HEADER HYDROLASE 12-DEC-17 6BV1
TITLE CRYSTAL STRUCTURE OF PORCINE AMINOPEPTIDASE-N WITH ASPARTIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE N;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PAPN,ALANYL AMINOPEPTIDASE,AMINOPEPTIDASE M,AP-M,MICROSOMAL
COMPND 5 AMINOPEPTIDASE,GP130;
COMPND 6 EC: 3.4.11.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: ANPEP;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS ZINC AMINOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CHEN,Y.-L.LIN,F.LI
REVDAT 5 04-OCT-23 6BV1 1 HETSYN
REVDAT 4 29-JUL-20 6BV1 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 18-DEC-19 6BV1 1 REMARK
REVDAT 2 14-FEB-18 6BV1 1 REMARK
REVDAT 1 17-JAN-18 6BV1 0
JRNL AUTH S.JOSHI,L.CHEN,M.B.WINTER,Y.L.LIN,Y.YANG,M.SHAPOVALOVA,
JRNL AUTH 2 P.M.SMITH,C.LIU,F.LI,A.M.LEBEAU
JRNL TITL THE RATIONAL DESIGN OF THERAPEUTIC PEPTIDES FOR
JRNL TITL 2 AMINOPEPTIDASE N USING A SUBSTRATE-BASED APPROACH.
JRNL REF SCI REP V. 7 1424 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28465619
JRNL DOI 10.1038/S41598-017-01542-5
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 81490
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4288
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5874
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 336
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 382
REMARK 3 SOLVENT ATOMS : 842
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.77000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.537
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.167
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.165
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.896
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7824 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 6859 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10704 ; 1.132 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16005 ; 1.960 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 901 ; 7.333 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 367 ;41.095 ;24.986
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1218 ;16.176 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;18.689 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1227 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8479 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1546 ; 0.005 ; 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): 3610 ; 1.628 ; 2.529
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3609 ; 1.627 ; 2.529
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4509 ; 1.758 ; 3.783
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4510 ; 1.758 ; 3.784
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4213 ; 1.583 ; 2.668
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4170 ; 1.533 ; 2.656
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6136 ; 1.575 ; 3.965
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 34578 ; 1.871 ;49.190
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 33733 ; 1.830 ;48.775
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 14682 ; 6.026 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 198 ; 6.025 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 15126 ; 3.142 ; 5.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 63 A 281
REMARK 3 RESIDUE RANGE : A 282 A 543
REMARK 3 RESIDUE RANGE : A 544 A 632
REMARK 3 RESIDUE RANGE : A 633 A 964
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8539 18.2570 59.8344
REMARK 3 T TENSOR
REMARK 3 T11: 0.0499 T22: 0.0268
REMARK 3 T33: 0.0466 T12: -0.0094
REMARK 3 T13: -0.0063 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.5336 L22: 0.2012
REMARK 3 L33: 0.2600 L12: -0.1285
REMARK 3 L13: -0.0496 L23: -0.0622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0092 S12: 0.0191 S13: 0.0398
REMARK 3 S21: -0.0357 S22: -0.0112 S23: 0.0669
REMARK 3 S31: 0.0033 S32: -0.0683 S33: 0.0020
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0814 T22: 0.0814
REMARK 3 T33: 0.0814 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6BV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1000231660.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85779
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.6400
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.57400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.550
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4FKE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 200 MM LITHIUM SULFATE,
REMARK 280 100 MM HEPES, PH 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 129.90500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.34100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 129.90500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.34100
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 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 OD1 ASP A 849 O HOH A 1101 1.76
REMARK 500 NH1 ARG A 69 O2 SO4 A 1034 1.93
REMARK 500 OE1 GLU A 176 O HOH A 1102 2.01
REMARK 500 OE1 GLU A 281 O HOH A 1103 2.03
REMARK 500 OD1 ASP A 779 O HOH A 1104 2.04
REMARK 500 O2 SO4 A 1026 O HOH A 1105 2.05
REMARK 500 O HOH A 1861 O HOH A 1866 2.06
REMARK 500 O HOH A 1376 O HOH A 1509 2.08
REMARK 500 O HOH A 1814 O HOH A 1849 2.09
REMARK 500 O HOH A 1473 O HOH A 1669 2.10
REMARK 500 OE1 GLU A 111 O HOH A 1106 2.11
REMARK 500 OE1 GLN A 283 O HOH A 1107 2.13
REMARK 500 O HOH A 1712 O HOH A 1918 2.15
REMARK 500 O HOH A 1514 O HOH A 1746 2.15
REMARK 500 O HOH A 1144 O HOH A 1561 2.16
REMARK 500 O HOH A 1407 O HOH A 1590 2.16
REMARK 500 O HOH A 1872 O HOH A 1935 2.18
REMARK 500 O HOH A 1732 O HOH A 1813 2.19
REMARK 500 O5 NAG D 1 O3 SO4 A 1033 2.19
REMARK 500 O HOH A 1830 O HOH A 1917 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 O1 SO4 A 1029 O HOH A 1213 2556 2.07
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 ALA A 93 -15.30 86.66
REMARK 500 ASP A 220 58.62 -93.00
REMARK 500 ASP A 256 96.98 -163.47
REMARK 500 PHE A 344 96.67 -69.22
REMARK 500 GLU A 350 35.11 -83.83
REMARK 500 TRP A 389 -62.31 -109.78
REMARK 500 SER A 447 -173.14 -67.28
REMARK 500 THR A 487 146.52 68.86
REMARK 500 GLN A 505 -161.07 -126.41
REMARK 500 ASN A 620 64.98 66.60
REMARK 500 ASP A 779 69.24 -157.83
REMARK 500 LYS A 882 63.69 -48.57
REMARK 500 LYS A 883 17.07 -169.85
REMARK 500 PHE A 893 -60.46 103.23
REMARK 500 SER A 894 55.80 77.75
REMARK 500 PHE A 895 -30.30 -37.65
REMARK 500 SER A 907 16.06 -150.43
REMARK 500 LYS A 920 13.60 -64.55
REMARK 500 ASN A 921 49.23 -93.57
REMARK 500 MET A 923 58.00 -62.92
REMARK 500 ASP A 924 164.31 124.71
REMARK 500 VAL A 925 -41.56 56.41
REMARK 500 PHE A 927 -13.32 -146.67
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 A1939 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A1940 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A1941 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A1942 DISTANCE = 7.18 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1035 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 383 NE2
REMARK 620 2 HIS A 387 NE2 108.3
REMARK 620 3 GLU A 406 OE2 104.7 99.6
REMARK 620 4 HOH A1176 O 106.4 104.3 131.9
REMARK 620 N 1 2 3
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE INHIBITOR
REMARK 630 MOLECULE NAME: 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 NAG A 1020
REMARK 630 NAG A 1023
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
DBREF 6BV1 A 63 963 UNP P15145 AMPN_PIG 63 963
SEQADV 6BV1 PHE A 107 UNP P15145 LEU 107 CONFLICT
SEQADV 6BV1 SER A 964 UNP P15145 EXPRESSION TAG
SEQRES 1 A 902 GLN SER LYS PRO TRP ASN ARG TYR ARG LEU PRO THR THR
SEQRES 2 A 902 LEU LEU PRO ASP SER TYR ASN VAL THR LEU ARG PRO TYR
SEQRES 3 A 902 LEU THR PRO ASN ALA ASP GLY LEU TYR ILE PHE LYS GLY
SEQRES 4 A 902 LYS SER ILE VAL ARG PHE LEU CYS GLN GLU PRO THR ASP
SEQRES 5 A 902 VAL ILE ILE ILE HIS SER LYS LYS LEU ASN TYR THR THR
SEQRES 6 A 902 GLN GLY HIS MET VAL VAL LEU ARG GLY VAL GLY ASP SER
SEQRES 7 A 902 GLN VAL PRO GLU ILE ASP ARG THR GLU LEU VAL GLU LEU
SEQRES 8 A 902 THR GLU TYR LEU VAL VAL HIS LEU LYS GLY SER LEU GLN
SEQRES 9 A 902 PRO GLY HIS MET TYR GLU MET GLU SER GLU PHE GLN GLY
SEQRES 10 A 902 GLU LEU ALA ASP ASP LEU ALA GLY PHE TYR ARG SER GLU
SEQRES 11 A 902 TYR MET GLU GLY ASN VAL LYS LYS VAL LEU ALA THR THR
SEQRES 12 A 902 GLN MET GLN SER THR ASP ALA ARG LYS SER PHE PRO CYS
SEQRES 13 A 902 PHE ASP GLU PRO ALA MET LYS ALA THR PHE ASN ILE THR
SEQRES 14 A 902 LEU ILE HIS PRO ASN ASN LEU THR ALA LEU SER ASN MET
SEQRES 15 A 902 PRO PRO LYS GLY SER SER THR PRO LEU ALA GLU ASP PRO
SEQRES 16 A 902 ASN TRP SER VAL THR GLU PHE GLU THR THR PRO VAL MET
SEQRES 17 A 902 SER THR TYR LEU LEU ALA TYR ILE VAL SER GLU PHE GLN
SEQRES 18 A 902 SER VAL ASN GLU THR ALA GLN ASN GLY VAL LEU ILE ARG
SEQRES 19 A 902 ILE TRP ALA ARG PRO ASN ALA ILE ALA GLU GLY HIS GLY
SEQRES 20 A 902 MET TYR ALA LEU ASN VAL THR GLY PRO ILE LEU ASN PHE
SEQRES 21 A 902 PHE ALA ASN HIS TYR ASN THR SER TYR PRO LEU PRO LYS
SEQRES 22 A 902 SER ASP GLN ILE ALA LEU PRO ASP PHE ASN ALA GLY ALA
SEQRES 23 A 902 MET GLU ASN TRP GLY LEU VAL THR TYR ARG GLU ASN ALA
SEQRES 24 A 902 LEU LEU PHE ASP PRO GLN SER SER SER ILE SER ASN LYS
SEQRES 25 A 902 GLU ARG VAL VAL THR VAL ILE ALA HIS GLU LEU ALA HIS
SEQRES 26 A 902 GLN TRP PHE GLY ASN LEU VAL THR LEU ALA TRP TRP ASN
SEQRES 27 A 902 ASP LEU TRP LEU ASN GLU GLY PHE ALA SER TYR VAL GLU
SEQRES 28 A 902 TYR LEU GLY ALA ASP HIS ALA GLU PRO THR TRP ASN LEU
SEQRES 29 A 902 LYS ASP LEU ILE VAL PRO GLY ASP VAL TYR ARG VAL MET
SEQRES 30 A 902 ALA VAL ASP ALA LEU ALA SER SER HIS PRO LEU THR THR
SEQRES 31 A 902 PRO ALA GLU GLU VAL ASN THR PRO ALA GLN ILE SER GLU
SEQRES 32 A 902 MET PHE ASP SER ILE SER TYR SER LYS GLY ALA SER VAL
SEQRES 33 A 902 ILE ARG MET LEU SER ASN PHE LEU THR GLU ASP LEU PHE
SEQRES 34 A 902 LYS GLU GLY LEU ALA SER TYR LEU HIS ALA PHE ALA TYR
SEQRES 35 A 902 GLN ASN THR THR TYR LEU ASP LEU TRP GLU HIS LEU GLN
SEQRES 36 A 902 LYS ALA VAL ASP ALA GLN THR SER ILE ARG LEU PRO ASP
SEQRES 37 A 902 THR VAL ARG ALA ILE MET ASP ARG TRP THR LEU GLN MET
SEQRES 38 A 902 GLY PHE PRO VAL ILE THR VAL ASP THR LYS THR GLY ASN
SEQRES 39 A 902 ILE SER GLN LYS HIS PHE LEU LEU ASP SER GLU SER ASN
SEQRES 40 A 902 VAL THR ARG SER SER ALA PHE ASP TYR LEU TRP ILE VAL
SEQRES 41 A 902 PRO ILE SER SER ILE LYS ASN GLY VAL MET GLN ASP HIS
SEQRES 42 A 902 TYR TRP LEU ARG ASP VAL SER GLN ALA GLN ASN ASP LEU
SEQRES 43 A 902 PHE LYS THR ALA SER ASP ASP TRP VAL LEU LEU ASN VAL
SEQRES 44 A 902 ASN VAL THR GLY TYR PHE GLN VAL ASN TYR ASP GLU ASP
SEQRES 45 A 902 ASN TRP ARG MET ILE GLN HIS GLN LEU GLN THR ASN LEU
SEQRES 46 A 902 SER VAL ILE PRO VAL ILE ASN ARG ALA GLN VAL ILE TYR
SEQRES 47 A 902 ASP SER PHE ASN LEU ALA THR ALA HIS MET VAL PRO VAL
SEQRES 48 A 902 THR LEU ALA LEU ASP ASN THR LEU PHE LEU ASN GLY GLU
SEQRES 49 A 902 LYS GLU TYR MET PRO TRP GLN ALA ALA LEU SER SER LEU
SEQRES 50 A 902 SER TYR PHE SER LEU MET PHE ASP ARG SER GLU VAL TYR
SEQRES 51 A 902 GLY PRO MET LYS LYS TYR LEU ARG LYS GLN VAL GLU PRO
SEQRES 52 A 902 LEU PHE GLN HIS PHE GLU THR LEU THR LYS ASN TRP THR
SEQRES 53 A 902 GLU ARG PRO GLU ASN LEU MET ASP GLN TYR SER GLU ILE
SEQRES 54 A 902 ASN ALA ILE SER THR ALA CYS SER ASN GLY LEU PRO GLN
SEQRES 55 A 902 CYS GLU ASN LEU ALA LYS THR LEU PHE ASP GLN TRP MET
SEQRES 56 A 902 SER ASP PRO GLU ASN ASN PRO ILE HIS PRO ASN LEU ARG
SEQRES 57 A 902 SER THR ILE TYR CYS ASN ALA ILE ALA GLN GLY GLY GLN
SEQRES 58 A 902 ASP GLN TRP ASP PHE ALA TRP GLY GLN LEU GLN GLN ALA
SEQRES 59 A 902 GLN LEU VAL ASN GLU ALA ASP LYS LEU ARG SER ALA LEU
SEQRES 60 A 902 ALA CYS SER ASN GLU VAL TRP LEU LEU ASN ARG TYR LEU
SEQRES 61 A 902 GLY TYR THR LEU ASN PRO ASP LEU ILE ARG LYS GLN ASP
SEQRES 62 A 902 ALA THR SER THR ILE ASN SER ILE ALA SER ASN VAL ILE
SEQRES 63 A 902 GLY GLN PRO LEU ALA TRP ASP PHE VAL GLN SER ASN TRP
SEQRES 64 A 902 LYS LYS LEU PHE GLN ASP TYR GLY GLY GLY SER PHE SER
SEQRES 65 A 902 PHE SER ASN LEU ILE GLN GLY VAL THR ARG ARG PHE SER
SEQRES 66 A 902 SER GLU PHE GLU LEU GLN GLN LEU GLU GLN PHE LYS LYS
SEQRES 67 A 902 ASN ASN MET ASP VAL GLY PHE GLY SER GLY THR ARG ALA
SEQRES 68 A 902 LEU GLU GLN ALA LEU GLU LYS THR LYS ALA ASN ILE LYS
SEQRES 69 A 902 TRP VAL LYS GLU ASN LYS GLU VAL VAL LEU ASN TRP PHE
SEQRES 70 A 902 ILE GLU HIS SER SER
HET NAG B 1 14
HET NAG B 2 14
HET NAG B 3 14
HET NAG C 1 14
HET NAG C 2 14
HET NAG C 3 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG F 3 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG A1020 14
HET NAG A1023 14
HET ASP A1024 9
HET SO4 A1025 5
HET SO4 A1026 5
HET SO4 A1027 5
HET SO4 A1028 5
HET SO4 A1029 5
HET SO4 A1030 5
HET SO4 A1031 5
HET SO4 A1032 5
HET SO4 A1033 5
HET SO4 A1034 5
HET ZN A1035 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ASP ASPARTIC ACID
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 23(C8 H15 N O6)
FORMUL 13 ASP C4 H7 N O4
FORMUL 14 SO4 10(O4 S 2-)
FORMUL 24 ZN ZN 2+
FORMUL 25 HOH *842(H2 O)
HELIX 1 AA1 LYS A 65 ARG A 69 5 5
HELIX 2 AA2 ASP A 211 SER A 215 5 5
HELIX 3 AA3 SER A 271 LEU A 275 5 5
HELIX 4 AA4 ARG A 300 GLU A 306 1 7
HELIX 5 AA5 GLY A 309 TYR A 327 1 19
HELIX 6 AA6 GLU A 359 LEU A 363 1 5
HELIX 7 AA7 SER A 370 HIS A 387 1 18
HELIX 8 AA8 TRP A 398 ASN A 400 5 3
HELIX 9 AA9 ASP A 401 GLU A 421 1 21
HELIX 10 AB1 ASN A 425 ASP A 428 5 4
HELIX 11 AB2 LEU A 429 ASP A 434 1 6
HELIX 12 AB3 ASP A 434 ALA A 443 1 10
HELIX 13 AB4 PRO A 453 VAL A 457 5 5
HELIX 14 AB5 THR A 459 GLU A 465 1 7
HELIX 15 AB6 ASP A 468 THR A 487 1 20
HELIX 16 AB7 THR A 487 ALA A 503 1 17
HELIX 17 AB8 THR A 508 ALA A 522 1 15
HELIX 18 AB9 THR A 531 LEU A 541 1 11
HELIX 19 AC1 ASP A 607 LYS A 610 5 4
HELIX 20 AC2 VAL A 621 THR A 624 5 4
HELIX 21 AC3 ASP A 632 ASN A 646 1 15
HELIX 22 AC4 LEU A 647 ILE A 650 5 4
HELIX 23 AC5 PRO A 651 ALA A 668 1 18
HELIX 24 AC6 PRO A 672 ASN A 679 1 8
HELIX 25 AC7 THR A 680 GLU A 686 5 7
HELIX 26 AC8 GLU A 688 ASP A 707 1 20
HELIX 27 AC9 VAL A 711 THR A 734 1 24
HELIX 28 AD1 ASN A 743 ASN A 760 1 18
HELIX 29 AD2 LEU A 762 SER A 778 1 17
HELIX 30 AD3 LEU A 789 GLY A 801 1 13
HELIX 31 AD4 GLY A 802 ALA A 816 1 15
HELIX 32 AD5 LEU A 818 ALA A 830 1 13
HELIX 33 AD6 GLU A 834 GLY A 843 1 10
HELIX 34 AD7 ARG A 852 GLN A 854 5 3
HELIX 35 AD8 ASP A 855 ASN A 866 1 12
HELIX 36 AD9 ILE A 868 ASN A 880 1 13
HELIX 37 AE1 LYS A 883 TYR A 888 1 6
HELIX 38 AE2 SER A 894 ARG A 904 1 11
HELIX 39 AE3 SER A 908 LYS A 920 1 13
HELIX 40 AE4 PHE A 927 SER A 929 5 3
HELIX 41 AE5 GLY A 930 SER A 963 1 34
SHEET 1 AA1 3 ASN A 124 TYR A 125 0
SHEET 2 AA1 3 MET A 170 GLU A 180 -1 O GLN A 178 N ASN A 124
SHEET 3 AA1 3 VAL A 133 GLY A 136 -1 N VAL A 133 O GLU A 174
SHEET 1 AA2 7 ASN A 124 TYR A 125 0
SHEET 2 AA2 7 MET A 170 GLU A 180 -1 O GLN A 178 N ASN A 124
SHEET 3 AA2 7 ILE A 98 CYS A 109 -1 N GLY A 101 O PHE A 177
SHEET 4 AA2 7 LEU A 76 PRO A 87 -1 N ASP A 79 O ARG A 106
SHEET 5 AA2 7 THR A 227 PRO A 235 1 O ASN A 229 N VAL A 83
SHEET 6 AA2 7 TRP A 259 GLU A 263 -1 O SER A 260 N HIS A 234
SHEET 7 AA2 7 THR A 251 PRO A 252 -1 N THR A 251 O VAL A 261
SHEET 1 AA3 3 THR A 113 HIS A 119 0
SHEET 2 AA3 3 TYR A 156 LEU A 165 -1 O LEU A 157 N ILE A 118
SHEET 3 AA3 3 ILE A 145 VAL A 151 -1 N ASP A 146 O HIS A 160
SHEET 1 AA4 2 GLY A 187 GLU A 195 0
SHEET 2 AA4 2 VAL A 198 GLN A 206 -1 O LYS A 200 N TYR A 193
SHEET 1 AA5 2 THR A 239 SER A 242 0
SHEET 2 AA5 2 TYR A 277 SER A 280 -1 O SER A 280 N THR A 239
SHEET 1 AA6 5 GLN A 283 THR A 288 0
SHEET 2 AA6 5 LEU A 294 ALA A 299 -1 O ILE A 295 N GLU A 287
SHEET 3 AA6 5 LYS A 335 LEU A 341 1 O GLN A 338 N TRP A 298
SHEET 4 AA6 5 LEU A 354 ARG A 358 1 O TYR A 357 N LEU A 341
SHEET 5 AA6 5 ALA A 348 MET A 349 -1 N MET A 349 O THR A 356
SHEET 1 AA7 2 THR A 395 LEU A 396 0
SHEET 2 AA7 2 ASN A 506 THR A 507 1 O THR A 507 N THR A 395
SHEET 1 AA8 4 GLN A 603 GLN A 605 0
SHEET 2 AA8 4 ASN A 556 HIS A 561 -1 N ILE A 557 O ALA A 604
SHEET 3 AA8 4 PRO A 546 VAL A 550 -1 N VAL A 547 O LYS A 560
SHEET 4 AA8 4 GLN A 628 TYR A 631 1 O GLN A 628 N ILE A 548
SHEET 1 AA9 2 VAL A 582 ILE A 584 0
SHEET 2 AA9 2 TYR A 596 LEU A 598 -1 O TYR A 596 N ILE A 584
SHEET 1 AB1 3 VAL A 591 MET A 592 0
SHEET 2 AB1 3 SER A 586 LYS A 588 -1 N LYS A 588 O VAL A 591
SHEET 3 AB1 3 VAL A 617 LEU A 619 -1 O LEU A 618 N ILE A 587
SSBOND 1 CYS A 758 CYS A 765 1555 1555 2.05
SSBOND 2 CYS A 795 CYS A 831 1555 1555 2.05
LINK ND2 ASN A 82 C1 NAG B 1 1555 1555 1.44
LINK ND2 ASN A 124 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 237 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 314 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN A 328 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN A 506 C1 NAG H 1 1555 1555 1.42
LINK ND2 ASN A 556 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN A 569 C1 NAG A1020 1555 1555 1.45
LINK ND2 ASN A 622 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN A 646 C1 NAG A1023 1555 1555 1.46
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG B 2 C1 NAG B 3 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 NAG C 3 1555 1555 1.46
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.46
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46
LINK O4 NAG F 2 C1 NAG F 3 1555 1555 1.46
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.46
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.47
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK NE2 HIS A 383 ZN ZN A1035 1555 1555 2.13
LINK NE2 HIS A 387 ZN ZN A1035 1555 1555 2.13
LINK OE2 GLU A 406 ZN ZN A1035 1555 1555 1.93
LINK ZN ZN A1035 O HOH A1176 1555 1555 2.19
CISPEP 1 GLN A 208 SER A 209 0 -3.05
CRYST1 259.810 62.682 81.717 90.00 100.40 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 0.003849 0.000000 0.000707 0.00000
SCALE2 0.000000 0.015954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012442 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
