HEADER HYDROLASE/HYDROLASE INHIBITOR 02-NOV-13 4NGS
TITLE CRYSTAL STRUCTURE OF GLUTAMATE CARBOXYPEPTIDASE II IN A COMPLEX WITH
TITLE 2 UREA-BASED INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE CARBOXYPEPTIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 44-750;
COMPND 5 SYNONYM: CELL GROWTH-INHIBITING GENE 27 PROTEIN, FOLATE HYDROLASE 1,
COMPND 6 FOLYLPOLY-GAMMA-GLUTAMATE CARBOXYPEPTIDASE, FGCP, GLUTAMATE
COMPND 7 CARBOXYPEPTIDASE II, GCPII, MEMBRANE GLUTAMATE CARBOXYPEPTIDASE,
COMPND 8 MGCP, N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE I, NAALADASE I,
COMPND 9 PROSTATE-SPECIFIC MEMBRANE ANTIGEN, PSM, PSMA, PTEROYLPOLY-GAMMA-
COMPND 10 GLUTAMATE CARBOXYPEPTIDASE;
COMPND 11 EC: 3.4.17.21;
COMPND 12 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: FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER 2(S2) CELLS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMT/BIP
KEYWDS HYDROLASE, GLUTAMATE CARBOXYPEPTIDASE II, PSMA, NAALADASE, UREA-BASED
KEYWDS 2 INHIBITOR, CABOXYPEPTIDASE, GLYCOPROTEIN, METALLOPEPTIDASE,
KEYWDS 3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.TYKVART,P.PACHL
REVDAT 3 29-JUL-20 4NGS 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 18-DEC-19 4NGS 1 JRNL SEQADV LINK
REVDAT 1 18-JUN-14 4NGS 0
JRNL AUTH J.TYKVART,J.SCHIMER,J.BARINKOVA,P.PACHL,
JRNL AUTH 2 L.POSTOVA-SLAVETINSKA,P.MAJER,J.KONVALINKA,P.SACHA
JRNL TITL RATIONAL DESIGN OF UREA-BASED GLUTAMATE CARBOXYPEPTIDASE II
JRNL TITL 2 (GCPII) INHIBITORS AS VERSATILE TOOLS FOR SPECIFIC DRUG
JRNL TITL 3 TARGETING AND DELIVERY.
JRNL REF BIOORG.MED.CHEM. V. 22 4099 2014
JRNL REFN ESSN 1464-3391
JRNL PMID 24954515
JRNL DOI 10.1016/J.BMC.2014.05.061
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 119023
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5952
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8034
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 423
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 232
REMARK 3 SOLVENT ATOMS : 551
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : 0.17000
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): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.841
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5953 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8102 ; 1.939 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 709 ; 5.995 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 270 ;36.942 ;23.778
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 917 ;13.999 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;14.623 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 874 ; 0.138 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4597 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2800 ; 1.992 ; 2.234
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3503 ; 2.720 ; 3.345
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3153 ; 3.010 ; 2.571
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4NGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119024
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 42.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.650
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 (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, PEG 3350, PENTAERYTHRITOL
REMARK 280 PROPOXYLATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 50.72250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.02300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 79.56150
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.72250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.02300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.56150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.72250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.02300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 79.56150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 50.72250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.02300
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 79.56150
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -101.44500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 978 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG A 12
REMARK 465 SER A 13
REMARK 465 GLY A 14
REMARK 465 LEU A 15
REMARK 465 ASN A 16
REMARK 465 ASP A 17
REMARK 465 ILE A 18
REMARK 465 PHE A 19
REMARK 465 GLU A 20
REMARK 465 ALA A 21
REMARK 465 GLN A 22
REMARK 465 LYS A 23
REMARK 465 ILE A 24
REMARK 465 GLU A 25
REMARK 465 TRP A 26
REMARK 465 HIS A 27
REMARK 465 GLU A 28
REMARK 465 GLY A 29
REMARK 465 SER A 30
REMARK 465 GLY A 31
REMARK 465 SER A 32
REMARK 465 GLY A 33
REMARK 465 SER A 34
REMARK 465 GLU A 35
REMARK 465 ASN A 36
REMARK 465 LEU A 37
REMARK 465 TYR A 38
REMARK 465 PHE A 39
REMARK 465 GLN A 40
REMARK 465 GLY A 41
REMARK 465 ARG A 42
REMARK 465 SER A 43
REMARK 465 LYS A 44
REMARK 465 SER A 45
REMARK 465 SER A 46
REMARK 465 ASN A 47
REMARK 465 GLU A 48
REMARK 465 ALA A 49
REMARK 465 THR A 50
REMARK 465 ASN A 51
REMARK 465 ILE A 52
REMARK 465 THR A 53
REMARK 465 PRO A 54
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 324 NZ
REMARK 470 GLU A 480 CD OE1 OE2
REMARK 470 LYS A 482 NZ
REMARK 470 GLU A 486 CD OE1 OE2
REMARK 470 LYS A 491 NZ
REMARK 470 SER A 507 OG
REMARK 470 LYS A 539 CE NZ
REMARK 470 GLU A 542 CD OE1 OE2
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 LYS A 617 CD CE NZ
REMARK 470 LYS A 655 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O4 NAG F 1 O5 NAG F 2 2.19
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 370 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 465 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 673 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 673 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
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 PHE A 164 2.75 90.08
REMARK 500 ASN A 178 -125.32 58.56
REMARK 500 LYS A 207 -46.03 70.94
REMARK 500 VAL A 382 -107.95 -131.01
REMARK 500 ALA A 452 56.26 -151.01
REMARK 500 ASP A 453 -154.59 -80.23
REMARK 500 SER A 507 119.42 57.51
REMARK 500 PHE A 525 -62.22 -90.11
REMARK 500 ASP A 567 64.54 -152.22
REMARK 500 ASN A 698 97.76 -168.73
REMARK 500
REMARK 500 REMARK: NULL
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 J34 A 815
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 CA A 819 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 269 O
REMARK 620 2 THR A 269 OG1 73.4
REMARK 620 3 TYR A 272 O 74.1 92.5
REMARK 620 4 GLU A 433 OE2 149.2 97.2 136.4
REMARK 620 5 GLU A 433 OE1 151.6 88.1 85.7 52.4
REMARK 620 6 GLU A 436 OE2 103.5 171.3 78.7 89.5 91.6
REMARK 620 7 HOH A 902 O 74.2 88.7 146.5 76.4 127.8 98.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 816 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 377 NE2
REMARK 620 2 ASP A 387 OD1 108.0
REMARK 620 3 ASP A 453 OD2 103.9 114.7
REMARK 620 4 HOH A 901 O 108.0 108.1 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 817 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 387 OD2
REMARK 620 2 GLU A 425 OE2 100.8
REMARK 620 3 GLU A 425 OE1 156.2 56.0
REMARK 620 4 HIS A 553 NE2 92.0 99.6 87.7
REMARK 620 5 J34 A 815 O6 105.6 152.5 98.1 87.2
REMARK 620 6 HOH A 901 O 96.5 91.1 89.5 164.9 78.5
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D7H RELATED DB: PDB
REMARK 900 RELATED ID: 4NGM RELATED DB: PDB
REMARK 900 RELATED ID: 4NGN RELATED DB: PDB
REMARK 900 RELATED ID: 4NGP RELATED DB: PDB
REMARK 900 RELATED ID: 4NGQ RELATED DB: PDB
REMARK 900 RELATED ID: 4NGR RELATED DB: PDB
REMARK 900 RELATED ID: 4NGT RELATED DB: PDB
DBREF 4NGS A 44 750 UNP Q04609 FOLH1_HUMAN 44 750
SEQADV 4NGS ARG A 12 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS SER A 13 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLY A 14 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS LEU A 15 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS ASN A 16 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS ASP A 17 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS ILE A 18 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS PHE A 19 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLU A 20 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS ALA A 21 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLN A 22 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS LYS A 23 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS ILE A 24 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLU A 25 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS TRP A 26 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS HIS A 27 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLU A 28 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLY A 29 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS SER A 30 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLY A 31 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS SER A 32 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLY A 33 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS SER A 34 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLU A 35 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS ASN A 36 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS LEU A 37 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS TYR A 38 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS PHE A 39 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLN A 40 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS GLY A 41 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS ARG A 42 UNP Q04609 EXPRESSION TAG
SEQADV 4NGS SER A 43 UNP Q04609 EXPRESSION TAG
SEQRES 1 A 739 ARG SER GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE
SEQRES 2 A 739 GLU TRP HIS GLU GLY SER GLY SER GLY SER GLU ASN LEU
SEQRES 3 A 739 TYR PHE GLN GLY ARG SER LYS SER SER ASN GLU ALA THR
SEQRES 4 A 739 ASN ILE THR PRO LYS HIS ASN MET LYS ALA PHE LEU ASP
SEQRES 5 A 739 GLU LEU LYS ALA GLU ASN ILE LYS LYS PHE LEU TYR ASN
SEQRES 6 A 739 PHE THR GLN ILE PRO HIS LEU ALA GLY THR GLU GLN ASN
SEQRES 7 A 739 PHE GLN LEU ALA LYS GLN ILE GLN SER GLN TRP LYS GLU
SEQRES 8 A 739 PHE GLY LEU ASP SER VAL GLU LEU ALA HIS TYR ASP VAL
SEQRES 9 A 739 LEU LEU SER TYR PRO ASN LYS THR HIS PRO ASN TYR ILE
SEQRES 10 A 739 SER ILE ILE ASN GLU ASP GLY ASN GLU ILE PHE ASN THR
SEQRES 11 A 739 SER LEU PHE GLU PRO PRO PRO PRO GLY TYR GLU ASN VAL
SEQRES 12 A 739 SER ASP ILE VAL PRO PRO PHE SER ALA PHE SER PRO GLN
SEQRES 13 A 739 GLY MET PRO GLU GLY ASP LEU VAL TYR VAL ASN TYR ALA
SEQRES 14 A 739 ARG THR GLU ASP PHE PHE LYS LEU GLU ARG ASP MET LYS
SEQRES 15 A 739 ILE ASN CYS SER GLY LYS ILE VAL ILE ALA ARG TYR GLY
SEQRES 16 A 739 LYS VAL PHE ARG GLY ASN LYS VAL LYS ASN ALA GLN LEU
SEQRES 17 A 739 ALA GLY ALA LYS GLY VAL ILE LEU TYR SER ASP PRO ALA
SEQRES 18 A 739 ASP TYR PHE ALA PRO GLY VAL LYS SER TYR PRO ASP GLY
SEQRES 19 A 739 TRP ASN LEU PRO GLY GLY GLY VAL GLN ARG GLY ASN ILE
SEQRES 20 A 739 LEU ASN LEU ASN GLY ALA GLY ASP PRO LEU THR PRO GLY
SEQRES 21 A 739 TYR PRO ALA ASN GLU TYR ALA TYR ARG ARG GLY ILE ALA
SEQRES 22 A 739 GLU ALA VAL GLY LEU PRO SER ILE PRO VAL HIS PRO ILE
SEQRES 23 A 739 GLY TYR TYR ASP ALA GLN LYS LEU LEU GLU LYS MET GLY
SEQRES 24 A 739 GLY SER ALA PRO PRO ASP SER SER TRP ARG GLY SER LEU
SEQRES 25 A 739 LYS VAL PRO TYR ASN VAL GLY PRO GLY PHE THR GLY ASN
SEQRES 26 A 739 PHE SER THR GLN LYS VAL LYS MET HIS ILE HIS SER THR
SEQRES 27 A 739 ASN GLU VAL THR ARG ILE TYR ASN VAL ILE GLY THR LEU
SEQRES 28 A 739 ARG GLY ALA VAL GLU PRO ASP ARG TYR VAL ILE LEU GLY
SEQRES 29 A 739 GLY HIS ARG ASP SER TRP VAL PHE GLY GLY ILE ASP PRO
SEQRES 30 A 739 GLN SER GLY ALA ALA VAL VAL HIS GLU ILE VAL ARG SER
SEQRES 31 A 739 PHE GLY THR LEU LYS LYS GLU GLY TRP ARG PRO ARG ARG
SEQRES 32 A 739 THR ILE LEU PHE ALA SER TRP ASP ALA GLU GLU PHE GLY
SEQRES 33 A 739 LEU LEU GLY SER THR GLU TRP ALA GLU GLU ASN SER ARG
SEQRES 34 A 739 LEU LEU GLN GLU ARG GLY VAL ALA TYR ILE ASN ALA ASP
SEQRES 35 A 739 SER SER ILE GLU GLY ASN TYR THR LEU ARG VAL ASP CYS
SEQRES 36 A 739 THR PRO LEU MET TYR SER LEU VAL HIS ASN LEU THR LYS
SEQRES 37 A 739 GLU LEU LYS SER PRO ASP GLU GLY PHE GLU GLY LYS SER
SEQRES 38 A 739 LEU TYR GLU SER TRP THR LYS LYS SER PRO SER PRO GLU
SEQRES 39 A 739 PHE SER GLY MET PRO ARG ILE SER LYS LEU GLY SER GLY
SEQRES 40 A 739 ASN ASP PHE GLU VAL PHE PHE GLN ARG LEU GLY ILE ALA
SEQRES 41 A 739 SER GLY ARG ALA ARG TYR THR LYS ASN TRP GLU THR ASN
SEQRES 42 A 739 LYS PHE SER GLY TYR PRO LEU TYR HIS SER VAL TYR GLU
SEQRES 43 A 739 THR TYR GLU LEU VAL GLU LYS PHE TYR ASP PRO MET PHE
SEQRES 44 A 739 LYS TYR HIS LEU THR VAL ALA GLN VAL ARG GLY GLY MET
SEQRES 45 A 739 VAL PHE GLU LEU ALA ASN SER ILE VAL LEU PRO PHE ASP
SEQRES 46 A 739 CYS ARG ASP TYR ALA VAL VAL LEU ARG LYS TYR ALA ASP
SEQRES 47 A 739 LYS ILE TYR SER ILE SER MET LYS HIS PRO GLN GLU MET
SEQRES 48 A 739 LYS THR TYR SER VAL SER PHE ASP SER LEU PHE SER ALA
SEQRES 49 A 739 VAL LYS ASN PHE THR GLU ILE ALA SER LYS PHE SER GLU
SEQRES 50 A 739 ARG LEU GLN ASP PHE ASP LYS SER ASN PRO ILE VAL LEU
SEQRES 51 A 739 ARG MET MET ASN ASP GLN LEU MET PHE LEU GLU ARG ALA
SEQRES 52 A 739 PHE ILE ASP PRO LEU GLY LEU PRO ASP ARG PRO PHE TYR
SEQRES 53 A 739 ARG HIS VAL ILE TYR ALA PRO SER SER HIS ASN LYS TYR
SEQRES 54 A 739 ALA GLY GLU SER PHE PRO GLY ILE TYR ASP ALA LEU PHE
SEQRES 55 A 739 ASP ILE GLU SER LYS VAL ASP PRO SER LYS ALA TRP GLY
SEQRES 56 A 739 GLU VAL LYS ARG GLN ILE TYR VAL ALA ALA PHE THR VAL
SEQRES 57 A 739 GLN ALA ALA ALA GLU THR LEU SER GLU VAL ALA
MODRES 4NGS ASN A 476 ASN GLYCOSYLATION SITE
MODRES 4NGS ASN A 76 ASN GLYCOSYLATION SITE
MODRES 4NGS ASN A 638 ASN GLYCOSYLATION SITE
MODRES 4NGS ASN A 121 ASN GLYCOSYLATION SITE
MODRES 4NGS ASN A 140 ASN GLYCOSYLATION SITE
MODRES 4NGS ASN A 459 ASN GLYCOSYLATION SITE
MODRES 4NGS ASN A 195 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 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 BMA F 3 11
HET MAN F 4 11
HET NAG A 803 14
HET NAG A 806 14
HET J34 A 815 38
HET ZN A 816 1
HET ZN A 817 1
HET CL A 818 1
HET CA A 819 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM J34 N-{[(1S)-1-CARBOXY-5-({[2-({4,44-DIOXO-48-[(3AS,4S,
HETNAM 2 J34 6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]-7,
HETNAM 3 J34 10,13,16,19,22,25,28,31,34,37,40-DODECAOXA-3,43-
HETNAM 4 J34 DIAZAOCTATETRACONT-1-YL}OXY)PHENYL]CARBAMOYL}AMINO)
HETNAM 5 J34 PENTYL]CARBAMOYL}-L-GLUTAMIC ACID
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
FORMUL 2 NAG 12(C8 H15 N O6)
FORMUL 6 BMA C6 H12 O6
FORMUL 6 MAN C6 H12 O6
FORMUL 9 J34 C58 H98 N8 O24 S
FORMUL 10 ZN 2(ZN 2+)
FORMUL 12 CL CL 1-
FORMUL 13 CA CA 2+
FORMUL 14 HOH *551(H2 O)
HELIX 1 1 ASN A 57 LEU A 65 1 9
HELIX 2 2 LYS A 66 THR A 78 1 13
HELIX 3 3 THR A 86 GLY A 104 1 19
HELIX 4 4 ARG A 181 ASP A 191 1 11
HELIX 5 5 PHE A 209 ALA A 220 1 12
HELIX 6 6 ASP A 230 PHE A 235 1 6
HELIX 7 7 GLY A 282 ALA A 286 5 5
HELIX 8 8 GLY A 298 GLU A 307 1 10
HELIX 9 9 ASP A 316 ARG A 320 5 5
HELIX 10 10 THR A 334 SER A 338 5 5
HELIX 11 11 PRO A 388 GLU A 408 1 21
HELIX 12 12 ALA A 423 GLY A 427 5 5
HELIX 13 13 LEU A 428 ASN A 438 1 11
HELIX 14 14 ASN A 438 ARG A 445 1 8
HELIX 15 15 MET A 470 LYS A 479 1 10
HELIX 16 16 SER A 492 SER A 501 1 10
HELIX 17 17 PHE A 521 GLN A 526 1 6
HELIX 18 18 THR A 558 TYR A 566 1 9
HELIX 19 19 PHE A 570 SER A 590 1 21
HELIX 20 20 ASP A 596 MET A 616 1 21
HELIX 21 21 HIS A 618 SER A 626 1 9
HELIX 22 22 PHE A 629 PHE A 653 1 25
HELIX 23 23 ASN A 657 ALA A 674 1 18
HELIX 24 24 PHE A 705 PHE A 713 1 9
HELIX 25 25 ASP A 714 LYS A 718 5 5
HELIX 26 26 ASP A 720 THR A 745 1 26
SHEET 1 A 7 SER A 107 TYR A 119 0
SHEET 2 A 7 THR A 349 LEU A 362 -1 O ASN A 357 N ALA A 111
SHEET 3 A 7 ARG A 414 TRP A 421 -1 O PHE A 418 N GLY A 360
SHEET 4 A 7 GLU A 367 HIS A 377 1 N LEU A 374 O LEU A 417
SHEET 5 A 7 GLY A 446 ASN A 451 1 O ILE A 450 N ILE A 373
SHEET 6 A 7 ALA A 531 THR A 538 1 O GLY A 533 N ASN A 451
SHEET 7 A 7 THR A 461 CYS A 466 -1 N THR A 461 O THR A 538
SHEET 1 B 4 GLU A 137 ASN A 140 0
SHEET 2 B 4 TYR A 127 ILE A 131 -1 N ILE A 130 O PHE A 139
SHEET 3 B 4 LYS A 341 HIS A 345 -1 O LYS A 341 N ILE A 131
SHEET 4 B 4 GLU A 171 GLY A 172 -1 N GLY A 172 O VAL A 342
SHEET 1 C 2 SER A 162 ALA A 163 0
SHEET 2 C 2 GLY A 256 ASN A 257 1 N GLY A 256 O ALA A 163
SHEET 1 D 4 LEU A 174 TYR A 176 0
SHEET 2 D 4 ILE A 200 ARG A 204 1 O ILE A 202 N VAL A 175
SHEET 3 D 4 GLY A 224 TYR A 228 1 O ILE A 226 N VAL A 201
SHEET 4 D 4 VAL A 294 ILE A 297 1 O HIS A 295 N LEU A 227
SHEET 1 E 2 TYR A 692 SER A 695 0
SHEET 2 E 2 ASN A 698 SER A 704 -1 O GLU A 703 N ALA A 693
LINK ND2 ASN A 76 C1 NAG B 1 1555 1555 1.43
LINK ND2 ASN A 121 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN A 140 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 195 C1 NAG A 806 1555 1555 1.46
LINK ND2 ASN A 459 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN A 476 C1 NAG E 1 1555 1555 1.43
LINK ND2 ASN A 638 C1 NAG F 1 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.43
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.43
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.44
LINK O THR A 269 CA CA A 819 1555 1555 2.41
LINK OG1 THR A 269 CA CA A 819 1555 1555 2.49
LINK O TYR A 272 CA CA A 819 1555 1555 2.30
LINK NE2 HIS A 377 ZN ZN A 816 1555 1555 2.04
LINK OD1 ASP A 387 ZN ZN A 816 1555 1555 2.00
LINK OD2 ASP A 387 ZN ZN A 817 1555 1555 2.04
LINK OE2 GLU A 425 ZN ZN A 817 1555 1555 2.14
LINK OE1 GLU A 425 ZN ZN A 817 1555 1555 2.46
LINK OE2 GLU A 433 CA CA A 819 1555 1555 2.52
LINK OE1 GLU A 433 CA CA A 819 1555 1555 2.53
LINK OE2 GLU A 436 CA CA A 819 1555 1555 2.30
LINK OD2 ASP A 453 ZN ZN A 816 1555 1555 1.98
LINK NE2 HIS A 553 ZN ZN A 817 1555 1555 2.04
LINK O6 J34 A 815 ZN ZN A 817 1555 1555 2.67
LINK ZN ZN A 816 O HOH A 901 1555 1555 1.83
LINK ZN ZN A 817 O HOH A 901 1555 1555 2.02
LINK CA CA A 819 O HOH A 902 1555 1555 2.48
CISPEP 1 TYR A 242 PRO A 243 0 9.06
CISPEP 2 GLY A 330 PRO A 331 0 2.54
CISPEP 3 ASP A 387 PRO A 388 0 7.78
CRYST1 101.445 130.046 159.123 90.00 90.00 90.00 I 2 2 2 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 0.009858 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007690 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006284 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
