HEADER HYDROLASE 14-MAY-10 2XEF
TITLE HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ANTIBODY-
TITLE 2 RECRUITING MOLECULE ARM-P8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE CARBOXYPEPTIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ECTODOMAIN, RESIDUES 44-750;
COMPND 5 SYNONYM: GLUTAMATE CARBOXYPEPTIDASE II, MEMBRANE GLUTAMATE
COMPND 6 CARBOXYPEPTIDASE, GCPII, N-ACETYLATED -ALPHA-LINKED ACIDIC
COMPND 7 DIPEPTIDASE I, NAALADASE I, PTEROYLPOLY-GAMMA-GLUTAMATE
COMPND 8 CARBOXYPEPTIDASE, FOLYLPOLY-GAMMA-GLUTAMATE CARBOXYPEPTIDASE, MGCP,
COMPND 9 FGCP, FOLATE HYDROLASE 1, PROSTATE-SPECIFIC MEMBRANE ANTIGEN, PSMA,
COMPND 10 PSM, CELL GROWTH-INHIBITING GENE 27 PROTEIN;
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 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: S2
KEYWDS METALLOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.X.ZHANG,R.P.MURELLI,C.BARINKA,J.MICHEL,A.COCLEAZA,W.L.JORGENSEN,
AUTHOR 2 J.LUBKOWSKI,D.A.SPIEGEL
REVDAT 5 20-DEC-23 2XEF 1 REMARK HETSYN
REVDAT 4 29-JUL-20 2XEF 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 2XEF 1 REMARK
REVDAT 2 10-NOV-10 2XEF 1 JRNL
REVDAT 1 08-SEP-10 2XEF 0
JRNL AUTH A.X.ZHANG,R.P.MURELLI,C.BARINKA,J.MICHEL,A.COCLEAZA,
JRNL AUTH 2 W.L.JORGENSEN,J.LUBKOWSKI,D.A.SPIEGEL
JRNL TITL A REMOTE ARENE-BINDING SITE ON PROSTATE SPECIFIC MEMBRANE
JRNL TITL 2 ANTIGEN REVEALED BY ANTIBODY-RECRUITING SMALL MOLECULES.
JRNL REF J.AM.CHEM.SOC. V. 132 12711 2010
JRNL REFN ISSN 0002-7863
JRNL PMID 20726553
JRNL DOI 10.1021/JA104591M
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0057
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) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 135631
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2037
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) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7726
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5524
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 244
REMARK 3 SOLVENT ATOMS : 581
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.62000
REMARK 3 B22 (A**2) : -1.84000
REMARK 3 B33 (A**2) : 1.21000
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): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.277
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6302 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8575 ; 1.692 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 751 ; 5.600 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 286 ;35.534 ;23.986
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1017 ;13.410 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;13.027 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 913 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4852 ; 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): 3620 ; 0.985 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5900 ; 1.638 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2682 ; 2.598 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2658 ; 4.198 ; 4.500
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 : 1
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 55 A 750
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8260 49.3280 44.7170
REMARK 3 T TENSOR
REMARK 3 T11: -0.0729 T22: -0.0415
REMARK 3 T33: -0.0545 T12: 0.0174
REMARK 3 T13: 0.0044 T23: -0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.5316 L22: 0.8993
REMARK 3 L33: 0.3127 L12: -0.2763
REMARK 3 L13: 0.0277 L23: 0.0639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0673 S12: 0.0111 S13: -0.0387
REMARK 3 S21: 0.0239 S22: 0.0770 S23: -0.1606
REMARK 3 S31: 0.0275 S32: 0.0645 S33: -0.0097
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS.
REMARK 4
REMARK 4 2XEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1290043914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-09
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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 137748
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 2OOT
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 33% (V/V) PENTAERYTHRITOL PROPOXYLATE
REMARK 280 PO/OH 5/4, 1% (W/V) PEG 3350, 100 MM TRIS-HCL, PH 8.0
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 50.92200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.01300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 79.37050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.92200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.01300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.37050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.92200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.01300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 79.37050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 50.92200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.01300
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 79.37050
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: 12090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 130.02600
REMARK 350 BIOMT3 2 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 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 465 ASP A 654
REMARK 465 LYS A 655
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 280 CG CD NE CZ NH1 NH2
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 OE1 GLN A 620 O HOH A 2426 2.07
REMARK 500 OG SER A 613 O HOH A 2420 2.15
REMARK 500 OH TYR A 242 O HOH A 2165 2.18
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 O HOH A 2469 O HOH A 2469 2565 1.04
REMARK 500 OE1 GLU A 276 O2 BMA E 3 2565 1.96
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 440 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 673 NE - CZ - NH2 ANGL. DEV. = -5.2 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 HIS A 124 76.61 -151.14
REMARK 500 PHE A 164 2.96 87.07
REMARK 500 ASN A 178 -127.42 56.92
REMARK 500 LYS A 207 -46.91 72.93
REMARK 500 ASP A 369 30.52 -93.09
REMARK 500 VAL A 382 -109.88 -129.69
REMARK 500 ALA A 452 58.41 -148.53
REMARK 500 ASP A 453 -155.19 -83.61
REMARK 500 SER A 454 127.75 -37.19
REMARK 500 ASP A 567 66.68 -154.43
REMARK 500 ASN A 698 97.15 -170.17
REMARK 500 PHE A 705 55.38 39.39
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 A2074 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A2075 DISTANCE = 7.15 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 AR8 A 1770
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 A1753 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 269 OG1
REMARK 620 2 THR A 269 O 72.3
REMARK 620 3 TYR A 272 O 92.3 74.7
REMARK 620 4 GLU A 433 OE1 87.6 150.4 85.0
REMARK 620 5 GLU A 433 OE2 98.9 149.3 135.8 53.3
REMARK 620 6 GLU A 436 OE2 172.3 105.5 80.0 91.5 86.7
REMARK 620 7 HOH A2189 O 88.8 73.4 146.1 128.9 77.2 97.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1752 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 377 NE2
REMARK 620 2 ASP A 387 OD1 105.2
REMARK 620 3 ASP A 453 OD2 102.2 120.4
REMARK 620 4 HOH A2562 O 108.2 106.3 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1751 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 387 OD2
REMARK 620 2 GLU A 425 OE1 155.6
REMARK 620 3 GLU A 425 OE2 100.0 56.5
REMARK 620 4 HIS A 553 NE2 90.2 88.4 100.4
REMARK 620 5 AR8 A1770 OAD 104.8 99.5 153.7 88.3
REMARK 620 6 HOH A2562 O 96.0 91.5 92.2 164.8 76.7
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C6G RELATED DB: PDB
REMARK 900 MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) WITH BOUND
REMARK 900 GLUTAMATE
REMARK 900 RELATED ID: 2C6P RELATED DB: PDB
REMARK 900 MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX
REMARK 900 WITH PHOSPHATE ANION
REMARK 900 RELATED ID: 2C6C RELATED DB: PDB
REMARK 900 MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX
REMARK 900 WITH GPI-18431 (S)-2-( 4-IODOBENZYLPHOSPHONOMETHYL)-PENTANEDIOIC
REMARK 900 ACID
REMARK 900 RELATED ID: 1Z8L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROSTATE-SPECIFIC MEMBRANE ANTIGEN, ATUMOR
REMARK 900 MARKER AND PEPTIDASE
REMARK 900 RELATED ID: 2JBJ RELATED DB: PDB
REMARK 900 MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX
REMARK 900 WITH 2-PMPA (2- PHOSPHONOMETHYL-PENTANEDIOIC ACID)
REMARK 900 RELATED ID: 2JBK RELATED DB: PDB
REMARK 900 MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX
REMARK 900 WITH QUISQUALIC ACID (QUISQUALATE, ALPHA-AMINO-3,5-DIOXO-1,2,4 -
REMARK 900 OXADIAZOLIDINE-2-PROPANOIC ACID)
REMARK 900 RELATED ID: 2CIJ RELATED DB: PDB
REMARK 900 MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) WITH BOUND
REMARK 900 METHIONINE
REMARK 900 RELATED ID: 2XEG RELATED DB: PDB
REMARK 900 HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ANTIBODY-
REMARK 900 RECRUITING MOLECULE ARM-P4
REMARK 900 RELATED ID: 2XEI RELATED DB: PDB
REMARK 900 HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ANTIBODY-
REMARK 900 RECRUITING MOLECULE ARM-P2
REMARK 900 RELATED ID: 2XEJ RELATED DB: PDB
REMARK 900 HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ARM-M4, UREA-
REMARK 900 BASED INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RS - CLONING ARTIFACT AT THE N-TERMINUS
DBREF 2XEF A 44 750 UNP Q04609 FOLH1_HUMAN 44 750
SEQADV 2XEF ARG A 42 UNP Q04609 EXPRESSION TAG
SEQADV 2XEF SER A 43 UNP Q04609 EXPRESSION TAG
SEQADV 2XEF GLN A 593 UNP Q04609 LEU 593 CONFLICT
SEQRES 1 A 709 ARG SER LYS SER SER ASN GLU ALA THR ASN ILE THR PRO
SEQRES 2 A 709 LYS HIS ASN MET LYS ALA PHE LEU ASP GLU LEU LYS ALA
SEQRES 3 A 709 GLU ASN ILE LYS LYS PHE LEU TYR ASN PHE THR GLN ILE
SEQRES 4 A 709 PRO HIS LEU ALA GLY THR GLU GLN ASN PHE GLN LEU ALA
SEQRES 5 A 709 LYS GLN ILE GLN SER GLN TRP LYS GLU PHE GLY LEU ASP
SEQRES 6 A 709 SER VAL GLU LEU ALA HIS TYR ASP VAL LEU LEU SER TYR
SEQRES 7 A 709 PRO ASN LYS THR HIS PRO ASN TYR ILE SER ILE ILE ASN
SEQRES 8 A 709 GLU ASP GLY ASN GLU ILE PHE ASN THR SER LEU PHE GLU
SEQRES 9 A 709 PRO PRO PRO PRO GLY TYR GLU ASN VAL SER ASP ILE VAL
SEQRES 10 A 709 PRO PRO PHE SER ALA PHE SER PRO GLN GLY MET PRO GLU
SEQRES 11 A 709 GLY ASP LEU VAL TYR VAL ASN TYR ALA ARG THR GLU ASP
SEQRES 12 A 709 PHE PHE LYS LEU GLU ARG ASP MET LYS ILE ASN CYS SER
SEQRES 13 A 709 GLY LYS ILE VAL ILE ALA ARG TYR GLY LYS VAL PHE ARG
SEQRES 14 A 709 GLY ASN LYS VAL LYS ASN ALA GLN LEU ALA GLY ALA LYS
SEQRES 15 A 709 GLY VAL ILE LEU TYR SER ASP PRO ALA ASP TYR PHE ALA
SEQRES 16 A 709 PRO GLY VAL LYS SER TYR PRO ASP GLY TRP ASN LEU PRO
SEQRES 17 A 709 GLY GLY GLY VAL GLN ARG GLY ASN ILE LEU ASN LEU ASN
SEQRES 18 A 709 GLY ALA GLY ASP PRO LEU THR PRO GLY TYR PRO ALA ASN
SEQRES 19 A 709 GLU TYR ALA TYR ARG ARG GLY ILE ALA GLU ALA VAL GLY
SEQRES 20 A 709 LEU PRO SER ILE PRO VAL HIS PRO ILE GLY TYR TYR ASP
SEQRES 21 A 709 ALA GLN LYS LEU LEU GLU LYS MET GLY GLY SER ALA PRO
SEQRES 22 A 709 PRO ASP SER SER TRP ARG GLY SER LEU LYS VAL PRO TYR
SEQRES 23 A 709 ASN VAL GLY PRO GLY PHE THR GLY ASN PHE SER THR GLN
SEQRES 24 A 709 LYS VAL LYS MET HIS ILE HIS SER THR ASN GLU VAL THR
SEQRES 25 A 709 ARG ILE TYR ASN VAL ILE GLY THR LEU ARG GLY ALA VAL
SEQRES 26 A 709 GLU PRO ASP ARG TYR VAL ILE LEU GLY GLY HIS ARG ASP
SEQRES 27 A 709 SER TRP VAL PHE GLY GLY ILE ASP PRO GLN SER GLY ALA
SEQRES 28 A 709 ALA VAL VAL HIS GLU ILE VAL ARG SER PHE GLY THR LEU
SEQRES 29 A 709 LYS LYS GLU GLY TRP ARG PRO ARG ARG THR ILE LEU PHE
SEQRES 30 A 709 ALA SER TRP ASP ALA GLU GLU PHE GLY LEU LEU GLY SER
SEQRES 31 A 709 THR GLU TRP ALA GLU GLU ASN SER ARG LEU LEU GLN GLU
SEQRES 32 A 709 ARG GLY VAL ALA TYR ILE ASN ALA ASP SER SER ILE GLU
SEQRES 33 A 709 GLY ASN TYR THR LEU ARG VAL ASP CYS THR PRO LEU MET
SEQRES 34 A 709 TYR SER LEU VAL HIS ASN LEU THR LYS GLU LEU LYS SER
SEQRES 35 A 709 PRO ASP GLU GLY PHE GLU GLY LYS SER LEU TYR GLU SER
SEQRES 36 A 709 TRP THR LYS LYS SER PRO SER PRO GLU PHE SER GLY MET
SEQRES 37 A 709 PRO ARG ILE SER LYS LEU GLY SER GLY ASN ASP PHE GLU
SEQRES 38 A 709 VAL PHE PHE GLN ARG LEU GLY ILE ALA SER GLY ARG ALA
SEQRES 39 A 709 ARG TYR THR LYS ASN TRP GLU THR ASN LYS PHE SER GLY
SEQRES 40 A 709 TYR PRO LEU TYR HIS SER VAL TYR GLU THR TYR GLU LEU
SEQRES 41 A 709 VAL GLU LYS PHE TYR ASP PRO MET PHE LYS TYR HIS LEU
SEQRES 42 A 709 THR VAL ALA GLN VAL ARG GLY GLY MET VAL PHE GLU LEU
SEQRES 43 A 709 ALA ASN SER ILE VAL GLN PRO PHE ASP CYS ARG ASP TYR
SEQRES 44 A 709 ALA VAL VAL LEU ARG LYS TYR ALA ASP LYS ILE TYR SER
SEQRES 45 A 709 ILE SER MET LYS HIS PRO GLN GLU MET LYS THR TYR SER
SEQRES 46 A 709 VAL SER PHE ASP SER LEU PHE SER ALA VAL LYS ASN PHE
SEQRES 47 A 709 THR GLU ILE ALA SER LYS PHE SER GLU ARG LEU GLN ASP
SEQRES 48 A 709 PHE ASP LYS SER ASN PRO ILE VAL LEU ARG MET MET ASN
SEQRES 49 A 709 ASP GLN LEU MET PHE LEU GLU ARG ALA PHE ILE ASP PRO
SEQRES 50 A 709 LEU GLY LEU PRO ASP ARG PRO PHE TYR ARG HIS VAL ILE
SEQRES 51 A 709 TYR ALA PRO SER SER HIS ASN LYS TYR ALA GLY GLU SER
SEQRES 52 A 709 PHE PRO GLY ILE TYR ASP ALA LEU PHE ASP ILE GLU SER
SEQRES 53 A 709 LYS VAL ASP PRO SER LYS ALA TRP GLY GLU VAL LYS ARG
SEQRES 54 A 709 GLN ILE TYR VAL ALA ALA PHE THR VAL GLN ALA ALA ALA
SEQRES 55 A 709 GLU THR LEU SER GLU VAL ALA
MODRES 2XEF ASN A 76 ASN GLYCOSYLATION SITE
MODRES 2XEF ASN A 121 ASN GLYCOSYLATION SITE
MODRES 2XEF ASN A 140 ASN GLYCOSYLATION SITE
MODRES 2XEF ASN A 195 ASN GLYCOSYLATION SITE
MODRES 2XEF ASN A 459 ASN GLYCOSYLATION SITE
MODRES 2XEF ASN A 476 ASN GLYCOSYLATION SITE
MODRES 2XEF ASN A 638 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 BMA E 3 11
HET MAN E 4 11
HET AR8 A1770 128
HET ZN A1751 1
HET ZN A1752 1
HET CA A1753 1
HET CL A1754 1
HET NAG A1757 14
HET NAG A1759 14
HET NAG A1760 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM AR8 N-{[(1S)-5-{4-[25-({2,4-BIS[HYDROXY(OXO)
HETNAM 2 AR8 AMMONIO]PHENYL}AMINO)-2,5,8,11,14,17,20,23-
HETNAM 3 AR8 OCTAOXAPENTACOS-1-YL]-1H-1,2,3-TRIAZOL-1-YL}-1-
HETNAM 4 AR8 CARBOXYPENTYL]CARBAMOYL}-L-GLUTAMIC ACID
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE 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
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 NAG 11(C8 H15 N O6)
FORMUL 5 BMA C6 H12 O6
FORMUL 5 MAN C6 H12 O6
FORMUL 6 AR8 C37 H60 N8 O19 2+
FORMUL 7 ZN 2(ZN 2+)
FORMUL 9 CA CA 2+
FORMUL 10 CL CL 1-
FORMUL 14 HOH *581(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 ARG A 445 1 18
HELIX 14 14 MET A 470 LEU A 481 1 12
HELIX 15 15 SER A 492 SER A 501 1 10
HELIX 16 16 ASP A 520 ARG A 527 1 8
HELIX 17 17 THR A 558 TYR A 566 1 9
HELIX 18 18 PHE A 570 SER A 590 1 21
HELIX 19 19 ASP A 596 MET A 616 1 21
HELIX 20 20 HIS A 618 TYR A 625 1 8
HELIX 21 21 PHE A 629 PHE A 653 1 25
HELIX 22 22 ASN A 657 PHE A 675 1 19
HELIX 23 23 PHE A 705 PHE A 713 1 9
HELIX 24 24 ASP A 714 LYS A 718 5 5
HELIX 25 25 ASP A 720 THR A 745 1 26
SHEET 1 AA 7 SER A 107 TYR A 119 0
SHEET 2 AA 7 THR A 349 LEU A 362 -1 O THR A 349 N TYR A 119
SHEET 3 AA 7 ARG A 414 TRP A 421 -1 O ILE A 416 N LEU A 362
SHEET 4 AA 7 GLU A 367 HIS A 377 1 O ARG A 370 N THR A 415
SHEET 5 AA 7 GLY A 446 ASN A 451 1 N VAL A 447 O TYR A 371
SHEET 6 AA 7 ALA A 531 THR A 538 1 O ALA A 531 N TYR A 449
SHEET 7 AA 7 THR A 461 CYS A 466 -1 O THR A 461 N THR A 538
SHEET 1 AB 4 GLU A 137 ASN A 140 0
SHEET 2 AB 4 TYR A 127 ILE A 131 -1 O ILE A 130 N ILE A 138
SHEET 3 AB 4 LYS A 341 HIS A 345 -1 O LYS A 341 N ILE A 131
SHEET 4 AB 4 GLU A 171 GLY A 172 -1 O GLY A 172 N VAL A 342
SHEET 1 AC 2 SER A 162 ALA A 163 0
SHEET 2 AC 2 GLY A 256 ASN A 257 1 O GLY A 256 N ALA A 163
SHEET 1 AD 4 LEU A 174 TYR A 176 0
SHEET 2 AD 4 ILE A 200 ARG A 204 1 O ILE A 200 N VAL A 175
SHEET 3 AD 4 GLY A 224 TYR A 228 1 O GLY A 224 N VAL A 201
SHEET 4 AD 4 VAL A 294 ILE A 297 1 O HIS A 295 N LEU A 227
SHEET 1 AE 2 TYR A 692 SER A 695 0
SHEET 2 AE 2 ASN A 698 SER A 704 -1 N ASN A 698 O SER A 695
LINK ND2 ASN A 76 C1 NAG B 1 1555 1555 1.44
LINK ND2 ASN A 121 C1 NAG A1757 1555 1555 1.45
LINK ND2 ASN A 140 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN A 195 C1 NAG A1759 1555 1555 1.44
LINK ND2 ASN A 459 C1 NAG A1760 1555 1555 1.45
LINK ND2 ASN A 476 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 638 C1 NAG E 1 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.43
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.43
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45
LINK OG1 THR A 269 CA CA A1753 1555 1555 2.49
LINK O THR A 269 CA CA A1753 1555 1555 2.44
LINK O TYR A 272 CA CA A1753 1555 1555 2.30
LINK NE2 HIS A 377 ZN ZN A1752 1555 1555 2.01
LINK OD2 ASP A 387 ZN ZN A1751 1555 1555 2.08
LINK OD1 ASP A 387 ZN ZN A1752 1555 1555 2.00
LINK OE1 GLU A 425 ZN ZN A1751 1555 1555 2.42
LINK OE2 GLU A 425 ZN ZN A1751 1555 1555 2.13
LINK OE1 GLU A 433 CA CA A1753 1555 1555 2.52
LINK OE2 GLU A 433 CA CA A1753 1555 1555 2.50
LINK OE2 GLU A 436 CA CA A1753 1555 1555 2.29
LINK OD2 ASP A 453 ZN ZN A1752 1555 1555 1.96
LINK NE2 HIS A 553 ZN ZN A1751 1555 1555 2.08
LINK ZN ZN A1751 OADAAR8 A1770 1555 1555 2.61
LINK ZN ZN A1751 O HOH A2562 1555 1555 2.03
LINK ZN ZN A1752 O HOH A2562 1555 1555 1.89
LINK CA CA A1753 O HOH A2189 1555 1555 2.43
CISPEP 1 TYR A 242 PRO A 243 0 9.73
CISPEP 2 GLY A 330 PRO A 331 0 2.98
CISPEP 3 ASP A 387 PRO A 388 0 8.77
CRYST1 101.844 130.026 158.741 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 0.009819 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007691 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006300 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
