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HEADER HYDROLASE 26-JUL-06 2HU7
TITLE BINDING OF INHIBITORS BY ACYLAMINOACYL PEPTIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-
COMPND 5 PEPTIDASE;
COMPND 6 EC: 3.4.19.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA HYDROLASE, BETA-PROPELLER, ENZYME-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.L.KISS,B.HORNUNG,K.RADI,Z.GENGELICZKI,B.SZTARAY,V.HARMAT,
AUTHOR 2 L.POLGAR
REVDAT 1 15-MAY-07 2HU7 0
JRNL AUTH A.L.KISS,B.HORNUNG,K.RADI,Z.GENGELICZKI,B.SZTARAY,
JRNL AUTH 2 T.JUHASZ,Z.SZELTNER,V.HARMAT,L.POLGAR
JRNL TITL THE ACYLAMINOACYL PEPTIDASE FROM AEROPYRUM PERNIX
JRNL TITL 2 K1 THOUGHT TO BE AN EXOPEPTIDASE DISPLAYS
JRNL TITL 3 ENDOPEPTIDASE ACTIVITY
JRNL REF J.MOL.BIOL. V. 368 509 2007
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.BARTLAM,G.WANG,H.YANG,R.GAO,X.ZHAO,G.XIE,S.CAO,
REMARK 1 AUTH 2 Y.FENG,Z.RAO
REMARK 1 TITL CRYSTAL STRUCTURE OF AN ACYLPEPTIDE
REMARK 1 TITL 2 HYDROLASE/ESTERASE FROM AEROPYRUM PERNIX K1
REMARK 1 REF STRUCTURE V. 12 1481 2004
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 68079
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM (AS FOR RELATED PDB
REMARK 3 ENTRY 2HU5)
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3602
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3859
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 186
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 9049
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.194
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.124
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.633
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8890 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 8241 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12067 ; 1.274 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19034 ; 0.838 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1152 ; 6.421 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1343 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10074 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1869 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1698 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 10060 ; 0.248 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 5797 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 465 ; 0.147 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 24 ; 0.266 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 88 ; 0.248 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.183 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5695 ; 1.087 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9108 ; 1.747 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3195 ; 1.210 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2958 ; 1.968 ; 3.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 22
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 22 A 30 5
REMARK 3 1 B 22 B 30 5
REMARK 3 2 A 47 A 52 5
REMARK 3 2 B 47 B 52 5
REMARK 3 3 A 57 A 72 5
REMARK 3 3 B 57 B 72 5
REMARK 3 4 A 77 A 82 5
REMARK 3 4 B 77 B 82 5
REMARK 3 5 A 90 A 100 5
REMARK 3 5 B 90 B 100 5
REMARK 3 6 A 106 A 161 5
REMARK 3 6 B 106 B 161 5
REMARK 3 7 A 165 A 179 5
REMARK 3 7 B 165 B 179 5
REMARK 3 8 A 186 A 198 5
REMARK 3 8 B 186 B 198 5
REMARK 3 9 A 261 A 274 5
REMARK 3 9 B 261 B 274 5
REMARK 3 10 A 279 A 290 5
REMARK 3 10 B 279 B 290 5
REMARK 3 11 A 296 A 300 5
REMARK 3 11 B 296 B 300 5
REMARK 3 12 A 345 A 350 5
REMARK 3 12 B 345 B 350 5
REMARK 3 13 A 362 A 382 5
REMARK 3 13 B 362 B 382 5
REMARK 3 14 A 385 A 425 5
REMARK 3 14 B 385 B 425 5
REMARK 3 15 A 431 A 435 5
REMARK 3 15 B 431 B 435 5
REMARK 3 16 A 436 A 468 5
REMARK 3 16 B 436 B 468 5
REMARK 3 17 A 481 A 493 5
REMARK 3 17 B 481 B 493 5
REMARK 3 18 A 503 A 514 5
REMARK 3 18 B 503 B 514 5
REMARK 3 19 A 516 A 519 5
REMARK 3 19 B 516 B 519 5
REMARK 3 20 A 538 A 543 5
REMARK 3 20 B 538 B 543 5
REMARK 3 21 A 550 A 560 5
REMARK 3 21 B 550 B 560 5
REMARK 3 22 A 568 A 579 5
REMARK 3 22 B 568 B 579 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1901 ; 0.10 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 2915 ; 0.41 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1901 ; 0.72 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 2915 ; 1.17 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 581
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7585 27.7033 18.1999
REMARK 3 T TENSOR
REMARK 3 T11: 0.0149 T22: 0.0294
REMARK 3 T33: 0.0056 T12: 0.0096
REMARK 3 T13: -0.0076 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.1871 L22: 0.5382
REMARK 3 L33: 0.2881 L12: -0.0242
REMARK 3 L13: 0.1214 L23: 0.1131
REMARK 3 S TENSOR
REMARK 3 S11: 0.0283 S12: 0.0015 S13: -0.0168
REMARK 3 S21: -0.0518 S22: -0.0182 S23: -0.0141
REMARK 3 S31: -0.0320 S32: -0.0162 S33: -0.0101
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 9 B 581
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8464 -18.1985 26.3915
REMARK 3 T TENSOR
REMARK 3 T11: 0.0298 T22: 0.0409
REMARK 3 T33: 0.0209 T12: -0.0062
REMARK 3 T13: -0.0205 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.5381 L22: 0.9891
REMARK 3 L33: 0.3013 L12: 0.0747
REMARK 3 L13: 0.2011 L23: -0.0234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.0586 S13: -0.0300
REMARK 3 S21: -0.1217 S22: 0.0152 S23: -0.0772
REMARK 3 S31: 0.0509 S32: 0.0367 S33: -0.0194
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2HU7 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76464
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.537
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1VE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 78MM SODIUM ACETATE, 0.44MM EDTA,
REMARK 280 2.2% PEG 4000, 0.56% BETA-OCTYL-GLUCOSIDE, PH 5.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 31.84100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.29700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.99450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.29700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.84100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.99450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ARG A 2
REMARK 465 ILE A 3
REMARK 465 ILE A 4
REMARK 465 MET A 5
REMARK 465 PRO A 6
REMARK 465 VAL A 7
REMARK 465 GLU A 8
REMARK 465 ARG A 582
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ILE B 3
REMARK 465 ILE B 4
REMARK 465 MET B 5
REMARK 465 PRO B 6
REMARK 465 VAL B 7
REMARK 465 GLU B 8
REMARK 465 ARG B 582
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 ARG A 11 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 149 CD NE CZ NH1 NH2
REMARK 470 ARG A 216 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 217 CG CD OE1 OE2
REMARK 470 GLU A 324 CG CD OE1 OE2
REMARK 470 ARG A 327 CD NE CZ NH1 NH2
REMARK 470 ARG A 328 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 497 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 501 CD NE CZ NH1 NH2
REMARK 470 PHE B 9 CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 11 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 14 NE CZ NH1 NH2
REMARK 470 ASP B 52 CG OD1 OD2
REMARK 470 LYS B 110 CE NZ
REMARK 470 ARG B 188 CD NE CZ NH1 NH2
REMARK 470 ARG B 216 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 LYS B 294 CG CD CE NZ
REMARK 470 GLU B 315 CG CD OE1 OE2
REMARK 470 ARG B 327 CZ NH1 NH2
REMARK 470 ARG B 328 CD NE CZ NH1 NH2
REMARK 470 ARG B 511 CD NE CZ NH1 NH2
REMARK 470 ARG B 581 NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 28 CD GLN A 28 NE2 -0.071
REMARK 500 MET A 394 SD MET A 394 CE -0.081
REMARK 500 MET A 450 SD MET A 450 CE -0.071
REMARK 500 MET A 500 SD MET A 500 CE -0.102
REMARK 500 MET B 394 SD MET B 394 CE -0.114
REMARK 500 MET B 457 SD MET B 457 CE -0.065
REMARK 500 MET B 477 SD MET B 477 CE -0.067
REMARK 500 MET B 536 SD MET B 536 CE -0.201
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA A 215 N - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 ASP B 227 N - CA - C ANGL. DEV. = -9.1 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER B 445 -118.07 68.41
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HU5 RELATED DB: PDB
REMARK 900 RELATED ID: 2HU8 RELATED DB: PDB
DBREF 2HU7 A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 2HU7 B 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
SEQRES 1 A 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 A 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 A 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 A 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 A 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 A 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 A 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 A 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 A 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 A 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 A 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 A 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 A 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 A 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 A 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 A 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 A 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 A 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 A 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 A 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 A 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 A 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 A 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 A 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 A 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 A 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 A 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 A 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 A 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 A 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 A 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 A 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 A 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 A 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 A 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 A 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 A 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 A 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 A 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 A 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 A 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 A 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 A 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 A 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 A 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 B 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 B 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 B 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 B 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 B 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 B 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 B 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 B 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 B 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 B 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 B 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 B 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 B 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 B 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 B 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 B 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 B 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 B 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 B 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 B 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 B 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 B 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 B 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 B 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 B 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 B 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 B 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 B 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 B 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 B 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 B 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 B 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 B 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 B 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 B 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 B 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 B 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 B 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 B 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 B 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 B 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 B 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 B 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 B 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 B 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
HET ACE 1001 3
HET PHE 1002 12
HET ACE 2001 3
HET PHE 2002 12
HET GOL 3001 6
HET GOL 3002 6
HETNAM ACE ACETYL GROUP
HETNAM PHE PHENYLALANINE
HETNAM GOL GLYCEROL
FORMUL 3 ACE 2(C2 H3 O1)
FORMUL 4 PHE 2(C9 H11 N1 O2)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 HOH *349(H2 O1)
HELIX 1 1 PHE A 9 VAL A 22 1 14
HELIX 2 2 LYS A 238 ARG A 244 1 7
HELIX 3 3 PRO A 323 SER A 329 1 7
HELIX 4 4 ASP A 379 GLY A 389 1 11
HELIX 5 5 GLY A 404 LYS A 410 1 7
HELIX 6 6 GLY A 417 SER A 433 1 17
HELIX 7 7 SER A 445 LYS A 458 1 14
HELIX 8 8 ASP A 473 LEU A 480 1 8
HELIX 9 9 ASP A 482 GLY A 494 1 13
HELIX 10 10 SER A 496 ARG A 503 1 8
HELIX 11 11 SER A 504 ILE A 512 5 9
HELIX 12 12 LEU A 529 ARG A 542 1 14
HELIX 13 13 THR A 560 ARG A 581 1 22
HELIX 14 14 PHE B 9 VAL B 22 1 14
HELIX 15 15 LYS B 238 ARG B 244 1 7
HELIX 16 16 PRO B 323 SER B 329 1 7
HELIX 17 17 ASP B 379 ALA B 388 1 10
HELIX 18 18 GLY B 404 LYS B 410 1 7
HELIX 19 19 GLY B 417 SER B 433 1 17
HELIX 20 20 SER B 445 LYS B 458 1 14
HELIX 21 21 ASP B 473 LEU B 480 1 8
HELIX 22 22 ASP B 482 GLY B 494 1 13
HELIX 23 23 SER B 496 ARG B 503 1 8
HELIX 24 24 SER B 504 ILE B 512 5 9
HELIX 25 25 PRO B 528 ARG B 542 1 15
HELIX 26 26 THR B 560 ARG B 579 1 20
SHEET 1 A 4 LYS A 24 VAL A 31 0
SHEET 2 A 4 LYS A 35 SER A 42 -1 O LEU A 37 N GLY A 29
SHEET 3 A 4 SER A 45 TYR A 51 -1 O TYR A 49 N VAL A 38
SHEET 4 A 4 VAL A 57 LYS A 58 -1 O VAL A 57 N LEU A 50
SHEET 1 B 4 SER A 66 VAL A 67 0
SHEET 2 B 4 ARG A 76 ASP A 82 -1 O VAL A 80 N SER A 66
SHEET 3 B 4 HIS A 90 ASN A 96 -1 O PHE A 93 N LEU A 79
SHEET 4 B 4 GLU A 103 ARG A 105 -1 O GLN A 104 N LYS A 94
SHEET 1 C 5 ASP A 69 PRO A 70 0
SHEET 2 C 5 ARG A 113 ASP A 119 1 O ASP A 119 N ASP A 69
SHEET 3 C 5 VAL A 124 ALA A 129 -1 O VAL A 125 N VAL A 118
SHEET 4 C 5 VAL A 134 ASP A 140 -1 O TYR A 137 N PHE A 126
SHEET 5 C 5 GLY A 143 LEU A 150 -1 O ALA A 148 N LEU A 136
SHEET 1 D 4 GLY A 154 ARG A 160 0
SHEET 2 D 4 LEU A 163 GLY A 171 -1 O LEU A 167 N PHE A 155
SHEET 3 D 4 ARG A 174 ASN A 181 -1 O SER A 176 N GLY A 168
SHEET 4 D 4 GLY A 185 PHE A 190 -1 O PHE A 190 N LEU A 177
SHEET 1 E 4 GLY A 195 ILE A 202 0
SHEET 2 E 4 VAL A 208 THR A 214 -1 O GLU A 213 N SER A 196
SHEET 3 E 4 ALA A 218 VAL A 223 -1 O ARG A 219 N LEU A 212
SHEET 4 E 4 VAL A 230 ASP A 232 -1 O GLU A 231 N THR A 222
SHEET 1 F 4 ALA A 247 TYR A 253 0
SHEET 2 F 4 LEU A 259 ARG A 265 -1 O VAL A 262 N TRP A 250
SHEET 3 F 4 ARG A 268 ILE A 273 -1 O PHE A 272 N VAL A 261
SHEET 4 F 4 GLU A 276 VAL A 278 -1 O VAL A 278 N VAL A 271
SHEET 1 G 4 ASN A 284 TRP A 291 0
SHEET 2 G 4 LYS A 294 SER A 301 -1 O THR A 300 N ASN A 284
SHEET 3 G 4 THR A 304 LEU A 311 -1 O VAL A 309 N THR A 297
SHEET 4 G 4 PRO A 316 LEU A 318 -1 O LEU A 317 N ILE A 308
SHEET 1 H16 ILE A 330 GLU A 339 0
SHEET 2 H16 ARG A 345 SER A 353 -1 O VAL A 346 N VAL A 338
SHEET 3 H16 HIS A 391 PRO A 395 -1 O MET A 394 N TYR A 349
SHEET 4 H16 GLY A 360 VAL A 366 1 N VAL A 363 O HIS A 391
SHEET 5 H16 ALA A 436 TYR A 444 1 O MET A 442 N VAL A 366
SHEET 6 H16 ALA A 464 GLY A 468 1 O GLY A 468 N GLY A 443
SHEET 7 H16 LEU A 516 PRO A 521 1 O ALA A 517 N ALA A 467
SHEET 8 H16 PHE A 546 ILE A 551 1 O GLU A 547 N LEU A 518
SHEET 9 H16 PHE B 546 ILE B 551 -1 O ALA B 548 N ILE A 550
SHEET 10 H16 LEU B 516 PRO B 521 1 N LEU B 518 O GLU B 547
SHEET 11 H16 ALA B 464 GLY B 468 1 N ALA B 467 O ALA B 517
SHEET 12 H16 ALA B 436 TYR B 444 1 N GLY B 443 O GLY B 468
SHEET 13 H16 GLY B 360 VAL B 366 1 N VAL B 364 O TYR B 440
SHEET 14 H16 HIS B 391 PRO B 395 1 O HIS B 391 N VAL B 363
SHEET 15 H16 ARG B 345 SER B 353 -1 N LEU B 351 O VAL B 392
SHEET 16 H16 ILE B 330 GLU B 339 -1 N VAL B 336 O THR B 348
SHEET 1 I 4 LYS B 24 VAL B 31 0
SHEET 2 I 4 LYS B 35 SER B 42 -1 O PHE B 41 N LYS B 24
SHEET 3 I 4 SER B 45 TYR B 51 -1 O TYR B 49 N VAL B 38
SHEET 4 I 4 THR B 56 LYS B 58 -1 O VAL B 57 N LEU B 50
SHEET 1 J 4 SER B 66 VAL B 67 0
SHEET 2 J 4 ARG B 76 ASP B 82 -1 O VAL B 80 N SER B 66
SHEET 3 J 4 HIS B 90 ASN B 96 -1 O PHE B 93 N LEU B 79
SHEET 4 J 4 GLN B 104 ARG B 105 -1 O GLN B 104 N LYS B 94
SHEET 1 K 5 ASP B 69 PRO B 70 0
SHEET 2 K 5 ARG B 113 ASP B 119 1 O ASP B 119 N ASP B 69
SHEET 3 K 5 VAL B 124 ALA B 129 -1 O VAL B 125 N VAL B 118
SHEET 4 K 5 VAL B 134 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 K 5 GLY B 143 LEU B 150 -1 O ALA B 148 N LEU B 136
SHEET 1 L 4 GLY B 154 ARG B 160 0
SHEET 2 L 4 LEU B 163 GLY B 171 -1 O ALA B 165 N SER B 157
SHEET 3 L 4 ARG B 174 ASN B 181 -1 O SER B 176 N GLY B 168
SHEET 4 L 4 ARG B 188 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 M 4 GLY B 195 ILE B 202 0
SHEET 2 M 4 VAL B 208 THR B 214 -1 O GLU B 213 N SER B 196
SHEET 3 M 4 ALA B 218 VAL B 223 -1 O VAL B 223 N VAL B 208
SHEET 4 M 4 VAL B 230 ASP B 232 -1 O GLU B 231 N THR B 222
SHEET 1 N 4 ALA B 247 TYR B 253 0
SHEET 2 N 4 LEU B 259 ARG B 265 -1 O VAL B 262 N TRP B 250
SHEET 3 N 4 ARG B 268 ILE B 273 -1 O ALA B 270 N ALA B 263
SHEET 4 N 4 GLU B 276 VAL B 278 -1 O VAL B 278 N VAL B 271
SHEET 1 O 4 ASN B 284 TRP B 291 0
SHEET 2 O 4 LYS B 294 SER B 301 -1 O THR B 300 N ASN B 284
SHEET 3 O 4 THR B 304 LEU B 311 -1 O LEU B 311 N LEU B 295
SHEET 4 O 4 PRO B 316 LEU B 318 -1 O LEU B 318 N ILE B 308
LINK C ACE 1001 N PHE 1002
LINK C ACE 2001 N PHE 2002
CISPEP 1 LEU A 311 PRO A 312 0 2.09
CISPEP 2 LEU A 311 PRO A 312 0 2.05
CISPEP 3 THR A 358 PRO A 359 0 3.99
CISPEP 4 GLY A 369 PRO A 370 0 9.29
CISPEP 5 LEU B 311 PRO B 312 0 10.20
CISPEP 6 THR B 358 PRO B 359 0 -0.03
CISPEP 7 GLY B 369 PRO B 370 0 11.90
CRYST1 63.682 103.989 168.594 90.00 90.00 90.00 P 21 21 21 8
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 0.015703 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009616 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005931 0.00000
TER 4345 ARG A 581
TER 8660 ARG B 581
MASTER 435 0 6 26 74 0 0 6 9049 2 20 90
END |