMARK 500 CA ALA B 36 CA ASP A 327 2656 0.59
REMARK 500 CB PHE B 259 CA ARG A 295 2656 0.60
REMARK 500 O SER B 20 O TYR A 287 2656 0.60
REMARK 500 C GLY B 41 CE1 PHE A 300 2656 0.60
REMARK 500 CG TYR B 258 CA GLU A 291 2656 0.60
REMARK 500 CG2 VAL B 337 O ALA A 324 2656 0.62
REMARK 500 CA GLY B 257 CB GLU A 293 2656 0.64
REMARK 500 O HOH 358 CD1 PHE B 344 2656 0.66
REMARK 500 C GLU B 35 N VAL A 328 2656 0.69
REMARK 500 O VAL B 45 CD1 LEU A 213 2656 0.70
REMARK 500 N GLY B 22 NH1 ARG A 320 2656 0.71
REMARK 500 N LEU B 221 NE ARG B 218 2655 0.72
REMARK 500 O PRO B 23 N ARG A 320 2656 0.74
REMARK 500 C ALA B 36 N ASP A 327 2656 0.75
REMARK 500 O TRP B 347 O TRP B 347 2656 0.77
REMARK 500 CG PHE B 259 C ARG A 295 2656 0.77
REMARK 500 O HOH 130 CD1 PHE A 317 2656 0.77
REMARK 500 O HOH 189 CA ASN B 255 2656 0.78
REMARK 500 CD1 PHE B 259 N GLY A 296 2656 0.80
REMARK 500 CG PHE B 259 N GLY A 296 2656 0.82
REMARK 500 N THR B 25 O ALA A 316 2656 0.82
REMARK 500 O HOH 426 CA PRO B 27 2656 0.83
REMARK 500 O HOH 95 CA PRO B 31 2656 0.86
REMARK 500 O HOH 139 CB ARG A 319 2656 0.86
REMARK 500 C ARG B 24 C ALA A 316 2656 0.86
REMARK 500 CB PHE B 40 CA PRO A 298 2656 0.87
REMARK 500 O HOH 35 C PHE B 29 2656 0.87
REMARK 500 CA LEU B 37 CG1 VAL A 326 2656 0.88
REMARK 500 O HOH 269 N SER B 21 2656 0.88
REMARK 500 N GLY B 22 CZ ARG A 320 2656 0.88
REMARK 500 O ALA B 38 CA PHE A 300 2656 0.88
REMARK 500 N THR B 25 C ALA A 316 2656 0.89
REMARK 500 O GLY B 41 CZ PHE A 300 2656 0.89
REMARK 500 O HOH 189 CB ASN B 255 2656 0.89
REMARK 500 CA GLY B 22 NH1 ARG A 320 2656 0.89
REMARK 500 O HOH 176 CD PRO B 31 2656 0.89
REMARK 500 OD1 ASP B 43 CD2 PHE A 300 2656 0.91
REMARK 500 CB TYR B 258 C GLU A 291 2656 0.91
REMARK 500 CG LEU B 42 CB LEU A 297 2656 0.92
REMARK 500 CB THR B 39 CB PRO A 299 2656 0.92
REMARK 500 O HOH 35 O PHE B 29 2656 0.92
REMARK 500 O HOH 439 CB SER B 77 2656 0.93
REMARK 500 O HOH 351 CD2 LEU B 214 2655 0.94
REMARK 500 CE2 PHE B 29 O ARG A 320 2656 0.95
REMARK 500 N PHE B 259 C LEU A 294 2656 0.96
REMARK 500 O HOH 296 CG LEU B 221 2655 0.97
REMARK 500 CG2 VAL B 45 CB ALA A 289 2656 0.97
REMARK 500 C ARG B 220 CD ARG B 218 2655 0.97
REMARK 500 CD2 TYR B 258 CB GLU A 291 2656 0.98
REMARK 500 O HOH 370 CA ALA B 350 2656 0.99
REMARK 500 CE MET B 33 CA GLY A 325 2656 1.00
REMARK 500 O ASP B 26 NH1 ARG A 323 2656 1.00
REMARK 500 N ARG B 218 C ALA B 215 2655 1.02
REMARK 500 O HOH 118 CZ PHE B 344 2656 1.02
REMARK 500 CB SER B 30 CB SER B 30 2656 1.02
REMARK 500 CA ARG B 24 C PHE A 317 2656 1.03
REMARK 500 N THR B 39 N PHE A 300 2656 1.04
REMARK 500 O HOH 358 CE1 PHE B 344 2656 1.04
REMARK 500 N LEU B 221 CD ARG B 218 2655 1.04
REMARK 500 N SER B 20 CD1 PHE A 288 2656 1.04
REMARK 500 N PRO B 309 OD1 ASP A 292 2656 1.04
REMARK 500 CD PRO B 50 CG ARG A 218 2656 1.05
REMARK 500 CB VAL B 45 CB ALA A 289 2656 1.05
REMARK 500 CB PHE B 29 O ARG A 319 2656 1.05
REMARK 500 O HOH 482 OE1 GLU A 293 2656 1.06
REMARK 500 CA ALA B 44 CZ PHE A 317 2656 1.06
REMARK 500 N LEU B 42 CE1 PHE A 300 2656 1.07
REMARK 500 O PRO B 83 OD2 ASP B 81 2656 1.07
REMARK 500 CB SER B 30 CA SER B 30 2656 1.07
REMARK 500 O HOH 224 CE LYS A 216 2656 1.07
REMARK 500 O HOH 262 N ASP B 26 2656 1.07
REMARK 500 CA GLU B 35 O VAL A 328 2656 1.08
REMARK 500 O HOH 237 CA LEU B 348 2656 1.08
REMARK 500 CA PHE B 259 N ARG A 295 2656 1.08
REMARK 500 N ARG B 217 N ARG B 217 2655 1.09
REMARK 500 CB PHE B 40 CB PRO A 298 2656 1.10
REMARK 500 CD PRO B 83 C ASP B 81 2656 1.10
REMARK 500 O HOH 224 CD LYS A 216 2656 1.10
REMARK 500 CD PRO B 50 CD ARG A 218 2656 1.10
REMARK 500 O GLU B 35 C ASP A 327 2656 1.11
REMARK 500 CZ ARG B 217 NZ LYS B 216 2655 1.11
REMARK 500 C ALA B 350 OE2 GLU B 35 2656 1.12
REMARK 500 C ARG B 24 O ALA A 316 2656 1.12
REMARK 500 O HOH 516 CA GLU B 261 2656 1.12
REMARK 500 CD1 LEU B 42 CA LEU A 297 2656 1.12
REMARK 500 CG LEU B 37 CB VAL A 326 2656 1.13
REMARK 500 O HOH 237 N LEU B 348 2656 1.13
REMARK 500 CB MET B 33 O ALA A 322 2656 1.14
REMARK 500 N ARG B 24 O PHE A 317 2656 1.14
REMARK 500 CB LEU B 37 CB VAL A 326 2656 1.15
REMARK 500 N LEU B 37 C VAL A 326 2656 1.15
REMARK 500 CD PRO B 83 O ASP B 81 2656 1.15
REMARK 500 CB ASP B 26 NH2 ARG A 323 2656 1.15
REMARK 500 CB LEU B 42 CB LEU A 297 2656 1.16
REMARK 500 NH1 ARG B 217 NZ LYS B 216 2655 1.16
REMARK 500 C ALA B 36 CA ASP A 327 2656 1.17
REMARK 500 CG PRO B 83 CA ASP B 81 2656 1.17
REMARK 500 C ALA B 38 CA PHE A 300 2656 1.17
REMARK 500 N ALA B 48 NE ARG A 217 2656 1.18
REMARK 500 CB GLU B 35 O VAL A 328 2656 1.18
REMARK 500 O VAL B 34 CG2 VAL A 328 2656 1.18
REMARK 500 O SER B 20 C TYR A 287 2656 1.19
REMARK 500 CA PHE B 259 C LEU A 294 2656 1.20
REMARK 500 CG TYR B 258 N GLU A 291 2656 1.21
REMARK 500 N ARG B 24 C PHE A 317 2656 1.21
REMARK 500 CD1 PHE B 40 CD PRO A 299 2656 1.21
REMARK 500 N PHE B 259 N ARG A 295 2656 1.22
REMARK 500 CG ASP B 26 NH2 ARG A 323 2656 1.22
REMARK 500 CG2 THR B 39 CG PRO A 299 2656 1.22
REMARK 500 CA SER B 30 CA SER B 30 2656 1.23
REMARK 500 CZ PHE B 259 CA GLY A 296 2656 1.23
REMARK 500 CD2 TYR B 258 CA GLU A 291 2656 1.24
REMARK 500 O HOH 420 CZ PHE B 40 2656 1.24
REMARK 500 N PHE B 40 N PRO A 299 2656 1.24
REMARK 500 O ALA B 38 N PHE A 300 2656 1.24
REMARK 500 CD PRO B 309 CG ASP A 292 2656 1.24
REMARK 500 CZ ARG B 217 CE LYS B 216 2655 1.24
REMARK 500 CB TYR B 258 O GLU A 291 2656 1.24
REMARK 500 O HOH 223 NH2 ARG B 15 2656 1.25
REMARK 500 CE1 PHE B 259 C GLY A 296 2656 1.25
REMARK 500 CD ARG B 217 CG LYS B 216 2655 1.26
REMARK 500 O HOH 291 CA ALA B 32 2656 1.26
REMARK 500 CG LEU B 42 CA LEU A 297 2656 1.27
REMARK 500 O HOH 331 O ARG B 28 2656 1.27
REMARK 500 NE ARG B 217 CE LYS B 216 2655 1.27
REMARK 500 CB PRO B 83 CA ASP B 81 2656 1.28
REMARK 500 O HOH 38 NE ARG A 295 2656 1.28
REMARK 500 N PHE B 259 CA LEU A 294 2656 1.28
REMARK 500 CB ARG B 24 N ALA A 318 2656 1.28
REMARK 500 C ALA B 66 O GLY A 219 2656 1.29
REMARK 500 CB TYR B 258 CA GLU A 291 2656 1.29
REMARK 500 O HOH 111 CE2 PHE B 40 2656 1.29
REMARK 500 O HOH 320 O HOH 231 2656 1.29
REMARK 500 O HOH 161 O ALA B 32 2656 1.30
REMARK 500 CB PRO B 23 N LEU A 321 2656 1.31
REMARK 500 O HOH 262 C THR B 25 2656 1.31
REMARK 500 N PRO B 309 CG ASP A 292 2656 1.31
REMARK 500 O HOH 130 CG PHE A 317 2656 1.32
REMARK 500 CA ARG B 218 C ALA B 215 2655 1.32
REMARK 500 CD1 PHE B 259 CA GLY A 296 2656 1.32
REMARK 500 CG PRO B 83 C LEU B 80 2656 1.32
REMARK 500 N PRO B 49 CB ARG A 217 2656 1.32
REMARK 500 C ASP B 256 OG SER A 290 2656 1.32
REMARK 500 N HIS B 338 NH1 ARG A 295 2656 1.32
REMARK 500 CA THR B 39 CB PRO A 299 2656 1.32
REMARK 500 CA ALA B 38 CB PHE A 300 2656 1.33
REMARK 500 CD1 TYR B 258 C SER A 290 2656 1.33
REMARK 500 O HOH 291 C ALA B 32 2656 1.33
REMARK 500 CA THR B 39 CA PRO A 299 2656 1.34
REMARK 500 NH1 ARG B 15 C PHE A 288 2656 1.34
REMARK 500 CD1 LEU B 42 O LEU A 297 2656 1.36
REMARK 500 CD2 LEU B 42 CB LEU A 297 2656 1.36
REMARK 500 O VAL B 34 CB VAL A 328 2656 1.36
REMARK 500 O HOH 296 CB LEU B 221 2655 1.36
REMARK 500 CA GLU B 35 C VAL A 328 2656 1.36
REMARK 500 O ARG B 24 O ILE A 315 2656 1.36
REMARK 500 CG2 THR B 39 CB PRO A 299 2656 1.37
REMARK 500 O GLU B 35 N VAL A 328 2656 1.38
REMARK 500 CB ARG B 217 CB LYS B 216 2655 1.38
REMARK 500 O VAL B 337 NH1 ARG A 295 2656 1.38
REMARK 500 CB PHE B 259 C ARG A 295 2656 1.38
REMARK 500 CA ASP B 43 CD2 LEU A 321 2656 1.38
REMARK 500 CD1 TYR B 258 N GLU A 291 2656 1.38
REMARK 500 CB PHE B 259 N ARG A 295 2656 1.38
REMARK 500 CA ARG B 24 N ALA A 318 2656 1.38
REMARK 500 CB PRO B 83 N ASP B 81 2656 1.39
REMARK 500 CB ARG B 24 C PHE A 317 2656 1.39
REMARK 500 O HOH 223 CZ ARG B 15 2656 1.39
REMARK 500 O GLY B 257 N LEU A 294 2656 1.40
REMARK 500 N LEU B 37 N ASP A 327 2656 1.40
REMARK 500 CA ASP B 43 CG LEU A 321 2656 1.40
REMARK 500 CA VAL B 337 NH1 ARG A 295 2656 1.40
REMARK 500 C THR B 39 C PRO A 299 2656 1.40
REMARK 500 C THR B 39 CA PRO A 299 2656 1.40
REMARK 500 O HOH 120 CD1 TRP B 347 2656 1.40
REMARK 500 O ASN B 255 N ASP A 292 2656 1.41
REMARK 500 CG PRO B 50 CD ARG A 218 2656 1.42
REMARK 500 NE ARG B 24 CG2 VAL A 302 2656 1.42
REMARK 500 C ARG B 217 N LYS B 216 2655 1.42
REMARK 500 CG2 VAL B 34 O ALA A 318 2656 1.42
REMARK 500 C GLU B 19 CD1 PHE A 288 2656 1.42
REMARK 500 CA VAL B 337 CZ ARG A 295 2656 1.42
REMARK 500 CZ ARG B 15 O PHE A 288 2656 1.43
REMARK 500 C ARG B 218 CA ALA B 215 2655 1.43
REMARK 500 C THR B 39 O PRO A 299 2656 1.43
REMARK 500 CB PHE B 40 C PRO A 298 2656 1.43
REMARK 500 O ALA B 46 OE2 GLU A 293 2656 1.43
REMARK 500 CA ALA B 46 CD2 LEU A 213 2656 1.43
REMARK 500 CA VAL B 34 CG2 VAL A 328 2656 1.43
REMARK 500 CE MET B 33 C GLY A 325 2656 1.44
REMARK 500 C VAL B 337 CZ ARG A 295 2656 1.44
REMARK 500 O HOH 471 CG1 ILE B 78 2656 1.44
REMARK 500 CD1 LEU B 37 O LEU A 321 2656 1.45
REMARK 500 CA ASP B 43 CD1 LEU A 321 2656 1.45
REMARK 500 C GLU B 35 C ASP A 327 2656 1.45
REMARK 500 CA ALA B 48 NE ARG A 217 2656 1.45
REMARK 500 O GLY B 41 CE1 PHE A 300 2656 1.45
REMARK 500 O HOH 358 CG PHE B 344 2656 1.45
REMARK 500 C GLY B 41 CZ PHE A 300 2656 1.46
REMARK 500 CD PRO B 83 CA ASP B 81 2656 1.46
REMARK 500 N ASP B 256 OG SER A 290 2656 1.46
REMARK 500 O ASP B 256 OG SER A 290 2656 1.46
REMARK 500 O HOH 291 N MET B 33 2656 1.46
REMARK 500 CB ARG B 217 CA LYS B 216 2655 1.47
REMARK 500 CD2 LEU B 42 CG LEU A 297 2656 1.47
REMARK 500 O HOH 370 C ALA B 350 2656 1.47
REMARK 500 N PRO B 83 CB ASP B 81 2656 1.47
REMARK 500 O ALA B 66 O GLY A 219 2656 1.48
REMARK 500 CD PRO B 23 CD1 LEU A 294 2656 1.48
REMARK 500 O ILE B 260 O ASP A 292 2656 1.48
REMARK 500 OE2 GLU B 19 OE1 GLU A 280 2656 1.49
REMARK 500 CB VAL B 337 O ALA A 324 2656 1.49
REMARK 500 OG SER B 20 CD2 TYR A 287 2656 1.49
REMARK 500 O HOH 224 CG LYS A 216 2656 1.49
REMARK 500 C ARG B 28 CD ARG A 323 2656 1.49
REMARK 500 O VAL B 45 CG LEU A 213 2656 1.50
REMARK 500 CD2 LEU B 42 CA LEU A 297 2656 1.50
REMARK 500 CG ARG B 218 O ALA B 215 2655 1.50
REMARK 500 CB SER B 30 C SER B 30 2656 1.51
REMARK 500 CG PHE B 40 CA PRO A 298 2656 1.51
REMARK 500 C SER B 20 O TYR A 287 2656 1.52
REMARK 500 CG1 VAL B 337 C ALA A 324 2656 1.52
REMARK 500 CA PHE B 29 CG ARG A 323 2656 1.52
REMARK 500 CA PRO B 83 CG ASP B 81 2656 1.52
REMARK 500 CA ASP B 256 OG SER A 290 2656 1.52
REMARK 500 O ARG B 24 C ALA A 316 2656 1.52
REMARK 500 CG ARG B 24 N ALA A 318 2656 1.52
REMARK 500 O GLU B 35 O ASP A 327 2656 1.52
REMARK 500 N PHE B 29 CD ARG A 323 2656 1.52
REMARK 500 CB ARG B 218 O ALA B 215 2655 1.52
REMARK 500 CZ3 TRP B 347 OD2 ASP A 327 2656 1.53
REMARK 500 CB PRO B 349 CD2 HIS B 346 2656 1.54
REMARK 500 C ALA B 48 CD ARG A 217 2656 1.54
REMARK 500 O HOH 238 CA ARG B 220 2655 1.54
REMARK 500 N ALA B 36 N VAL A 328 2656 1.54
REMARK 500 C ARG B 24 N PHE A 317 2656 1.54
REMARK 500 N ALA B 48 CD ARG A 217 2656 1.54
REMARK 500 CD2 TYR B 258 CG GLU A 291 2656 1.54
REMARK 500 CB THR B 25 CB ALA A 316 2656 1.55
REMARK 500 CD2 PHE B 29 O ARG A 320 2656 1.55
REMARK 500 CG1 VAL B 337 CB ALA A 324 2656 1.55
REMARK 500 CB LEU B 37 CG1 VAL A 326 2656 1.55
REMARK 500 CB PRO B 83 CB ASP B 81 2656 1.55
REMARK 500 O HOH 227 CH2 TRP B 347 2656 1.55
REMARK 500 N THR B 39 C PRO A 299 2656 1.55
REMARK 500 N PHE B 40 C PRO A 299 2656 1.55
REMARK 500 N PHE B 40 CA PRO A 299 2656 1.56
REMARK 500 N HIS B 338 CZ ARG A 295 2656 1.56
REMARK 500 N ALA B 350 NE1 TRP B 347 2656 1.56
REMARK 500 CB ALA B 48 NH1 ARG A 217 2656 1.56
REMARK 500 O HOH 388 CE3 TRP B 347 2656 1.56
REMARK 500 O HOH 464 CB LEU B 178 2655 1.56
REMARK 500 CB ALA B 48 CD ARG A 217 2656 1.56
REMARK 500 N PHE B 40 O PRO A 299 2656 1.56
REMARK 500 CB ARG B 24 CA PHE A 317 2656 1.56
REMARK 500 O GLY B 257 C GLU A 293 2656 1.56
REMARK 500 O HOH 426 CB PRO B 27 2656 1.56
REMARK 500 N VAL B 34 CB ALA A 322 2656 1.57
REMARK 500 N ARG B 218 CA ALA B 215 2655 1.57
REMARK 500 O ALA B 36 N ASP A 327 2656 1.57
REMARK 500 O PHE B 259 O ARG A 295 2656 1.57
REMARK 500 O HOH 119 CA LEU A 294 2656 1.57
REMARK 500 CA ARG B 217 O LEU B 213 2655 1.57
REMARK 500 O HOH 439 CA SER B 77 2656 1.57
REMARK 500 O HOH 139 CA ARG A 319 2656 1.57
REMARK 500 C SER B 21 NH1 ARG A 320 2656 1.58
REMARK 500 CZ PHE B 29 O ARG A 320 2656 1.58
REMARK 500 CD PRO B 50 NE ARG A 218 2656 1.58
REMARK 500 CA THR B 39 C PRO A 299 2656 1.58
REMARK 500 CD GLU B 19 OE1 GLU A 280 2656 1.58
REMARK 500 O ARG B 24 C ILE A 315 2656 1.58
REMARK 500 CA PRO B 309 OD2 ASP A 292 2656 1.58
REMARK 500 CD2 PHE B 259 N GLY A 296 2656 1.58
REMARK 500 O HOH 495 CD PRO B 27 2656 1.59
REMARK 500 OG SER B 30 OG SER B 30 2656 1.59
REMARK 500 CD1 PHE B 259 C ARG A 295 2656 1.59
REMARK 500 CA ALA B 48 CG ARG A 217 2656 1.59
REMARK 500 O HOH 119 CB LEU A 294 2656 1.59
REMARK 500 CG PHE B 40 CB PRO A 298 2656 1.59
REMARK 500 C LEU B 37 CG1 VAL A 326 2656 1.59
REMARK 500 N ALA B 351 CD GLU B 35 2656 1.60
REMARK 500 CD2 LEU B 37 CB VAL A 326 2656 1.60
REMARK 500 C VAL B 34 CB VAL A 328 2656 1.60
REMARK 500 N GLY B 22 NH2 ARG A 320 2656 1.60
REMARK 500 O HOH 525 C LEU B 348 2656 1.60
REMARK 500 CG LEU B 37 CG2 VAL A 326 2656 1.61
REMARK 500 O MET B 33 O VAL A 326 2656 1.61
REMARK 500 NH1 ARG B 217 CE LYS B 216 2655 1.61
REMARK 500 CD2 LEU B 307 OE1 GLU A 291 2656 1.61
REMARK 500 CA LEU B 37 CB VAL A 326 2656 1.61
REMARK 500 C ASP B 26 NH1 ARG A 323 2656 1.61
REMARK 500 O HOH 388 CZ3 TRP B 347 2656 1.61
REMARK 500 N LEU B 42 CD1 PHE A 300 2656 1.62
REMARK 500 OG SER B 30 CB SER B 30 2656 1.62
REMARK 500 O HOH 334 CB ALA B 79 2656 1.62
REMARK 500 CG MET B 33 C ALA A 322 2656 1.62
REMARK 500 O HOH 454 CB ASP B 292 2655 1.62
REMARK 500 O HOH 238 CG ARG B 220 2655 1.62
REMARK 500 CE1 PHE B 259 N GLY A 296 2656 1.62
REMARK 500 CB ARG B 217 C LYS B 216 2655 1.62
REMARK 500 O HOH 507 CG ASP B 26 2656 1.62
REMARK 500 CA ALA B 36 N ASP A 327 2656 1.62
REMARK 500 O HOH 483 O ARG B 345 2656 1.63
REMARK 500 CA ILE B 260 NZ LYS A 216 2656 1.63
REMARK 500 N GLY B 219 C LEU B 214 2655 1.63
REMARK 500 O ARG B 24 CA ALA A 316 2656 1.63
REMARK 500 O HOH 525 CA LEU B 348 2656 1.63
REMARK 500 CG PHE B 259 CA ARG A 295 2656 1.63
REMARK 500 OG SER B 20 CE2 TYR A 287 2656 1.63
REMARK 500 CG PRO B 49 O ARG A 217 2656 1.63
REMARK 500 N TYR B 258 N GLU A 293 2656 1.63
REMARK 500 N PRO B 83 C ASP B 81 2656 1.63
REMARK 500 CA VAL B 337 NH2 ARG A 295 2656 1.64
REMARK 500 NH2 ARG B 217 NZ LYS B 216 2655 1.64
REMARK 500 CG2 VAL B 337 C ALA A 324 2656 1.64
REMARK 500 CA ARG B 217 N ARG B 217 2655 1.64
REMARK 500 O HOH 516 C ILE B 260 2656 1.64
REMARK 500 O HOH 496 CD1 ILE B 78 2656 1.64
REMARK 500 CA GLY B 257 CA GLU A 293 2656 1.64
REMARK 500 N ARG B 218 N LYS B 216 2655 1.64
REMARK 500 CA GLU B 35 N VAL A 328 2656 1.64
REMARK 500 CG1 VAL B 45 CB ALA A 289 2656 1.64
REMARK 500 N PHE B 40 C PRO A 298 2656 1.64
REMARK 500 CB ALA B 44 CG2 ILE A 209 2656 1.65
REMARK 500 N PRO B 83 CA ASP B 81 2656 1.65
REMARK 500 N HIS B 338 NE ARG A 295 2656 1.65
REMARK 500 O HOH 269 CA SER B 21 2656 1.65
REMARK 500 N PRO B 309 OD2 ASP A 292 2656 1.65
REMARK 500 O HOH 426 N PRO B 27 2656 1.65
REMARK 500 CA ARG B 220 CD ARG B 218 2655 1.65
REMARK 500 C PHE B 259 O ARG A 295 2656 1.66
REMARK 500 CA THR B 25 CA ALA A 316 2656 1.66
REMARK 500 O HOH 237 C TRP B 347 2656 1.66
REMARK 500 O HOH 482 CD GLU A 293 2656 1.66
REMARK 500 N PHE B 29 CG ARG A 323 2656 1.66
REMARK 500 OD1 ASP B 43 CG PHE A 300 2656 1.67
REMARK 500 CA LEU B 221 NE ARG B 218 2655 1.67
REMARK 500 CA TYR B 258 O GLU A 291 2656 1.67
REMARK 500 CG2 THR B 25 CB ALA A 316 2656 1.67
REMARK 500 CA PHE B 259 O LEU A 294 2656 1.67
REMARK 500 O LEU B 42 CD2 LEU A 321 2656 1.68
REMARK 500 O HOH 407 O LEU B 348 2656 1.68
REMARK 500 C PRO B 23 N ARG A 320 2656 1.68
REMARK 500 CA PRO B 83 CA ASP B 81 2656 1.68
REMARK 500 CA GLU B 35 CA VAL A 328 2656 1.68
REMARK 500 CD2 TYR B 258 N GLU A 291 2656 1.69
REMARK 500 N HIS B 338 CD ARG A 295 2656 1.69
REMARK 500 O HOH 176 CG PRO B 31 2656 1.69
REMARK 500 O HOH 408 CG HIS B 346 2656 1.69
REMARK 500 C PRO B 23 O PHE A 317 2656 1.69
REMARK 500 N TYR B 258 O SER A 290 2656 1.69
REMARK 500 O HOH 332 CD2 LEU B 82 2656 1.69
REMARK 500 O PRO B 23 C ARG A 319 2656 1.70
REMARK 500 N VAL B 34 CA ALA A 322 2656 1.70
REMARK 500 N ALA B 47 CB LEU A 213 2656 1.70
REMARK 500 OD1 ASP B 26 NH2 ARG A 323 2656 1.70
REMARK 500 C SER B 21 CZ ARG A 320 2656 1.70
REMARK 500 O HOH 238 CB ARG B 220 2655 1.70
REMARK 500 N ALA B 46 CD2 LEU A 213 2656 1.71
REMARK 500 CB PRO B 49 C ARG A 217 2656 1.71
REMARK 500 CA SER B 20 CG PHE A 288 2656 1.71
REMARK 500 CA THR B 25 C ALA A 316 2656 1.71
REMARK 500 CA ALA B 38 CA PHE A 300 2656 1.72
REMARK 500 C TYR B 258 N ARG A 295 2656 1.72
REMARK 500 N PHE B 259 N LEU A 294 2656 1.72
REMARK 500 O HOH 189 N ASN B 255 2656 1.72
REMARK 500 CB THR B 39 CA PRO A 299 2656 1.72
REMARK 500 CD1 TYR B 258 O SER A 290 2656 1.72
REMARK 500 N ALA B 44 CZ PHE A 317 2656 1.72
REMARK 500 CA ARG B 24 CA PHE A 317 2656 1.72
REMARK 500 CA PHE B 40 C PRO A 298 2656 1.72
REMARK 500 CA ARG B 218 CB ALA B 215 2655 1.72
REMARK 500 O ALA B 44 CD2 LEU A 294 2656 1.72
REMARK 500 CD2 PHE B 29 N ARG A 323 2656 1.73
REMARK 500 C ALA B 36 C ASP A 327 2656 1.73
REMARK 500 N ALA B 36 CA ASP A 327 2656 1.73
REMARK 500 CA THR B 25 CB ALA A 316 2656 1.73
REMARK 500 CD ARG B 217 CD LYS B 216 2655 1.73
REMARK 500 CE3 TRP B 347 OD1 ASP A 327 2656 1.73
REMARK 500 C GLY B 257 CA GLU A 293 2656 1.73
REMARK 500 C ARG B 218 N ALA B 215 2655 1.73
REMARK 500 CG PRO B 23 CD1 LEU A 294 2656 1.73
REMARK 500 CB LEU B 307 OE1 GLU A 291 2656 1.73
REMARK 500 N GLY B 257 CB GLU A 293 2656 1.74
REMARK 500 O ALA B 38 C PRO A 299 2656 1.74
REMARK 500 O HOH 120 CG TRP B 347 2656 1.74
REMARK 500 C ALA B 38 C PRO A 299 2656 1.74
REMARK 500 CD2 LEU B 42 CD1 LEU A 297 2656 1.74
REMARK 500 CD PRO B 349 CA TRP B 347 2656 1.74
REMARK 500 C TYR B 258 O GLU A 291 2656 1.74
REMARK 500 N SER B 20 CE1 PHE A 288 2656 1.74
REMARK 500 CD1 LEU B 42 N PRO A 298 2656 1.74
REMARK 500 O HOH 335 O HOH 246 2656 1.75
REMARK 500 CD PRO B 83 N ASP B 81 2656 1.75
REMARK 500 O HOH 291 N ALA B 32 2656 1.75
REMARK 500 O ARG B 24 N ALA A 316 2656 1.75
REMARK 500 O TYR B 258 O GLU A 291 2656 1.75
REMARK 500 O ARG B 217 N ALA B 215 2655 1.75
REMARK 500 CA PRO B 23 CB ARG A 320 2656 1.75
REMARK 500 O PHE B 259 NZ LYS A 216 2656 1.76
REMARK 500 O HOH 469 O HOH 24 2656 1.76
REMARK 500 CH2 TRP B 347 OD2 ASP A 327 2656 1.76
REMARK 500 N GLU B 35 CG2 VAL A 328 2656 1.76
REMARK 500 C PRO B 83 OD2 ASP B 81 2656 1.76
REMARK 500 O HOH 417 CA MET B 33 2656 1.76
REMARK 500 C ALA B 36 C VAL A 326 2656 1.76
REMARK 500 CA ARG B 218 N ALA B 215 2655 1.76
REMARK 500 O GLY B 22 CB ARG A 320 2656 1.77
REMARK 500 CG2 VAL B 45 CA ALA A 289 2656 1.77
REMARK 500 O HOH 458 CG HIS B 346 2656 1.77
REMARK 500 N GLY B 219 N ALA B 215 2655 1.77
REMARK 500 CB MET B 33 C ALA A 322 2656 1.77
REMARK 500 O HOH 118 CE2 PHE B 344 2656 1.77
REMARK 500 O HOH 408 CA HIS B 346 2656 1.77
REMARK 500 CA SER B 20 CD1 PHE A 288 2656 1.77
REMARK 500 CB PRO B 83 CG ASP B 81 2656 1.77
REMARK 500 O HOH 38 CD ARG A 295 2656 1.77
REMARK 500 CZ ARG B 24 CB VAL A 302 2656 1.78
REMARK 500 O HOH 544 CD LYS B 216 2655 1.78
REMARK 500 CG LEU B 307 OE1 GLU A 291 2656 1.78
REMARK 500 O HOH 189 C ASN B 255 2656 1.78
REMARK 500 N ALA B 36 C ASP A 327 2656 1.78
REMARK 500 CA GLY B 41 CE1 PHE A 300 2656 1.78
REMARK 500 N ASP B 43 CD2 LEU A 321 2656 1.78
REMARK 500 O LYS B 216 CA LEU B 214 2655 1.78
REMARK 500 CD ARG B 217 CE LYS B 216 2655 1.79
REMARK 500 O PHE B 259 CE LYS A 216 2656 1.79
REMARK 500 CB THR B 39 CG PRO A 299 2656 1.79
REMARK 500 O HOH 439 N SER B 77 2656 1.79
REMARK 500 O HOH 223 NE ARG B 15 2656 1.79
REMARK 500 CA GLY B 335 CG PRO B 31 2656 1.80
REMARK 500 O ALA B 47 CG ARG A 217 2656 1.80
REMARK 500 C THR B 39 CB PRO A 299 2656 1.80
REMARK 500 O HOH 167 O HOH 87 2656 1.80
REMARK 500 CB ALA B 38 O PHE A 300 2656 1.80
REMARK 500 CD1 LEU B 307 CB ARG A 323 2656 1.80
REMARK 500 CE2 TYR B 258 CG GLU A 291 2656 1.81
REMARK 500 CB PRO B 50 NE ARG A 218 2656 1.81
REMARK 500 NH1 ARG B 24 CB ALA A 318 2656 1.81
REMARK 500 CA PRO B 23 C ARG A 320 2656 1.81
REMARK 500 C GLY B 257 N LEU A 294 2656 1.81
REMARK 500 C GLY B 257 C GLU A 293 2656 1.81
REMARK 500 O HOH 262 CA ASP B 26 2656 1.81
REMARK 500 CB VAL B 337 C ALA A 324 2656 1.82
REMARK 500 CG LEU B 42 C LEU A 297 2656 1.82
REMARK 500 O HOH 420 CE1 PHE B 40 2656 1.82
REMARK 500 N ARG B 218 O ALA B 215 2655 1.82
REMARK 500 O HOH 495 CB PRO B 27 2656 1.82
REMARK 500 CB ALA B 48 NE ARG A 217 2656 1.82
REMARK 500 O HOH 296 CD1 LEU B 221 2655 1.82
REMARK 500 O HOH 407 C PRO B 349 2656 1.82
REMARK 500 CG1 VAL B 34 O ALA A 318 2656 1.83
REMARK 500 OE1 GLU B 19 OE1 GLU A 280 2656 1.83
REMARK 500 CB ARG B 218 C ALA B 215 2655 1.83
REMARK 500 O HOH 249 O HOH 218 2656 1.83
REMARK 500 O HOH 358 CZ PHE B 344 2656 1.83
REMARK 500 O PHE B 40 CG PRO A 298 2656 1.83
REMARK 500 CA GLY B 22 CZ ARG A 320 2656 1.83
REMARK 500 N SER B 67 O GLY A 219 2656 1.83
REMARK 500 O HOH 35 N SER B 30 2656 1.83
REMARK 500 C GLY B 41 CD1 PHE A 300 2656 1.83
REMARK 500 O HOH 176 N PRO B 31 2656 1.83
REMARK 500 O HOH 291 CB ALA B 32 2656 1.84
REMARK 500 N ARG B 218 O LEU B 214 2655 1.84
REMARK 500 CB ARG B 217 N ARG B 217 2655 1.84
REMARK 500 O TRP B 347 C TRP B 347 2656 1.84
REMARK 500 CA PRO B 309 CG ASP A 292 2656 1.84
REMARK 500 CA ALA B 36 CB ASP A 327 2656 1.84
REMARK 500 O SER B 30 CB ALA A 322 2656 1.84
REMARK 500 C VAL B 45 CD1 LEU A 213 2656 1.84
REMARK 500 C THR B 39 N PRO A 299 2656 1.84
REMARK 500 C TYR B 258 N LEU A 294 2656 1.84
REMARK 500 CD2 TRP B 347 OD1 ASP A 327 2656 1.84
REMARK 500 CD2 PHE B 259 C ARG A 295 2656 1.84
REMARK 500 O HOH 237 CB LEU B 348 2656 1.84
REMARK 500 CB ALA B 48 CZ ARG A 217 2656 1.85
REMARK 500 CG PRO B 50 NE ARG A 218 2656 1.85
REMARK 500 CD1 PHE B 259 C GLY A 296 2656 1.85
REMARK 500 O TYR B 258 N ARG A 295 2656 1.86
REMARK 500 OD1 ASP B 43 CE2 PHE A 300 2656 1.86
REMARK 500 CA PRO B 23 CA ARG A 320 2656 1.86
REMARK 500 O HOH 370 O ALA B 350 2656 1.86
REMARK 500 CD PRO B 49 CB ARG A 217 2656 1.86
REMARK 500 CB HIS B 338 CD ARG A 295 2656 1.86
REMARK 500 C GLU B 35 CA VAL A 328 2656 1.86
REMARK 500 O ALA B 47 O LEU A 213 2656 1.86
REMARK 500 N ARG B 24 CA PHE A 317 2656 1.86
REMARK 500 N THR B 25 N PHE A 317 2656 1.87
REMARK 500 CG PHE B 29 O ARG A 319 2656 1.87
REMARK 500 CB ASP B 43 CG LEU A 321 2656 1.87
REMARK 500 N GLY B 257 N GLU A 293 2656 1.87
REMARK 500 O ILE B 260 C ASP A 292 2656 1.87
REMARK 500 CG PHE B 40 CD PRO A 299 2656 1.87
REMARK 500 CE1 PHE B 40 CD PRO A 299 2656 1.87
REMARK 500 N LEU B 221 CZ ARG B 218 2655 1.87
REMARK 500 OD2 ASP B 43 CG2 VAL A 302 2656 1.87
REMARK 500 O SER B 21 O ALA A 289 2656 1.87
REMARK 500 CA PHE B 259 CA ARG A 295 2656 1.87
REMARK 500 C MET B 33 CA ALA A 322 2656 1.87
REMARK 500 O HOH 256 OG SER B 77 2656 1.88
REMARK 500 CG ASP B 43 CD1 LEU A 321 2656 1.88
REMARK 500 CB VAL B 34 O ALA A 318 2656 1.88
REMARK 500 SD MET B 33 N GLY A 325 2656 1.88
REMARK 500 CB PRO B 49 O ARG A 217 2656 1.88
REMARK 500 CB ARG B 218 CA ALA B 215 2655 1.88
REMARK 500 O VAL B 34 CA VAL A 328 2656 1.88
REMARK 500 N THR B 39 CA PRO A 299 2656 1.88
REMARK 500 N ARG B 218 N ALA B 215 2655 1.89
REMARK 500 CG PRO B 309 CG ASP A 292 2656 1.89
REMARK 500 O HOH 259 N PHE B 29 2656 1.89
REMARK 500 O HOH 331 C ARG B 28 2656 1.89
REMARK 500 CG PRO B 309 CB ASP A 292 2656 1.89
REMARK 500 O ALA B 36 CA ASP A 327 2656 1.89
REMARK 500 O PRO B 27 O PRO B 27 2656 1.89
REMARK 500 CG TYR B 258 C GLU A 291 2656 1.89
REMARK 500 O HOH 351 CG LEU B 214 2655 1.89
REMARK 500 N LEU B 37 O VAL A 326 2656 1.89
REMARK 500 O HOH 382 O GLY B 335 2656 1.89
REMARK 500 N ASP B 256 CB SER A 290 2656 1.89
REMARK 500 C PRO B 83 CB ASP B 81 2656 1.90
REMARK 500 CD2 PHE B 40 CB PRO A 298 2656 1.90
REMARK 500 C ARG B 217 C ALA B 215 2655 1.90
REMARK 500 N ARG B 220 CD ARG B 218 2655 1.90
REMARK 500 C ALA B 48 CB ARG A 217 2656 1.90
REMARK 500 O ASP B 256 N SER A 290 2656 1.90
REMARK 500 O ILE B 260 CA GLU A 293 2656 1.90
REMARK 500 O ALA B 46 CD GLU A 293 2656 1.90
REMARK 500 CA TYR B 258 N LEU A 294 2656 1.90
REMARK 500 N GLU B 35 O VAL A 328 2656 1.90
REMARK 500 NE ARG B 24 CB VAL A 302 2656 1.90
REMARK 500 CA ALA B 38 N PHE A 300 2656 1.90
REMARK 500 CA PRO B 23 N LEU A 321 2656 1.91
REMARK 500 O ASP B 43 CE2 PHE A 317 2656 1.91
REMARK 500 O HOH 95 C PRO B 31 2656 1.91
REMARK 500 CB ALA B 350 CG GLU B 35 2656 1.92
REMARK 500 CA ALA B 36 C ASP A 327 2656 1.92
REMARK 500 O GLU B 19 CB PHE A 288 2656 1.92
REMARK 500 CG ARG B 218 C ALA B 215 2655 1.92
REMARK 500 C GLY B 257 CB GLU A 293 2656 1.92
REMARK 500 CE MET B 33 N GLY A 325 2656 1.92
REMARK 500 O HOH 331 O HOH 87 2656 1.93
REMARK 500 O HOH 269 C SER B 20 2656 1.93
REMARK 500 CB PRO B 309 CG ASP A 292 2656 1.93
REMARK 500 CE1 TYR B 258 N GLU A 291 2656 1.93
REMARK 500 C ARG B 220 NE ARG B 218 2655 1.93
REMARK 500 SD MET B 33 CA GLY A 325 2656 1.94
REMARK 500 C ASP B 308 OD1 ASP A 292 2656 1.94
REMARK 500 CG PRO B 309 OD1 ASP A 292 2656 1.94
REMARK 500 CA PHE B 40 N PRO A 299 2656 1.94
REMARK 500 CB PRO B 83 OD1 ASP B 81 2656 1.94
REMARK 500 CG PHE B 259 O ARG A 295 2656 1.94
REMARK 500 O HOH 311 O ALA B 63 2656 1.94
REMARK 500 O HOH 130 CE1 PHE A 317 2656 1.94
REMARK 500 CG ARG B 24 C PHE A 317 2656 1.94
REMARK 500 O ALA B 38 O PRO A 299 2656 1.94
REMARK 500 O HOH 237 O TRP B 347 2656 1.94
REMARK 500 N GLY B 70 OD1 ASP A 222 2656 1.95
REMARK 500 O HOH 259 O PHE B 29 2656 1.95
REMARK 500 CG LEU B 37 CA VAL A 326 2656 1.95
REMARK 500 CB PHE B 40 CG PRO A 298 2656 1.95
REMARK 500 O HOH 227 CZ2 TRP B 347 2656 1.95
REMARK 500 O HOH 290 O GLU B 254 2656 1.95
REMARK 500 C GLY B 22 CB ARG A 320 2656 1.95
REMARK 500 C PRO B 83 CG ASP B 81 2656 1.95
REMARK 500 O ALA B 36 CB ASP A 327 2656 1.95
REMARK 500 C LEU B 42 CD2 LEU A 321 2656 1.95
REMARK 500 CD PRO B 309 CB ASP A 292 2656 1.95
REMARK 500 CB SER B 20 CD2 PHE A 288 2656 1.96
REMARK 500 C ARG B 217 C LEU B 214 2655 1.96
REMARK 500 O HOH 407 O PRO B 349 2656 1.96
REMARK 500 N PRO B 23 CB ARG A 320 2656 1.96
REMARK 500 O LEU B 37 O PRO A 298 2656 1.96
REMARK 500 N GLY B 219 O LEU B 214 2655 1.96
REMARK 500 CB SER B 20 CE2 PHE A 288 2656 1.97
REMARK 500 O ASP B 26 CZ ARG A 323 2656 1.97
REMARK 500 C ASN B 255 OG SER A 290 2656 1.97
REMARK 500 O HOH 454 CG ASP B 292 2655 1.97
REMARK 500 CB PHE B 40 N PRO A 298 2656 1.97
REMARK 500 N PRO B 83 O ASP B 81 2656 1.97
REMARK 500 O HOH 35 CA PHE B 29 2656 1.97
REMARK 500 O ASP B 256 CB SER A 290 2656 1.97
REMARK 500 C ARG B 217 N ALA B 215 2655 1.97
REMARK 500 O HOH 439 OG SER B 77 2656 1.97
REMARK 500 O HOH 95 N PRO B 31 2656 1.97
REMARK 500 O HOH 167 CG ARG A 319 2656 1.98
REMARK 500 O THR B 39 O PRO A 299 2656 1.98
REMARK 500 CB PRO B 23 CA LEU A 321 2656 1.98
REMARK 500 N TYR B 258 N LEU A 294 2656 1.98
REMARK 500 O HOH 463 CB GLU B 261 2656 1.98
REMARK 500 CG TYR B 258 CB GLU A 291 2656 1.98
REMARK 500 CD1 TYR B 258 CA GLU A 291 2656 1.98
REMARK 500 CD1 PHE B 259 N LEU A 297 2656 1.98
REMARK 500 CA ARG B 24 O PHE A 317 2656 1.98
REMARK 500 CB PRO B 49 N ARG A 218 2656 1.98
REMARK 500 O HOH 485 CD PRO B 282 2655 1.98
REMARK 500 CA ALA B 351 OE2 GLU B 35 2656 1.98
REMARK 500 CG PRO B 83 O LEU B 80 2656 1.98
REMARK 500 C LYS B 216 O LEU B 214 2655 1.99
REMARK 500 O HOH 382 CA LEU B 336 2656 1.99
REMARK 500 CE1 TYR B 258 C SER A 290 2656 1.99
REMARK 500 CG1 VAL B 337 N ALA A 324 2656 1.99
REMARK 500 CZ ARG B 24 CG2 VAL A 302 2656 1.99
REMARK 500 NH1 ARG B 217 CD LYS B 216 2655 1.99
REMARK 500 O HOH 458 CD2 HIS B 346 2656 1.99
REMARK 500 N GLU B 35 CB VAL A 328 2656 1.99
REMARK 500 CA THR B 25 O ALA A 316 2656 2.00
REMARK 500 CB ALA B 47 CD1 ILE A 283 2656 2.00
REMARK 500 O HOH 95 CB PRO B 31 2656 2.00
REMARK 500 CA ARG B 218 O ALA B 215 2655 2.00
REMARK 500 N ALA B 44 CE2 PHE A 317 2656 2.00
REMARK 500 O ARG B 217 O THR B 212 2655 2.00
REMARK 500 C ALA B 48 CG ARG A 217 2656 2.01
REMARK 500 CB ALA B 38 CB PHE A 300 2656 2.01
REMARK 500 N ALA B 48 CZ ARG A 217 2656 2.01
REMARK 500 N PRO B 50 NE ARG A 218 2656 2.01
REMARK 500 C ASP B 43 CE2 PHE A 317 2656 2.01
REMARK 500 O ASP B 43 CZ PHE A 317 2656 2.01
REMARK 500 O LYS B 216 O LEU B 214 2655 2.01
REMARK 500 O HOH 525 O HOH 225 2656 2.01
REMARK 500 O HOH 516 CB GLU B 261 2656 2.01
REMARK 500 CB ALA B 36 CA ASP A 327 2656 2.01
REMARK 500 CA TYR B 258 C GLU A 291 2656 2.01
REMARK 500 CB ARG B 24 N PHE A 317 2656 2.01
REMARK 500 CA ARG B 24 N PHE A 317 2656 2.01
REMARK 500 N ARG B 218 C LEU B 214 2655 2.02
REMARK 500 O HOH 525 O LEU B 348 2656 2.02
REMARK 500 CA GLY B 41 CD1 PHE A 300 2656 2.02
REMARK 500 CB ALA B 38 C PHE A 300 2656 2.02
REMARK 500 C GLY B 257 N GLU A 293 2656 2.02
REMARK 500 CA ALA B 350 OE2 GLU B 35 2656 2.02
REMARK 500 CD1 PHE B 40 N PRO A 299 2656 2.02
REMARK 500 CA ASP B 26 NH2 ARG A 323 2656 2.02
REMARK 500 O PRO B 23 CA ARG A 320 2656 2.02
REMARK 500 O HOH 111 CZ PHE B 40 2656 2.03
REMARK 500 O HOH 112 O ASP B 256 2656 2.03
REMARK 500 O HOH 262 O THR B 25 2656 2.03
REMARK 500 O SER B 77 O LEU A 369 2656 2.03
REMARK 500 O GLU B 35 CA VAL A 328 2656 2.03
REMARK 500 O HOH 544 CG LYS B 216 2655 2.04
REMARK 500 O ARG B 218 CD2 LEU B 178 2655 2.04
REMARK 500 CA GLY B 70 N ASP A 222 2656 2.04
REMARK 500 CB PHE B 259 C LEU A 294 2656 2.04
REMARK 500 CG TYR B 258 C SER A 290 2656 2.04
REMARK 500 O PRO B 83 CG ASP B 81 2656 2.04
REMARK 500 O ASN B 255 CA ASP A 292 2656 2.04
REMARK 500 C ARG B 24 CA ALA A 316 2656 2.05
REMARK 500 CB ARG B 24 CB PHE A 317 2656 2.05
REMARK 500 N PHE B 40 O PRO A 298 2656 2.05
REMARK 500 O HOH 262 C ASP B 26 2656 2.05
REMARK 500 CB PRO B 23 C ARG A 320 2656 2.05
REMARK 500 N ALA B 350 CD1 TRP B 347 2656 2.05
REMARK 500 CB VAL B 337 CA ALA A 324 2656 2.05
REMARK 500 CE2 PHE B 29 N ALA A 324 2656 2.05
REMARK 500 O HOH 358 CD2 PHE B 344 2656 2.06
REMARK 500 O HOH 139 C ARG A 319 2656 2.06
REMARK 500 O HOH 253 CB MET B 33 2656 2.06
REMARK 500 O ILE B 260 N GLU A 293 2656 2.06
REMARK 500 CA THR B 39 N PHE A 300 2656 2.07
REMARK 500 O ALA B 38 C PHE A 300 2656 2.07
REMARK 500 CG LEU B 37 N VAL A 326 2656 2.07
REMARK 500 O HOH 259 C ARG B 28 2656 2.07
REMARK 500 O LEU B 37 CG1 VAL A 326 2656 2.07
REMARK 500 O HOH 311 CB ALA B 66 2656 2.07
REMARK 500 CA ALA B 44 CE1 PHE A 317 2656 2.07
REMARK 500 CD2 PHE B 344 O GLY A 325 2656 2.08
REMARK 500 CA SER B 21 NH2 ARG A 320 2656 2.08
REMARK 500 O HOH 492 CA GLY B 70 2656 2.08
REMARK 500 N THR B 25 CA ALA A 316 2656 2.08
REMARK 500 NH2 ARG B 24 CB VAL A 302 2656 2.08
REMARK 500 CD1 PHE B 259 O ARG A 295 2656 2.08
REMARK 500 O GLY B 22 NE ARG A 320 2656 2.08
REMARK 500 N SER B 20 CG PHE A 288 2656 2.08
REMARK 500 CB ALA B 46 O GLU A 293 2656 2.08
REMARK 500 CB PRO B 349 NE2 HIS B 346 2656 2.08
REMARK 500 CG1 VAL B 337 O ALA A 324 2656 2.08
REMARK 500 O SER B 21 NH1 ARG A 320 2656 2.08
REMARK 500 CA VAL B 45 CB ALA A 289 2656 2.08
REMARK 500 N ALA B 48 CG ARG A 217 2656 2.08
REMARK 500 CB ALA B 47 N LEU A 214 2656 2.08
REMARK 500 CA LEU B 82 O ASP B 81 2656 2.09
REMARK 500 O HOH 370 N ALA B 350 2656 2.09
REMARK 500 CB PRO B 50 CZ ARG A 218 2656 2.09
REMARK 500 O HOH 525 CB LEU B 348 2656 2.09
REMARK 500 O LEU B 336 NH2 ARG A 295 2656 2.09
REMARK 500 C VAL B 45 CD2 LEU A 213 2656 2.09
REMARK 500 N GLY B 257 CA GLU A 293 2656 2.09
REMARK 500 O ASN B 255 CB ASP A 292 2656 2.10
REMARK 500 O HOH 458 ND1 HIS B 346 2656 2.10
REMARK 500 CG ASP B 43 CD2 PHE A 300 2656 2.10
REMARK 500 CE1 PHE B 259 O GLY A 296 2656 2.10
REMARK 500 OG1 THR B 25 NH2 ARG A 320 2656 2.10
REMARK 500 CE2 PHE B 259 CA GLY A 296 2656 2.10
REMARK 500 CA ARG B 24 O ALA A 316 2656 2.10
REMARK 500 O HOH 24 OE1 GLU B 35 2656 2.10
REMARK 500 CA PHE B 259 C ARG A 295 2656 2.11
REMARK 500 O HOH 189 CG ASN B 255 2656 2.11
REMARK 500 CG ARG B 217 CB LYS B 216 2655 2.11
REMARK 500 C SER B 21 NH2 ARG A 320 2656 2.11
REMARK 500 O ARG B 24 O ALA A 316 2656 2.11
REMARK 500 CG PRO B 83 C ASP B 81 2656 2.11
REMARK 500 CG1 VAL B 45 CA ALA A 289 2656 2.11
REMARK 500 NH1 ARG B 15 N ALA A 289 2656 2.11
REMARK 500 CD1 LEU B 42 CB LEU A 297 2656 2.11
REMARK 500 NH2 ARG B 24 CG2 VAL A 302 2656 2.11
REMARK 500 O HOH 483 N PRO B 349 2656 2.11
REMARK 500 CD1 LEU B 42 N LEU A 297 2656 2.11
REMARK 500 CA SER B 30 N SER B 30 2656 2.11
REMARK 500 CB ALA B 351 OE1 GLU B 35 2656 2.11
REMARK 500 O HOH 482 OE2 GLU A 293 2656 2.12
REMARK 500 O SER B 20 N PHE A 288 2656 2.12
REMARK 500 N LEU B 37 CA VAL A 326 2656 2.12
REMARK 500 O ALA B 36 O ASP A 327 2656 2.12
REMARK 500 CB PHE B 259 CB ARG A 295 2656 2.12
REMARK 500 O VAL B 45 CD2 LEU A 213 2656 2.12
REMARK 500 CB PHE B 259 O LEU A 294 2656 2.12
REMARK 500 O HOH 492 N GLY B 70 2656 2.12
REMARK 500 O HOH 516 C GLU B 261 2656 2.12
REMARK 500 O GLU B 19 CD1 PHE A 288 2656 2.13
REMARK 500 O HOH 119 CD2 LEU A 294 2656 2.13
REMARK 500 C ALA B 44 CD2 LEU A 294 2656 2.13
REMARK 500 O ARG B 220 CD ARG B 218 2655 2.13
REMARK 500 N THR B 39 O ASP A 327 2656 2.13
REMARK 500 CA ALA B 44 CE2 PHE A 317 2656 2.13
REMARK 500 C ALA B 38 CB PHE A 300 2656 2.13
REMARK 500 C ASP B 43 CZ PHE A 317 2656 2.13
REMARK 500 CE2 TYR B 258 CB GLU A 291 2656 2.13
REMARK 500 OD1 ASP B 26 CZ ARG A 323 2656 2.13
REMARK 500 O ARG B 217 N LYS B 216 2655 2.13
REMARK 500 C SER B 20 C TYR A 287 2656 2.13
REMARK 500 N GLY B 22 NE ARG A 320 2656 2.13
REMARK 500 CA PHE B 259 O ARG A 295 2656 2.13
REMARK 500 N LEU B 221 CG ARG B 218 2655 2.13
REMARK 500 CB GLU B 35 C VAL A 328 2656 2.14
REMARK 500 N ILE B 260 O ASP A 292 2656 2.14
REMARK 500 CE2 PHE B 259 N GLY A 296 2656 2.14
REMARK 500 CG PRO B 349 CG TRP B 347 2656 2.14
REMARK 500 N ILE B 260 NZ LYS A 216 2656 2.14
REMARK 500 CG GLU B 261 CD GLU A 293 2656 2.14
REMARK 500 CB PHE B 29 C ARG A 319 2656 2.14
REMARK 500 CB ALA B 36 OD1 ASP A 327 2656 2.14
REMARK 500 C ALA B 38 C PHE A 300 2656 2.14
REMARK 500 O HOH 105 CE2 PHE B 344 2656 2.15
REMARK 500 O ARG B 217 C LEU B 214 2655 2.15
REMARK 500 CG PRO B 49 C ARG A 217 2656 2.15
REMARK 500 C ALA B 36 CB ASP A 327 2656 2.15
REMARK 500 O HOH 167 CB ARG A 319 2656 2.15
REMARK 500 CB ALA B 36 N ASP A 327 2656 2.15
REMARK 500 O HOH 130 CB PHE A 317 2656 2.15
REMARK 500 O ARG B 217 C LEU B 213 2655 2.16
REMARK 500 C ALA B 350 CD GLU B 35 2656 2.16
REMARK 500 CG PHE B 344 O GLY A 325 2656 2.16
REMARK 500 CB ALA B 47 C LEU A 213 2656 2.16
REMARK 500 O HOH 312 O THR B 25 2656 2.16
REMARK 500 CA GLY B 257 CG GLU A 293 2656 2.16
REMARK 500 CE3 TRP B 347 CG ASP A 327 2656 2.16
REMARK 500 O LYS B 216 C LEU B 214 2655 2.16
REMARK 500 O GLY B 22 CZ ARG A 320 2656 2.16
REMARK 500 CD ARG B 217 CB LYS B 216 2655 2.17
REMARK 500 CB PHE B 40 N PRO A 299 2656 2.17
REMARK 500 CD2 PHE B 29 C ARG A 320 2656 2.17
REMARK 500 CA PHE B 40 CB PRO A 298 2656 2.17
REMARK 500 O ARG B 24 N PHE A 317 2656 2.17
REMARK 500 CA ARG B 28 CD ARG A 323 2656 2.17
REMARK 500 CG LEU B 42 CG LEU A 297 2656 2.17
REMARK 500 CE2 PHE B 29 C ARG A 320 2656 2.17
REMARK 500 C ALA B 36 O ASP A 327 2656 2.17
REMARK 500 C ILE B 260 O ASP A 292 2656 2.17
REMARK 500 C PHE B 259 N ARG A 295 2656 2.17
REMARK 500 O ALA B 350 OE2 GLU B 35 2656 2.17
REMARK 500 O HOH 246 CA GLY B 264 2656 2.18
REMARK 500 C PRO B 23 CA ARG A 320 2656 2.18
REMARK 500 N PHE B 259 O LEU A 294 2656 2.18
REMARK 500 C TYR B 258 C LEU A 294 2656 2.18
REMARK 500 O ARG B 28 CD ARG A 323 2656 2.18
REMARK 500 CG GLU B 35 O VAL A 328 2656 2.18
REMARK 500 CZ PHE B 259 N GLY A 296 2656 2.18
REMARK 500 O HOH 176 CB PRO B 31 2656 2.19
REMARK 500 CG PHE B 40 N PRO A 299 2656 2.19
REMARK 500 C GLY B 22 NH1 ARG A 320 2656 2.19
REMARK 500 O HOH 57 CE1 PHE B 344 2656 2.19
REMARK 500 O ALA B 215 O LEU B 214 2655 2.19
REMARK 500 CD1 PHE B 29 CA ARG A 320 2656 2.19
REMARK 500 O HOH 259 O PRO B 27 2656 2.19
REMARK 500 CA SER B 20 CA PHE A 288 2656 2.19
REMARK 500 CB TYR B 258 N ASP A 292 2656 2.20
REMARK 500 O HOH 259 C PHE B 29 2656 2.20
REMARK 500 CE2 TYR B 258 N GLU A 291 2656 2.20
REMARK 500 OD1 ASP B 222 NH1 ARG B 218 2655 2.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE B 300 VAL B 301 0 148.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 15 DEGREES (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION
REMARK 500 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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 0 LEU A 121 CA - CB - CG ANGL. DEV. = 22.0 DEGREES
REMARK 500 0 ARG A 220 CD - NE - CZ ANGL. DEV. = 15.5 DEGREES
REMARK 500 0 VAL A 304 N - CA - CB ANGL. DEV. = 17.5 DEGREES
REMARK 500 0 VAL A 328 C - CA - CB ANGL. DEV. = 15.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JKM A 13 370 PDB 1JKM 1JKM 13 370
DBREF 1JKM B 10 370 PDB 1JKM 1JKM 10 370
SEQRES 1 A 358 PRO GLY ARG LEU GLY ASP GLU SER SER GLY PRO ARG THR
SEQRES 2 A 358 ASP PRO ARG PHE SER PRO ALA MET VAL GLU ALA LEU ALA
SEQRES 3 A 358 THR PHE GLY LEU ASP ALA VAL ALA ALA ALA PRO PRO VAL
SEQRES 4 A 358 SER ALA SER ASP ASP LEU PRO THR VAL LEU ALA ALA VAL
SEQRES 5 A 358 GLY ALA SER HIS ASP GLY PHE GLN ALA VAL TYR ASP SER
SEQRES 6 A 358 ILE ALA LEU ASP LEU PRO THR ASP ARG ASP ASP VAL GLU
SEQRES 7 A 358 THR SER THR GLU THR ILE LEU GLY VAL ASP GLY ASN GLU
SEQRES 8 A 358 ILE THR LEU HIS VAL PHE ARG PRO ALA GLY VAL GLU GLY
SEQRES 9 A 358 VAL LEU PRO GLY LEU VAL TYR THR HIS GLY GLY GLY MET
SEQRES 10 A 358 THR ILE LEU THR THR ASP ASN ARG VAL HIS ARG ARG TRP
SEQRES 11 A 358 CYS THR ASP LEU ALA ALA ALA GLY SER VAL VAL VAL MET
SEQRES 12 A 358 VAL ASP PHE ARG ASN ALA TRP THR ALA GLU GLY HIS HIS
SEQRES 13 A 358 PRO PHE PRO SER GLY VAL GLU ASP CYS LEU ALA ALA VAL
SEQRES 14 A 358 LEU TRP VAL ASP GLU HIS ARG GLU SER LEU GLY LEU SER
SEQRES 15 A 358 GLY VAL VAL VAL GLN GLY GLU SER GLY GLY GLY ASN LEU
SEQRES 16 A 358 ALA ILE ALA THR THR LEU LEU ALA LYS ARG ARG GLY ARG
SEQRES 17 A 358 LEU ASP ALA ILE ASP GLY VAL TYR ALA SER ILE PRO TYR
SEQRES 18 A 358 ILE SER GLY GLY TYR ALA TRP ASP HIS GLU ARG ARG LEU
SEQRES 19 A 358 THR GLU LEU PRO SER LEU VAL GLU ASN ASP GLY TYR PHE
SEQRES 20 A 358 ILE GLU ASN GLY GLY MET ALA LEU LEU VAL ARG ALA TYR
SEQRES 21 A 358 ASP PRO THR GLY GLU HIS ALA GLU ASP PRO ILE ALA TRP
SEQRES 22 A 358 PRO TYR PHE ALA SER GLU ASP GLU LEU ARG GLY LEU PRO
SEQRES 23 A 358 PRO PHE VAL VAL ALA VAL ASN GLU LEU ASP PRO LEU ARG
SEQRES 24 A 358 ASP GLU GLY ILE ALA PHE ALA ARG ARG LEU ALA ARG ALA
SEQRES 25 A 358 GLY VAL ASP VAL ALA ALA ARG VAL ASN ILE GLY LEU VAL
SEQRES 26 A 358 HIS GLY ALA ASP VAL ILE PHE ARG HIS TRP LEU PRO ALA
SEQRES 27 A 358 ALA LEU GLU SER THR VAL ARG ASP VAL ALA GLY PHE ALA
SEQRES 28 A 358 ALA ASP ARG ALA ARG LEU ARG
SEQRES 1 B 361 TYR THR PRO PRO GLY ARG LEU GLY ASP GLU SER SER GLY
SEQRES 2 B 361 PRO ARG THR ASP PRO ARG PHE SER PRO ALA MET VAL GLU
SEQRES 3 B 361 ALA LEU ALA THR PHE GLY LEU ASP ALA VAL ALA ALA ALA
SEQRES 4 B 361 PRO PRO VAL SER ALA SER ASP ASP LEU PRO THR VAL LEU
SEQRES 5 B 361 ALA ALA VAL GLY ALA SER HIS ASP GLY PHE GLN ALA VAL
SEQRES 6 B 361 TYR ASP SER ILE ALA LEU ASP LEU PRO THR ASP ARG ASP
SEQRES 7 B 361 ASP VAL GLU THR SER THR GLU THR ILE LEU GLY VAL ASP
SEQRES 8 B 361 GLY ASN GLU ILE THR LEU HIS VAL PHE ARG PRO ALA GLY
SEQRES 9 B 361 VAL GLU GLY VAL LEU PRO GLY LEU VAL TYR THR HIS GLY
SEQRES 10 B 361 GLY GLY MET THR ILE LEU THR THR ASP ASN ARG VAL HIS
SEQRES 11 B 361 ARG ARG TRP CYS THR ASP LEU ALA ALA ALA GLY SER VAL
SEQRES 12 B 361 VAL VAL MET VAL ASP PHE ARG ASN ALA TRP THR ALA GLU
SEQRES 13 B 361 GLY HIS HIS PRO PHE PRO SER GLY VAL GLU ASP CYS LEU
SEQRES 14 B 361 ALA ALA VAL LEU TRP VAL ASP GLU HIS ARG GLU SER LEU
SEQRES 15 B 361 GLY LEU SER GLY VAL VAL VAL GLN GLY GLU SER GLY GLY
SEQRES 16 B 361 GLY ASN LEU ALA ILE ALA THR THR LEU LEU ALA LYS ARG
SEQRES 17 B 361 ARG GLY ARG LEU ASP ALA ILE ASP GLY VAL TYR ALA SER
SEQRES 18 B 361 ILE PRO TYR ILE SER GLY GLY TYR ALA TRP ASP HIS GLU
SEQRES 19 B 361 ARG ARG LEU THR GLU LEU PRO SER LEU VAL GLU ASN ASP
SEQRES 20 B 361 GLY TYR PHE ILE GLU ASN GLY GLY MET ALA LEU LEU VAL
SEQRES 21 B 361 ARG ALA TYR ASP PRO THR GLY GLU HIS ALA GLU ASP PRO
SEQRES 22 B 361 ILE ALA TRP PRO TYR PHE ALA SER GLU ASP GLU LEU ARG
SEQRES 23 B 361 GLY LEU PRO PRO PHE VAL VAL ALA VAL ASN GLU LEU ASP
SEQRES 24 B 361 PRO LEU ARG ASP GLU GLY ILE ALA PHE ALA ARG ARG LEU
SEQRES 25 B 361 ALA ARG ALA GLY VAL ASP VAL ALA ALA ARG VAL ASN ILE
SEQRES 26 B 361 GLY LEU VAL HIS GLY ALA ASP VAL ILE PHE ARG HIS TRP
SEQRES 27 B 361 LEU PRO ALA ALA LEU GLU SER THR VAL ARG ASP VAL ALA
SEQRES 28 B 361 GLY PHE ALA ALA ASP ARG ALA ARG LEU ARG
FORMUL 3 HOH *531(H2 O1)
HELIX 1 1 GLY A 14 GLY A 17 1 4
HELIX 2 2 PRO A 31 PHE A 40 1 10
HELIX 3 3 LEU A 57 SER A 77 1 21
HELIX 4 4 ARG A 137 ALA A 148 1 12
HELIX 5 5 SER A 172 LEU A 191 1 20
HELIX 6 6 SER A 202 ARG A 217 5 16
HELIX 7 7 LEU A 221 ALA A 223 5 3
HELIX 8 8 HIS A 242 GLU A 248 1 7
HELIX 9 9 PRO A 250 GLU A 254 5 5
HELIX 10 10 ASN A 262 TYR A 272 1 11
HELIX 11 11 PRO A 286 PHE A 288 5 3
HELIX 12 12 GLU A 291 LEU A 294 1 4
HELIX 13 13 PRO A 309 ARG A 323 5 15
HELIX 14 14 ALA A 340 ILE A 343 1 4
HELIX 15 15 ARG A 345 TRP A 347 5 3
HELIX 16 16 PRO A 349 ARG A 368 1 20
HELIX 17 17 GLY B 14 GLY B 17 1 4
HELIX 18 18 PRO B 31 PHE B 40 1 10
HELIX 19 19 LEU B 57 SER B 77 1 21
HELIX 20 20 ARG B 137 ALA B 148 1 12
HELIX 21 21 SER B 172 GLU B 186 1 15
HELIX 22 22 ARG B 188 LEU B 191 1 4
HELIX 23 23 SER B 202 ARG B 217 5 16
HELIX 24 24 LEU B 221 ALA B 223 5 3
HELIX 25 25 HIS B 242 GLU B 248 1 7
HELIX 26 26 PRO B 250 GLU B 254 5 5
HELIX 27 27 ASN B 262 TYR B 272 1 11
HELIX 28 28 PRO B 286 PHE B 288 5 3
HELIX 29 29 GLU B 291 LEU B 294 1 4
HELIX 30 30 PRO B 309 ARG B 323 5 15
HELIX 31 31 ALA B 340 ILE B 343 1 4
HELIX 32 32 ARG B 345 TRP B 347 5 3
HELIX 33 33 PRO B 349 ARG B 368 1 20
SHEET 1 A 8 VAL A 89 LEU A 97 0
SHEET 2 A 8 GLU A 103 PRO A 111 -1 N ARG A 110 O GLU A 90
SHEET 3 A 8 VAL A 152 ASP A 157 -1 N ASP A 157 O THR A 105
SHEET 4 A 8 LEU A 118 THR A 124 1 N LEU A 121 O VAL A 152
SHEET 5 A 8 LEU A 193 GLU A 201 1 N SER A 194 O LEU A 118
SHEET 6 A 8 GLY A 226 SER A 230 1 N GLY A 226 O VAL A 198
SHEET 7 A 8 PRO A 299 ASN A 305 1 N PRO A 299 O VAL A 227
SHEET 8 A 8 VAL A 328 ASN A 333 1 N ALA A 329 O PHE A 300
SHEET 1 B 8 VAL B 89 LEU B 97 0
SHEET 2 B 8 GLU B 103 PRO B 111 -1 N ARG B 110 O GLU B 90
SHEET 3 B 8 SER B 151 VAL B 156 -1 N MET B 155 O HIS B 107
SHEET 4 B 8 LEU B 118 THR B 124 1 N PRO B 119 O VAL B 152
SHEET 5 B 8 LEU B 193 GLU B 201 1 N SER B 194 O LEU B 118
SHEET 6 B 8 GLY B 226 SER B 230 1 N GLY B 226 O VAL B 198
SHEET 7 B 8 PRO B 299 ASN B 305 1 N PRO B 299 O VAL B 227
SHEET 8 B 8 VAL B 328 ASN B 333 1 N ALA B 329 O PHE B 300
CISPEP 1 PHE A 170 PRO A 171 0 7.03
CISPEP 2 PHE B 170 PRO B 171 0 13.08
CRYST1 140.700 82.600 81.500 90.00 112.50 90.00 C 1 2 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 0.007107 0.000000 0.002944 0.00000
SCALE2 0.000000 0.012107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013281 0.00000 |