| content |
HEADER HYDROLASE 20-AUG-25 9Q5G
TITLE HUMAN PROLYL ENDOPEPTIDASE (PREP) - APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PE,POST-PROLINE CLEAVING ENZYME;
COMPND 5 EC: 3.4.21.26;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PREP, PEP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS APO FORM, PEPTIDE CLEAVAGE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.J.FUCCI,E.YOO,D.C.F.MONTEIRO
REVDAT 1 21-JAN-26 9Q5G 0
JRNL AUTH K.THAKUR,I.FUCCI,J.PANDIAN,K.F.SUAZO,D.C.F.MONTEIRO,E.YOO
JRNL TITL STRUCTURE-GUIDED OPTIMIZATION OF 4-CHLORO-PYRAZOLOPYRIDINE
JRNL TITL 2 ANALOGS FOR COVALENT PREP INHIBITION.
JRNL REF J.MED.CHEM. 2026
JRNL REFN ISSN 0022-2623
JRNL PMID 41512187
JRNL DOI 10.1021/ACS.JMEDCHEM.5C02680
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 77.5
REMARK 3 NUMBER OF REFLECTIONS : 201199
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
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10503
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2442
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 12.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17011
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 2284
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.288
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17848 ; 0.015 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 16463 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24183 ; 2.237 ; 1.820
REMARK 3 BOND ANGLES OTHERS (DEGREES): 38068 ; 0.774 ; 1.764
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2189 ; 7.115 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ; 9.883 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2985 ;13.530 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2558 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20912 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4160 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 8557 ; 1.369 ; 1.051
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8549 ; 1.358 ; 1.049
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10699 ; 1.985 ; 1.879
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 10700 ; 1.985 ; 1.879
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9291 ; 2.668 ; 1.357
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 9291 ; 2.668 ; 1.357
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 13448 ; 3.937 ; 2.333
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 20565 ; 5.993 ;14.660
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 20566 ; 5.994 ;14.660
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
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 5 A 710
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2053 -4.4355 26.4738
REMARK 3 T TENSOR
REMARK 3 T11: 0.0114 T22: 0.0048
REMARK 3 T33: 0.0319 T12: 0.0004
REMARK 3 T13: 0.0070 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.3590 L22: 0.6232
REMARK 3 L33: 0.4537 L12: 0.0675
REMARK 3 L13: -0.1094 L23: -0.1208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0105 S12: -0.0208 S13: -0.0134
REMARK 3 S21: 0.0517 S22: 0.0003 S23: -0.0210
REMARK 3 S31: 0.0361 S32: 0.0234 S33: 0.0103
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 4 B 710
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3797 -3.3344 -23.6259
REMARK 3 T TENSOR
REMARK 3 T11: 0.0094 T22: 0.0156
REMARK 3 T33: 0.0271 T12: -0.0017
REMARK 3 T13: 0.0050 T23: -0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.6386 L22: 0.5942
REMARK 3 L33: 0.4294 L12: 0.1982
REMARK 3 L13: -0.1591 L23: -0.1688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0427 S12: -0.0598 S13: 0.0489
REMARK 3 S21: 0.0567 S22: -0.0311 S23: -0.0103
REMARK 3 S31: -0.0083 S32: 0.0563 S33: -0.0116
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 710
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4500 0.2096 77.0437
REMARK 3 T TENSOR
REMARK 3 T11: 0.0741 T22: 0.0930
REMARK 3 T33: 0.0554 T12: 0.0017
REMARK 3 T13: -0.0020 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 0.4163 L22: 0.7835
REMARK 3 L33: 1.1653 L12: 0.1498
REMARK 3 L13: -0.1743 L23: -0.2969
REMARK 3 S TENSOR
REMARK 3 S11: -0.0261 S12: -0.0085 S13: -0.0346
REMARK 3 S21: -0.0058 S22: 0.0181 S23: -0.0895
REMARK 3 S31: 0.1381 S32: 0.1694 S33: 0.0081
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 9Q5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-25.
REMARK 100 THE DEPOSITION ID IS D_1000299176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-24
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 : NSLS-II
REMARK 200 BEAMLINE : 17-ID-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979340
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 211702
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 34.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-30% PEG 3350, 200 MM KSCN AND 100
REMARK 280 MM BIS-TRIS PROPANE PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.44000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 SER A 3
REMARK 465 LEU A 4
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 SER B 3
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 LEU C 2
REMARK 465 SER C 3
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 NH2 ARG C 66 OE1 GLU C 69 1.72
REMARK 500 O HOH A 965 O HOH A 1391 1.75
REMARK 500 O HOH B 1517 O HOH B 1588 1.81
REMARK 500 O HOH A 1537 O HOH B 1623 1.87
REMARK 500 NE2 GLN B 388 O HOH B 901 1.91
REMARK 500 O HOH C 1252 O HOH C 1374 1.92
REMARK 500 O HOH A 1558 O HOH A 1599 1.95
REMARK 500 O HOH A 1380 O HOH A 1684 1.97
REMARK 500 O HOH C 1288 O HOH C 1300 2.03
REMARK 500 O HOH B 1084 O HOH B 1497 2.03
REMARK 500 OE1 GLU A 609 O HOH A 901 2.03
REMARK 500 NE2 GLN C 268 O HOH C 901 2.04
REMARK 500 O HOH B 1513 O HOH B 1612 2.05
REMARK 500 O HOH A 1288 O HOH A 1451 2.06
REMARK 500 O HOH B 1227 O HOH B 1231 2.06
REMARK 500 OE2 GLU A 227 O HOH A 902 2.07
REMARK 500 O HOH A 1559 O HOH A 1706 2.08
REMARK 500 O HOH A 1351 O HOH A 1400 2.08
REMARK 500 O HOH B 1181 O HOH B 1604 2.10
REMARK 500 O HOH C 1301 O HOH C 1389 2.10
REMARK 500 O HOH A 1456 O HOH A 1743 2.11
REMARK 500 O HOH C 1219 O HOH C 1314 2.11
REMARK 500 O HOH B 1200 O HOH B 1547 2.11
REMARK 500 O HOH B 1663 O HOH B 1719 2.12
REMARK 500 O HOH B 1671 O HOH B 1736 2.13
REMARK 500 O HOH B 958 O HOH B 1083 2.13
REMARK 500 O HOH B 1499 O HOH B 1731 2.13
REMARK 500 O HOH A 1317 O HOH A 1446 2.13
REMARK 500 O HOH A 1333 O HOH A 1631 2.13
REMARK 500 O HOH A 1191 O HOH A 1316 2.14
REMARK 500 O HOH A 1690 O HOH A 1698 2.14
REMARK 500 OD2 ASP A 18 O HOH A 903 2.14
REMARK 500 O HOH A 1518 O HOH A 1734 2.15
REMARK 500 O HOH B 929 O HOH B 1535 2.16
REMARK 500 O HOH C 1201 O HOH C 1295 2.16
REMARK 500 O HOH B 1402 O HOH B 1568 2.16
REMARK 500 O HOH A 1151 O HOH A 1153 2.17
REMARK 500 OE1 GLU A 44 O HOH A 904 2.17
REMARK 500 O HOH B 942 O HOH B 1648 2.18
REMARK 500 OD1 ASP A 431 O HOH A 905 2.18
REMARK 500 OE1 GLU B 334 O HOH B 902 2.19
REMARK 500 O HOH B 1023 O HOH B 1595 2.19
REMARK 500 OE2 GLU A 163 O HOH A 906 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 121 NH1 ARG C 664 2556 2.08
REMARK 500 O HOH A 1132 O HOH B 1554 2555 2.12
REMARK 500 O HOH B 1134 O HOH C 1324 2545 2.17
REMARK 500 O HOH A 1615 O HOH A 1693 2555 2.17
REMARK 500 O HOH B 1654 O HOH B 1666 1565 2.18
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 289 CD GLU B 289 OE1 0.085
REMARK 500 GLU B 296 CD GLU B 296 OE1 0.088
REMARK 500 GLU C 289 CD GLU C 289 OE1 0.098
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 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 111 CG - CD - NE ANGL. DEV. = -13.6 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 128 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 GLN A 267 CB - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 GLU A 289 CG - CD - OE1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 GLU A 289 CG - CD - OE2 ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG A 312 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 THR A 399 OG1 - CB - CG2 ANGL. DEV. = -14.9 DEGREES
REMARK 500 ARG A 423 CD - NE - CZ ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG A 423 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 488 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 CYS A 526 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 ARG A 547 CD - NE - CZ ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG A 547 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TYR A 589 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR A 589 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 60 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 GLU B 169 CB - CG - CD ANGL. DEV. = 17.4 DEGREES
REMARK 500 GLN B 268 CB - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 GLU B 289 CG - CD - OE2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 ARG B 312 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 312 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 GLY B 405 C - N - CA ANGL. DEV. = -14.9 DEGREES
REMARK 500 ARG B 423 CB - CA - C ANGL. DEV. = -15.9 DEGREES
REMARK 500 ARG B 488 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG B 488 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG B 505 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 CYS B 526 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 LYS B 546 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG B 662 NE - CZ - NH1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 LYS C 23 CB - CA - C ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG C 60 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 66 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG C 66 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG C 128 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG C 245 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 252 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 GLU C 289 CG - CD - OE2 ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG C 306 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLN C 362 CB - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 53 ANGLE DEVIATIONS.
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 SER A 308 77.43 -151.36
REMARK 500 SER A 308 77.25 -151.34
REMARK 500 TYR A 311 155.91 78.02
REMARK 500 LYS A 335 -32.48 -133.96
REMARK 500 SER A 346 -55.92 71.20
REMARK 500 SER A 346 -61.60 76.70
REMARK 500 TYR A 473 -73.97 -132.41
REMARK 500 LEU A 520 -127.10 61.58
REMARK 500 SER A 554 -120.37 72.04
REMARK 500 THR A 590 -116.85 33.57
REMARK 500 ASN A 705 60.49 64.10
REMARK 500 ALA B 161 58.12 36.15
REMARK 500 SER B 308 76.41 -154.62
REMARK 500 TYR B 311 152.10 75.36
REMARK 500 LYS B 335 -33.09 -140.69
REMARK 500 SER B 346 -52.77 67.23
REMARK 500 SER B 346 -57.52 71.88
REMARK 500 TYR B 473 -77.09 -131.89
REMARK 500 LEU B 520 -124.34 59.95
REMARK 500 SER B 554 -112.43 71.67
REMARK 500 THR B 590 -110.64 32.77
REMARK 500 GLU C 107 61.92 -117.68
REMARK 500 ALA C 161 61.03 35.52
REMARK 500 SER C 197 48.17 -141.78
REMARK 500 SER C 270 86.81 -69.80
REMARK 500 SER C 271 1.15 87.12
REMARK 500 PHE C 286 43.56 -109.19
REMARK 500 SER C 308 75.99 -164.87
REMARK 500 TYR C 311 152.23 77.53
REMARK 500 ASP C 320 59.82 -152.12
REMARK 500 SER C 346 -56.48 75.77
REMARK 500 ASN C 347 27.42 -141.53
REMARK 500 LEU C 417 50.95 78.23
REMARK 500 TYR C 473 -81.05 -129.30
REMARK 500 LEU C 520 -120.08 63.91
REMARK 500 SER C 554 -122.92 76.65
REMARK 500 THR C 590 -120.34 36.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 547 0.13 SIDE CHAIN
REMARK 500 ARG B 66 0.10 SIDE CHAIN
REMARK 500 ARG B 252 0.09 SIDE CHAIN
REMARK 500 ARG B 420 0.11 SIDE CHAIN
REMARK 500 ARG B 423 0.11 SIDE CHAIN
REMARK 500 ARG B 488 0.13 SIDE CHAIN
REMARK 500 ARG B 662 0.10 SIDE CHAIN
REMARK 500 ARG B 664 0.17 SIDE CHAIN
REMARK 500 ARG C 66 0.08 SIDE CHAIN
REMARK 500 ARG C 306 0.07 SIDE CHAIN
REMARK 500 ARG C 319 0.13 SIDE CHAIN
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 A1791 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A1792 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A1793 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A1794 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A1795 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH B1768 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B1769 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B1770 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH B1771 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH C1417 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C1418 DISTANCE = 14.73 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEG A 808
DBREF 9Q5G A 1 710 UNP P48147 PPCE_HUMAN 1 710
DBREF 9Q5G B 1 710 UNP P48147 PPCE_HUMAN 1 710
DBREF 9Q5G C 1 710 UNP P48147 PPCE_HUMAN 1 710
SEQADV 9Q5G GLY A 0 UNP P48147 EXPRESSION TAG
SEQADV 9Q5G GLY B 0 UNP P48147 EXPRESSION TAG
SEQADV 9Q5G GLY C 0 UNP P48147 EXPRESSION TAG
SEQRES 1 A 711 GLY MET LEU SER LEU GLN TYR PRO ASP VAL TYR ARG ASP
SEQRES 2 A 711 GLU THR ALA VAL GLN ASP TYR HIS GLY HIS LYS ILE CYS
SEQRES 3 A 711 ASP PRO TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN
SEQRES 4 A 711 THR LYS ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL
SEQRES 5 A 711 PRO PHE LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS
SEQRES 6 A 711 GLU ARG MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER
SEQRES 7 A 711 CYS HIS PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR
SEQRES 8 A 711 ASN THR GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN
SEQRES 9 A 711 ASP SER LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO
SEQRES 10 A 711 ASN ILE LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY
SEQRES 11 A 711 TYR ALA PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY
SEQRES 12 A 711 LEU SER ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE
SEQRES 13 A 711 MET LYS VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU
SEQRES 14 A 711 GLU ARG VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP
SEQRES 15 A 711 GLY LYS GLY MET PHE TYR ASN SER TYR PRO GLN GLN ASP
SEQRES 16 A 711 GLY LYS SER ASP GLY THR GLU THR SER THR ASN LEU HIS
SEQRES 17 A 711 GLN LYS LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER
SEQRES 18 A 711 GLU ASP ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS
SEQRES 19 A 711 TRP MET GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR
SEQRES 20 A 711 VAL LEU LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN
SEQRES 21 A 711 ARG LEU TRP TYR CYS ASP LEU GLN GLN GLU SER SER GLY
SEQRES 22 A 711 ILE ALA GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN
SEQRES 23 A 711 PHE GLU GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR
SEQRES 24 A 711 VAL PHE THR PHE LYS THR ASN ARG GLN SER PRO ASN TYR
SEQRES 25 A 711 ARG VAL ILE ASN ILE ASP PHE ARG ASP PRO GLU GLU SER
SEQRES 26 A 711 LYS TRP LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL
SEQRES 27 A 711 LEU GLU TRP ILE ALA CYS VAL ARG SER ASN PHE LEU VAL
SEQRES 28 A 711 LEU CYS TYR LEU HIS ASP VAL LYS ASN ILE LEU GLN LEU
SEQRES 29 A 711 HIS ASP LEU THR THR GLY ALA LEU LEU LYS THR PHE PRO
SEQRES 30 A 711 LEU ASP VAL GLY SER ILE VAL GLY TYR SER GLY GLN LYS
SEQRES 31 A 711 LYS ASP THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU
SEQRES 32 A 711 SER PRO GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU
SEQRES 33 A 711 GLU LEU GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS
SEQRES 34 A 711 GLY ILE ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE
SEQRES 35 A 711 TYR PRO SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE
SEQRES 36 A 711 VAL HIS LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO
SEQRES 37 A 711 ALA PHE LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE
SEQRES 38 A 711 THR PRO ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG
SEQRES 39 A 711 HIS MET GLY GLY ILE LEU ALA VAL ALA ASN ILE ARG GLY
SEQRES 40 A 711 GLY GLY GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE
SEQRES 41 A 711 LEU ALA ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS
SEQRES 42 A 711 ALA ALA GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO
SEQRES 43 A 711 LYS ARG LEU THR ILE ASN GLY GLY SER ASN GLY GLY LEU
SEQRES 44 A 711 LEU VAL ALA ALA CYS ALA ASN GLN ARG PRO ASP LEU PHE
SEQRES 45 A 711 GLY CYS VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU
SEQRES 46 A 711 LYS PHE HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR
SEQRES 47 A 711 ASP TYR GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP
SEQRES 48 A 711 LEU VAL LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO
SEQRES 49 A 711 GLU ALA ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU
SEQRES 50 A 711 THR ALA ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER
SEQRES 51 A 711 LEU LYS PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG
SEQRES 52 A 711 SER ARG LYS GLN SER ASN PRO LEU LEU ILE HIS VAL ASP
SEQRES 53 A 711 THR LYS ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS
SEQRES 54 A 711 VAL ILE GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA
SEQRES 55 A 711 ARG CYS LEU ASN VAL ASP TRP ILE PRO
SEQRES 1 B 711 GLY MET LEU SER LEU GLN TYR PRO ASP VAL TYR ARG ASP
SEQRES 2 B 711 GLU THR ALA VAL GLN ASP TYR HIS GLY HIS LYS ILE CYS
SEQRES 3 B 711 ASP PRO TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN
SEQRES 4 B 711 THR LYS ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL
SEQRES 5 B 711 PRO PHE LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS
SEQRES 6 B 711 GLU ARG MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER
SEQRES 7 B 711 CYS HIS PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR
SEQRES 8 B 711 ASN THR GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN
SEQRES 9 B 711 ASP SER LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO
SEQRES 10 B 711 ASN ILE LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY
SEQRES 11 B 711 TYR ALA PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY
SEQRES 12 B 711 LEU SER ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE
SEQRES 13 B 711 MET LYS VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU
SEQRES 14 B 711 GLU ARG VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP
SEQRES 15 B 711 GLY LYS GLY MET PHE TYR ASN SER TYR PRO GLN GLN ASP
SEQRES 16 B 711 GLY LYS SER ASP GLY THR GLU THR SER THR ASN LEU HIS
SEQRES 17 B 711 GLN LYS LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER
SEQRES 18 B 711 GLU ASP ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS
SEQRES 19 B 711 TRP MET GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR
SEQRES 20 B 711 VAL LEU LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN
SEQRES 21 B 711 ARG LEU TRP TYR CYS ASP LEU GLN GLN GLU SER SER GLY
SEQRES 22 B 711 ILE ALA GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN
SEQRES 23 B 711 PHE GLU GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR
SEQRES 24 B 711 VAL PHE THR PHE LYS THR ASN ARG GLN SER PRO ASN TYR
SEQRES 25 B 711 ARG VAL ILE ASN ILE ASP PHE ARG ASP PRO GLU GLU SER
SEQRES 26 B 711 LYS TRP LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL
SEQRES 27 B 711 LEU GLU TRP ILE ALA CYS VAL ARG SER ASN PHE LEU VAL
SEQRES 28 B 711 LEU CYS TYR LEU HIS ASP VAL LYS ASN ILE LEU GLN LEU
SEQRES 29 B 711 HIS ASP LEU THR THR GLY ALA LEU LEU LYS THR PHE PRO
SEQRES 30 B 711 LEU ASP VAL GLY SER ILE VAL GLY TYR SER GLY GLN LYS
SEQRES 31 B 711 LYS ASP THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU
SEQRES 32 B 711 SER PRO GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU
SEQRES 33 B 711 GLU LEU GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS
SEQRES 34 B 711 GLY ILE ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE
SEQRES 35 B 711 TYR PRO SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE
SEQRES 36 B 711 VAL HIS LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO
SEQRES 37 B 711 ALA PHE LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE
SEQRES 38 B 711 THR PRO ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG
SEQRES 39 B 711 HIS MET GLY GLY ILE LEU ALA VAL ALA ASN ILE ARG GLY
SEQRES 40 B 711 GLY GLY GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE
SEQRES 41 B 711 LEU ALA ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS
SEQRES 42 B 711 ALA ALA GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO
SEQRES 43 B 711 LYS ARG LEU THR ILE ASN GLY GLY SER ASN GLY GLY LEU
SEQRES 44 B 711 LEU VAL ALA ALA CYS ALA ASN GLN ARG PRO ASP LEU PHE
SEQRES 45 B 711 GLY CYS VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU
SEQRES 46 B 711 LYS PHE HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR
SEQRES 47 B 711 ASP TYR GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP
SEQRES 48 B 711 LEU VAL LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO
SEQRES 49 B 711 GLU ALA ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU
SEQRES 50 B 711 THR ALA ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER
SEQRES 51 B 711 LEU LYS PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG
SEQRES 52 B 711 SER ARG LYS GLN SER ASN PRO LEU LEU ILE HIS VAL ASP
SEQRES 53 B 711 THR LYS ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS
SEQRES 54 B 711 VAL ILE GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA
SEQRES 55 B 711 ARG CYS LEU ASN VAL ASP TRP ILE PRO
SEQRES 1 C 711 GLY MET LEU SER LEU GLN TYR PRO ASP VAL TYR ARG ASP
SEQRES 2 C 711 GLU THR ALA VAL GLN ASP TYR HIS GLY HIS LYS ILE CYS
SEQRES 3 C 711 ASP PRO TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN
SEQRES 4 C 711 THR LYS ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL
SEQRES 5 C 711 PRO PHE LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS
SEQRES 6 C 711 GLU ARG MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER
SEQRES 7 C 711 CYS HIS PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR
SEQRES 8 C 711 ASN THR GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN
SEQRES 9 C 711 ASP SER LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO
SEQRES 10 C 711 ASN ILE LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY
SEQRES 11 C 711 TYR ALA PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY
SEQRES 12 C 711 LEU SER ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE
SEQRES 13 C 711 MET LYS VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU
SEQRES 14 C 711 GLU ARG VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP
SEQRES 15 C 711 GLY LYS GLY MET PHE TYR ASN SER TYR PRO GLN GLN ASP
SEQRES 16 C 711 GLY LYS SER ASP GLY THR GLU THR SER THR ASN LEU HIS
SEQRES 17 C 711 GLN LYS LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER
SEQRES 18 C 711 GLU ASP ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS
SEQRES 19 C 711 TRP MET GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR
SEQRES 20 C 711 VAL LEU LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN
SEQRES 21 C 711 ARG LEU TRP TYR CYS ASP LEU GLN GLN GLU SER SER GLY
SEQRES 22 C 711 ILE ALA GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN
SEQRES 23 C 711 PHE GLU GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR
SEQRES 24 C 711 VAL PHE THR PHE LYS THR ASN ARG GLN SER PRO ASN TYR
SEQRES 25 C 711 ARG VAL ILE ASN ILE ASP PHE ARG ASP PRO GLU GLU SER
SEQRES 26 C 711 LYS TRP LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL
SEQRES 27 C 711 LEU GLU TRP ILE ALA CYS VAL ARG SER ASN PHE LEU VAL
SEQRES 28 C 711 LEU CYS TYR LEU HIS ASP VAL LYS ASN ILE LEU GLN LEU
SEQRES 29 C 711 HIS ASP LEU THR THR GLY ALA LEU LEU LYS THR PHE PRO
SEQRES 30 C 711 LEU ASP VAL GLY SER ILE VAL GLY TYR SER GLY GLN LYS
SEQRES 31 C 711 LYS ASP THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU
SEQRES 32 C 711 SER PRO GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU
SEQRES 33 C 711 GLU LEU GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS
SEQRES 34 C 711 GLY ILE ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE
SEQRES 35 C 711 TYR PRO SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE
SEQRES 36 C 711 VAL HIS LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO
SEQRES 37 C 711 ALA PHE LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE
SEQRES 38 C 711 THR PRO ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG
SEQRES 39 C 711 HIS MET GLY GLY ILE LEU ALA VAL ALA ASN ILE ARG GLY
SEQRES 40 C 711 GLY GLY GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE
SEQRES 41 C 711 LEU ALA ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS
SEQRES 42 C 711 ALA ALA GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO
SEQRES 43 C 711 LYS ARG LEU THR ILE ASN GLY GLY SER ASN GLY GLY LEU
SEQRES 44 C 711 LEU VAL ALA ALA CYS ALA ASN GLN ARG PRO ASP LEU PHE
SEQRES 45 C 711 GLY CYS VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU
SEQRES 46 C 711 LYS PHE HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR
SEQRES 47 C 711 ASP TYR GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP
SEQRES 48 C 711 LEU VAL LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO
SEQRES 49 C 711 GLU ALA ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU
SEQRES 50 C 711 THR ALA ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER
SEQRES 51 C 711 LEU LYS PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG
SEQRES 52 C 711 SER ARG LYS GLN SER ASN PRO LEU LEU ILE HIS VAL ASP
SEQRES 53 C 711 THR LYS ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS
SEQRES 54 C 711 VAL ILE GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA
SEQRES 55 C 711 ARG CYS LEU ASN VAL ASP TRP ILE PRO
HET GOL A 801 6
HET SCN A 802 3
HET SCN A 803 3
HET SCN A 804 3
HET GOL A 805 6
HET PEG A 806 7
HET PEG A 807 7
HET PEG A 808 5
HET SCN A 809 3
HET GOL A 810 6
HET GOL A 811 6
HET PEG A 812 7
HET B3P B 801 19
HET GOL B 802 6
HET GOL B 803 6
HET GOL B 804 6
HET GOL B 805 6
HET SCN B 806 3
HET PEG B 807 14
HET SCN B 808 3
HET PEG B 809 7
HET PEG B 810 7
HET GOL B 811 6
HET PEG C 801 7
HET PEG C 802 7
HET SCN C 803 3
HET PEG C 804 7
HET PEG C 805 7
HET SCN C 806 3
HETNAM GOL GLYCEROL
HETNAM SCN THIOCYANATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GOL 9(C3 H8 O3)
FORMUL 5 SCN 8(C N S 1-)
FORMUL 9 PEG 11(C4 H10 O3)
FORMUL 16 B3P C11 H26 N2 O6
FORMUL 33 HOH *2284(H2 O)
HELIX 1 AA1 TYR A 28 ASP A 33 5 6
HELIX 2 AA2 SER A 36 GLN A 56 1 21
HELIX 3 AA3 ILE A 59 TYR A 71 1 13
HELIX 4 AA4 ASP A 115 SER A 120 5 6
HELIX 5 AA5 ASP A 218 ASP A 222 5 5
HELIX 6 AA6 GLN A 267 GLU A 269 5 3
HELIX 7 AA7 GLU A 322 TRP A 326 5 5
HELIX 8 AA8 ASP A 431 SER A 433 5 3
HELIX 9 AA9 SER A 485 GLY A 496 1 12
HELIX 10 AB1 GLY A 511 GLY A 517 1 7
HELIX 11 AB2 GLY A 518 ALA A 521 5 4
HELIX 12 AB3 ASN A 522 GLU A 540 1 19
HELIX 13 AB4 SER A 544 LYS A 546 5 3
HELIX 14 AB5 SER A 554 ARG A 567 1 14
HELIX 15 AB6 PRO A 568 PHE A 571 5 4
HELIX 16 AB7 LYS A 585 TYR A 589 5 5
HELIX 17 AB8 ILE A 591 ALA A 594 5 4
HELIX 18 AB9 TRP A 595 GLY A 600 1 6
HELIX 19 AC1 SER A 604 VAL A 612 1 9
HELIX 20 AC2 SER A 615 ASN A 619 5 5
HELIX 21 AC3 PRO A 646 VAL A 660 1 15
HELIX 22 AC4 PRO A 685 ASN A 705 1 21
HELIX 23 AC5 TYR B 28 ASP B 33 5 6
HELIX 24 AC6 SER B 36 GLN B 56 1 21
HELIX 25 AC7 ILE B 59 TYR B 71 1 13
HELIX 26 AC8 ASP B 115 SER B 120 5 6
HELIX 27 AC9 ASP B 218 ASP B 222 5 5
HELIX 28 AD1 GLN B 267 GLU B 269 5 3
HELIX 29 AD2 GLU B 322 TRP B 326 5 5
HELIX 30 AD3 ASP B 431 SER B 433 5 3
HELIX 31 AD4 SER B 485 GLY B 496 1 12
HELIX 32 AD5 GLY B 511 GLY B 517 1 7
HELIX 33 AD6 GLY B 518 ALA B 521 5 4
HELIX 34 AD7 ASN B 522 GLU B 540 1 19
HELIX 35 AD8 SER B 544 LYS B 546 5 3
HELIX 36 AD9 SER B 554 ARG B 567 1 14
HELIX 37 AE1 PRO B 568 PHE B 571 5 4
HELIX 38 AE2 LYS B 585 TYR B 589 5 5
HELIX 39 AE3 ILE B 591 ALA B 594 5 4
HELIX 40 AE4 TRP B 595 GLY B 600 1 6
HELIX 41 AE5 SER B 604 SER B 615 1 12
HELIX 42 AE6 PRO B 616 ASN B 619 5 4
HELIX 43 AE7 PRO B 646 VAL B 660 1 15
HELIX 44 AE8 PRO B 685 ASN B 705 1 21
HELIX 45 AE9 TYR C 28 ASP C 33 5 6
HELIX 46 AF1 SER C 36 GLN C 56 1 21
HELIX 47 AF2 ILE C 59 ASP C 72 1 14
HELIX 48 AF3 ASP C 115 SER C 120 5 6
HELIX 49 AF4 ASP C 218 ASP C 222 5 5
HELIX 50 AF5 GLN C 267 GLU C 269 5 3
HELIX 51 AF6 GLU C 322 TRP C 326 5 5
HELIX 52 AF7 ASP C 431 SER C 433 5 3
HELIX 53 AF8 SER C 485 GLY C 496 1 12
HELIX 54 AF9 TYR C 510 GLY C 517 1 8
HELIX 55 AG1 GLY C 518 ASN C 522 5 5
HELIX 56 AG2 LYS C 523 GLU C 540 1 18
HELIX 57 AG3 SER C 544 LYS C 546 5 3
HELIX 58 AG4 SER C 554 ARG C 567 1 14
HELIX 59 AG5 PRO C 568 PHE C 571 5 4
HELIX 60 AG6 LYS C 585 TYR C 589 5 5
HELIX 61 AG7 ILE C 591 ALA C 594 5 4
HELIX 62 AG8 TRP C 595 GLY C 600 1 6
HELIX 63 AG9 SER C 604 VAL C 612 1 9
HELIX 64 AH1 SER C 615 ASN C 619 5 5
HELIX 65 AH2 PRO C 646 VAL C 660 1 15
HELIX 66 AH3 PRO C 685 ASN C 705 1 21
SHEET 1 AA1 2 VAL A 16 TYR A 19 0
SHEET 2 AA1 2 HIS A 22 CYS A 25 -1 O HIS A 22 N TYR A 19
SHEET 1 AA2 3 LYS A 75 TYR A 76 0
SHEET 2 AA2 3 ARG A 85 ASN A 91 -1 O ASN A 91 N LYS A 75
SHEET 3 AA2 3 PHE A 80 LYS A 82 -1 N LYS A 82 O ARG A 85
SHEET 1 AA3 4 LYS A 75 TYR A 76 0
SHEET 2 AA3 4 ARG A 85 ASN A 91 -1 O ASN A 91 N LYS A 75
SHEET 3 AA3 4 VAL A 99 GLN A 103 -1 O TYR A 101 N TYR A 88
SHEET 4 AA3 4 ARG A 111 LEU A 114 -1 O PHE A 113 N LEU A 100
SHEET 1 AA4 4 VAL A 125 PHE A 132 0
SHEET 2 AA4 4 TYR A 138 ALA A 145 -1 O GLY A 142 N GLY A 129
SHEET 3 AA4 4 VAL A 151 LYS A 157 -1 O LYS A 154 N TYR A 141
SHEET 4 AA4 4 LYS A 162 VAL A 171 -1 O VAL A 171 N VAL A 151
SHEET 1 AA5 4 ALA A 177 TRP A 178 0
SHEET 2 AA5 4 GLY A 184 SER A 189 -1 O PHE A 186 N ALA A 177
SHEET 3 AA5 4 LYS A 209 VAL A 214 -1 O LYS A 209 N SER A 189
SHEET 4 AA5 4 ILE A 223 ALA A 226 -1 O CYS A 225 N LEU A 210
SHEET 1 AA6 4 MET A 235 LEU A 240 0
SHEET 2 AA6 4 TYR A 246 ARG A 252 -1 O LEU A 248 N GLU A 239
SHEET 3 AA6 4 ARG A 260 ASP A 265 -1 O TRP A 262 N LEU A 249
SHEET 4 AA6 4 VAL A 280 ILE A 283 -1 O VAL A 280 N TYR A 263
SHEET 1 AA7 4 TYR A 290 GLU A 296 0
SHEET 2 AA7 4 VAL A 299 THR A 304 -1 O THR A 301 N THR A 294
SHEET 3 AA7 4 ARG A 312 ASP A 317 -1 O ILE A 316 N PHE A 300
SHEET 4 AA7 4 LYS A 327 VAL A 330 -1 O LYS A 327 N ASN A 315
SHEET 1 AA8 4 VAL A 337 VAL A 344 0
SHEET 2 AA8 4 PHE A 348 HIS A 355 -1 O VAL A 350 N ALA A 342
SHEET 3 AA8 4 LYS A 358 ASP A 365 -1 O GLN A 362 N LEU A 351
SHEET 4 AA8 4 LEU A 371 PHE A 375 -1 O LEU A 372 N LEU A 363
SHEET 1 AA9 4 SER A 381 SER A 386 0
SHEET 2 AA9 4 GLU A 393 THR A 399 -1 O THR A 399 N SER A 381
SHEET 3 AA9 4 ILE A 406 ASP A 411 -1 O TYR A 408 N TYR A 396
SHEET 4 AA9 4 ARG A 420 GLU A 424 -1 O ARG A 423 N ILE A 407
SHEET 1 AB1 8 TYR A 435 PRO A 443 0
SHEET 2 AB1 8 LYS A 449 LYS A 457 -1 O HIS A 456 N GLN A 436
SHEET 3 AB1 8 ILE A 498 ALA A 502 -1 O LEU A 499 N VAL A 455
SHEET 4 AB1 8 ALA A 468 TYR A 471 1 N PHE A 469 O ILE A 498
SHEET 5 AB1 8 LEU A 548 GLY A 553 1 O THR A 549 N ALA A 468
SHEET 6 AB1 8 CYS A 573 GLN A 577 1 O GLN A 577 N GLY A 552
SHEET 7 AB1 8 SER A 632 ALA A 638 1 O LEU A 634 N ALA A 576
SHEET 8 AB1 8 LEU A 670 ASP A 675 1 O LEU A 671 N MET A 633
SHEET 1 AB2 2 VAL B 16 TYR B 19 0
SHEET 2 AB2 2 HIS B 22 CYS B 25 -1 O ILE B 24 N GLN B 17
SHEET 1 AB3 3 LYS B 75 TYR B 76 0
SHEET 2 AB3 3 ARG B 85 ASN B 91 -1 O ASN B 91 N LYS B 75
SHEET 3 AB3 3 PHE B 80 LYS B 82 -1 N LYS B 82 O ARG B 85
SHEET 1 AB4 4 LYS B 75 TYR B 76 0
SHEET 2 AB4 4 ARG B 85 ASN B 91 -1 O ASN B 91 N LYS B 75
SHEET 3 AB4 4 VAL B 99 GLN B 103 -1 O TYR B 101 N TYR B 88
SHEET 4 AB4 4 ARG B 111 LEU B 114 -1 O PHE B 113 N LEU B 100
SHEET 1 AB5 4 VAL B 125 PHE B 132 0
SHEET 2 AB5 4 TYR B 138 ALA B 145 -1 O ALA B 140 N ALA B 131
SHEET 3 AB5 4 VAL B 151 LYS B 157 -1 O LYS B 154 N TYR B 141
SHEET 4 AB5 4 LYS B 162 VAL B 171 -1 O VAL B 171 N VAL B 151
SHEET 1 AB6 4 MET B 176 TRP B 178 0
SHEET 2 AB6 4 GLY B 184 SER B 189 -1 O PHE B 186 N ALA B 177
SHEET 3 AB6 4 LYS B 209 VAL B 214 -1 O TYR B 211 N TYR B 187
SHEET 4 AB6 4 ILE B 223 ALA B 226 -1 O CYS B 225 N LEU B 210
SHEET 1 AB7 4 MET B 235 LEU B 240 0
SHEET 2 AB7 4 TYR B 246 ARG B 252 -1 O LEU B 248 N GLU B 239
SHEET 3 AB7 4 ARG B 260 ASP B 265 -1 O TRP B 262 N LEU B 249
SHEET 4 AB7 4 VAL B 280 ILE B 283 -1 O VAL B 280 N TYR B 263
SHEET 1 AB8 4 TYR B 290 GLU B 296 0
SHEET 2 AB8 4 VAL B 299 THR B 304 -1 O LYS B 303 N ASP B 291
SHEET 3 AB8 4 ARG B 312 ASP B 317 -1 O ILE B 316 N PHE B 300
SHEET 4 AB8 4 LYS B 327 VAL B 330 -1 O LYS B 327 N ASN B 315
SHEET 1 AB9 4 VAL B 337 VAL B 344 0
SHEET 2 AB9 4 PHE B 348 HIS B 355 -1 O VAL B 350 N ALA B 342
SHEET 3 AB9 4 LYS B 358 ASP B 365 -1 O LYS B 358 N HIS B 355
SHEET 4 AB9 4 LEU B 371 PHE B 375 -1 O LEU B 372 N LEU B 363
SHEET 1 AC1 4 SER B 381 SER B 386 0
SHEET 2 AC1 4 GLU B 393 THR B 399 -1 O THR B 399 N SER B 381
SHEET 3 AC1 4 ILE B 406 ASP B 411 -1 O TYR B 408 N TYR B 396
SHEET 4 AC1 4 ARG B 420 GLU B 424 -1 O PHE B 422 N ILE B 407
SHEET 1 AC2 8 TYR B 435 PRO B 443 0
SHEET 2 AC2 8 LYS B 449 LYS B 457 -1 O ILE B 450 N TYR B 442
SHEET 3 AC2 8 ILE B 498 ALA B 502 -1 O LEU B 499 N VAL B 455
SHEET 4 AC2 8 ALA B 468 TYR B 471 1 N PHE B 469 O ALA B 500
SHEET 5 AC2 8 LEU B 548 GLY B 553 1 O THR B 549 N LEU B 470
SHEET 6 AC2 8 CYS B 573 GLN B 577 1 O GLN B 577 N GLY B 552
SHEET 7 AC2 8 SER B 632 ALA B 638 1 O LEU B 636 N ALA B 576
SHEET 8 AC2 8 LEU B 670 ASP B 675 1 O ASP B 675 N THR B 637
SHEET 1 AC3 2 VAL C 16 TYR C 19 0
SHEET 2 AC3 2 HIS C 22 CYS C 25 -1 O ILE C 24 N GLN C 17
SHEET 1 AC4 3 LYS C 75 TYR C 76 0
SHEET 2 AC4 3 ARG C 85 ASN C 91 -1 O ASN C 91 N LYS C 75
SHEET 3 AC4 3 PHE C 80 LYS C 82 -1 N LYS C 82 O ARG C 85
SHEET 1 AC5 4 LYS C 75 TYR C 76 0
SHEET 2 AC5 4 ARG C 85 ASN C 91 -1 O ASN C 91 N LYS C 75
SHEET 3 AC5 4 VAL C 99 GLN C 103 -1 O TYR C 101 N TYR C 88
SHEET 4 AC5 4 ALA C 110 LEU C 114 -1 O PHE C 113 N LEU C 100
SHEET 1 AC6 4 VAL C 125 PHE C 132 0
SHEET 2 AC6 4 TYR C 138 ALA C 145 -1 O GLY C 142 N GLY C 129
SHEET 3 AC6 4 VAL C 151 LYS C 157 -1 O MET C 156 N PHE C 139
SHEET 4 AC6 4 LYS C 162 VAL C 171 -1 O VAL C 171 N VAL C 151
SHEET 1 AC7 4 MET C 176 TRP C 178 0
SHEET 2 AC7 4 GLY C 184 SER C 189 -1 O PHE C 186 N ALA C 177
SHEET 3 AC7 4 LYS C 209 VAL C 214 -1 O LYS C 209 N SER C 189
SHEET 4 AC7 4 ILE C 223 ALA C 226 -1 O CYS C 225 N LEU C 210
SHEET 1 AC8 4 MET C 235 LEU C 240 0
SHEET 2 AC8 4 TYR C 246 ARG C 252 -1 O LEU C 248 N GLU C 239
SHEET 3 AC8 4 ARG C 260 ASP C 265 -1 O TRP C 262 N LEU C 249
SHEET 4 AC8 4 VAL C 280 ILE C 283 -1 O VAL C 280 N TYR C 263
SHEET 1 AC9 4 TYR C 290 GLU C 296 0
SHEET 2 AC9 4 VAL C 299 THR C 304 -1 O THR C 301 N VAL C 293
SHEET 3 AC9 4 ARG C 312 ASP C 317 -1 O ARG C 312 N THR C 304
SHEET 4 AC9 4 LYS C 327 VAL C 330 -1 O LEU C 329 N VAL C 313
SHEET 1 AD1 4 VAL C 337 VAL C 344 0
SHEET 2 AD1 4 PHE C 348 HIS C 355 -1 O VAL C 350 N ALA C 342
SHEET 3 AD1 4 LYS C 358 ASP C 365 -1 O LYS C 358 N HIS C 355
SHEET 4 AD1 4 LEU C 371 PHE C 375 -1 O LEU C 372 N LEU C 363
SHEET 1 AD2 4 SER C 381 SER C 386 0
SHEET 2 AD2 4 GLU C 393 THR C 399 -1 O THR C 399 N SER C 381
SHEET 3 AD2 4 ILE C 406 ASP C 411 -1 O ILE C 406 N PHE C 398
SHEET 4 AD2 4 ARG C 420 GLU C 424 -1 O ARG C 423 N ILE C 407
SHEET 1 AD3 8 TYR C 435 PRO C 443 0
SHEET 2 AD3 8 LYS C 449 LYS C 457 -1 O ILE C 450 N TYR C 442
SHEET 3 AD3 8 ILE C 498 ALA C 502 -1 O VAL C 501 N PHE C 453
SHEET 4 AD3 8 ALA C 468 TYR C 471 1 N TYR C 471 O ALA C 500
SHEET 5 AD3 8 LEU C 548 GLY C 553 1 O THR C 549 N LEU C 470
SHEET 6 AD3 8 CYS C 573 GLN C 577 1 O ILE C 575 N ILE C 550
SHEET 7 AD3 8 SER C 632 ALA C 638 1 O LEU C 634 N VAL C 574
SHEET 8 AD3 8 LEU C 670 ASP C 675 1 O LEU C 671 N MET C 633
CRYST1 106.124 66.880 158.024 90.00 100.29 90.00 P 1 21 1 6
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 0.009423 0.000000 0.001711 0.00000
SCALE2 0.000000 0.014952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006432 0.00000
TER 5744 PRO A 710
TER 11502 PRO B 710
TER 17207 PRO C 710
MASTER 591 0 29 66 123 0 0 619467 3 179 165
END |