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HEADER LYASE 21-MAR-05 1Z68
TITLE CRYSTAL STRUCTURE OF HUMAN FIBROBLAST ACTIVATION PROTEIN
TITLE 2 ALPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST ACTIVATION PROTEIN, ALPHA SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SF9 CELLS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTB
KEYWDS SEPRASE, FIBROBLAST ACTIVATION PROTEIN ALPHA,FAPALPHA,
KEYWDS 2 DIPEPTIDYLPEPTIDASE,S9B, INTEGRAL MEMBRANE SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.AERTGEERTS,I.LEVIN,L.SHI,G.S.PRASAD,Y.ZHANG,M.L.KRAUS,
AUTHOR 2 S.SALAKIAN,G.SNELL,V.SRIDHAR,R.WIJNANDS,M.G.TENNANT
REVDAT 1 12-APR-05 1Z68 0
JRNL AUTH K.AERTGEERTS,I.LEVIN,L.SHI,G.S.PRASAD,Y.ZHANG,
JRNL AUTH 2 M.L.KRAUS,S.SALAKIAN,G.SNELL,V.SRIDHAR,R.WIJNANDS,
JRNL AUTH 3 M.G.TENNANT
JRNL TITL STRUCTURAL AND KINETIC ANALYSIS OF THE SUBSTRATE
JRNL TITL 2 SPECIFICITY OF HUMAN FIBROBLAST ACTIVATION PROTEIN
JRNL TITL 3 ALPHA
JRNL REF J.BIOL.CHEM. 2005
JRNL REFN ASTM JBCHA3 US ESSN 1083-351X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
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 : 66976
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3558
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4381
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3420
REMARK 3 BIN FREE R VALUE SET COUNT : 244
REMARK 3 BIN FREE R VALUE : 0.4130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 12600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.14000
REMARK 3 B22 (A**2) : 6.00000
REMARK 3 B33 (A**2) : -7.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.518
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.326
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.272
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.411
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12345 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16806 ; 1.382 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1436 ; 7.151 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1776 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9491 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6485 ; 0.216 ; 0.200
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): 658 ; 0.159 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.230 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.140 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7173 ; 1.143 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11635 ; 1.929 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5172 ; 1.171 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5170 ; 1.857 ; 3.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
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 : 8
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 39 A 53
REMARK 3 RESIDUE RANGE : A 54 A 229
REMARK 3 RESIDUE RANGE : A 230 A 259
REMARK 3 RESIDUE RANGE : A 260 A 492
REMARK 3 RESIDUE RANGE : A 493 A 757
REMARK 3 RESIDUE RANGE : A 4901 A 4901
REMARK 3 RESIDUE RANGE : A 9201 A 9202
REMARK 3 RESIDUE RANGE : A 2271 A 2272
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9729 0.7562 69.4363
REMARK 3 T TENSOR
REMARK 3 T11: 0.3639 T22: 0.2801
REMARK 3 T33: 0.2565 T12: 0.0191
REMARK 3 T13: -0.0828 T23: 0.1432
REMARK 3 L TENSOR
REMARK 3 L11: 0.9227 L22: 0.9407
REMARK 3 L33: 2.0685 L12: -0.0350
REMARK 3 L13: 0.1923 L23: -0.4036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.1637 S13: -0.0073
REMARK 3 S21: 0.3957 S22: -0.0620 S23: -0.1214
REMARK 3 S31: 0.0194 S32: 0.2575 S33: 0.0614
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 9
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 39 B 53
REMARK 3 RESIDUE RANGE : B 54 B 229
REMARK 3 RESIDUE RANGE : B 230 B 259
REMARK 3 RESIDUE RANGE : B 260 B 492
REMARK 3 RESIDUE RANGE : B 493 B 757
REMARK 3 RESIDUE RANGE : B 4901 B 4901
REMARK 3 RESIDUE RANGE : B 9201 B 9202
REMARK 3 RESIDUE RANGE : B 3141 B 3141
REMARK 3 RESIDUE RANGE : B 6791 B 6791
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9897 13.0862 15.7584
REMARK 3 T TENSOR
REMARK 3 T11: 0.0936 T22: 0.0564
REMARK 3 T33: 0.2111 T12: 0.0703
REMARK 3 T13: -0.0045 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 1.0577 L22: 0.9110
REMARK 3 L33: 1.3962 L12: 0.2906
REMARK 3 L13: 0.0415 L23: -0.4163
REMARK 3 S TENSOR
REMARK 3 S11: 0.0832 S12: 0.1185 S13: -0.1318
REMARK 3 S21: -0.1006 S22: -0.0180 S23: 0.0470
REMARK 3 S31: 0.3658 S32: 0.0091 S33: -0.0652
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z68 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-2005.
REMARK 100 THE RCSB ID CODE IS RCSB032349.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-2002
REMARK 200 TEMPERATURE (KELVIN) : 98.0
REMARK 200 PH : 7.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : SINGLE CRYSTAL, SINGLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70612
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50700
REMARK 200 FOR SHELL : 1.900
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: 1R9M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.6, VAPOR DIFFUSION, SITTING
REMARK 280 DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 35.14750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 107.42750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.29000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 107.42750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.14750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.29000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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
REMARK 500 O HOH 32 O HOH 251 2.12
REMARK 500 O HOH 429 O HOH 641 2.12
REMARK 500 O HOH 3 O HOH 317 2.16
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 149 CB PRO A 149 CG 0.079
REMARK 500 MET A 567 CG MET A 567 SD 0.057
REMARK 500 MET A 727 SD MET A 727 CE 0.060
REMARK 500 MET B 205 SD MET B 205 CE 0.067
REMARK 500 VAL B 356 CB VAL B 356 CG2 -0.058
REMARK 500 MET B 522 SD MET B 522 CE 0.101
REMARK 500 MET B 683 SD MET B 683 CE 0.061
REMARK 500 MET B 727 SD MET B 727 CE 0.117
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 480 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 LEU B 42 CA - CB - CG ANGL. DEV. = 12.5 DEGREES
REMARK 500 LEU B 78 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 PRO B 149 N - CD - CG ANGL. DEV. = -9.3 DEGREES
REMARK 500 LYS B 191 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 LEU B 221 CA - CB - CG ANGL. DEV. = 9.4 DEGREES
REMARK 500 GLY B 349 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 VAL B 356 CB - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLU B 417 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU B 503 CA - CB - CG ANGL. DEV. = 10.3 DEGREES
REMARK 500 LEU B 518 CA - CB - CG ANGL. DEV. = 8.8 DEGREES
REMARK 500 LEU B 571 CA - CB - CG ANGL. DEV. = 10.0 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 624 -111.95 54.68
REMARK 500 SER B 624 -109.04 56.33
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 148 PRO A 149 -146.58
REMARK 500 TYR A 432 PRO A 433 -144.18
REMARK 500 ARG B 148 PRO B 149 -124.23
REMARK 500 TYR B 432 PRO B 433 -106.21
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 83 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH 184 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH 193 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH 202 DISTANCE = 7.26 ANGSTROMS
REMARK 525 HOH 239 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH 248 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH 257 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH 308 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH 326 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH 351 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH 383 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH 389 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH 403 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH 404 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH 418 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH 461 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH 468 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH 486 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH 506 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH 514 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH 516 DISTANCE = 7.55 ANGSTROMS
REMARK 525 HOH 524 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH 536 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH 564 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH 566 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH 567 DISTANCE = 7.99 ANGSTROMS
REMARK 525 HOH 575 DISTANCE = 9.90 ANGSTROMS
REMARK 525 HOH 585 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH 588 DISTANCE = 8.40 ANGSTROMS
REMARK 525 HOH 599 DISTANCE = 5.44 ANGSTROMS
REMARK 525 HOH 600 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH 601 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH 602 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH 605 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH 606 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH 610 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH 612 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH 613 DISTANCE = 8.45 ANGSTROMS
REMARK 525 HOH 615 DISTANCE = 10.18 ANGSTROMS
REMARK 525 HOH 618 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH 620 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH 630 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH 647 DISTANCE = 8.63 ANGSTROMS
REMARK 525 HOH 648 DISTANCE = 11.51 ANGSTROMS
REMARK 525 HOH 659 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH 664 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH 668 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH 669 DISTANCE = 6.38 ANGSTROMS
DBREF 1Z68 A 39 757 GB 16933539 NM_004460 39 757
DBREF 1Z68 B 39 757 GB 16933539 NM_004460 39 757
SEQRES 1 A 719 MET ARG ALA LEU THR LEU LYS ASP ILE LEU ASN GLY THR
SEQRES 2 A 719 PHE SER TYR LYS THR PHE PHE PRO ASN TRP ILE SER GLY
SEQRES 3 A 719 GLN GLU TYR LEU HIS GLN SER ALA ASP ASN ASN ILE VAL
SEQRES 4 A 719 LEU TYR ASN ILE GLU THR GLY GLN SER TYR THR ILE LEU
SEQRES 5 A 719 SER ASN ARG THR MET LYS SER VAL ASN ALA SER ASN TYR
SEQRES 6 A 719 GLY LEU SER PRO ASP ARG GLN PHE VAL TYR LEU GLU SER
SEQRES 7 A 719 ASP TYR SER LYS LEU TRP ARG TYR SER TYR THR ALA THR
SEQRES 8 A 719 TYR TYR ILE TYR ASP LEU SER ASN GLY GLU PHE VAL ARG
SEQRES 9 A 719 GLY ASN GLU LEU PRO ARG PRO ILE GLN TYR LEU CYS TRP
SEQRES 10 A 719 SER PRO VAL GLY SER LYS LEU ALA TYR VAL TYR GLN ASN
SEQRES 11 A 719 ASN ILE TYR LEU LYS GLN ARG PRO GLY ASP PRO PRO PHE
SEQRES 12 A 719 GLN ILE THR PHE ASN GLY ARG GLU ASN LYS ILE PHE ASN
SEQRES 13 A 719 GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU MET LEU ALA
SEQRES 14 A 719 THR LYS TYR ALA LEU TRP TRP SER PRO ASN GLY LYS PHE
SEQRES 15 A 719 LEU ALA TYR ALA GLU PHE ASN ASP THR ASP ILE PRO VAL
SEQRES 16 A 719 ILE ALA TYR SER TYR TYR GLY ASP GLU GLN TYR PRO ARG
SEQRES 17 A 719 THR ILE ASN ILE PRO TYR PRO LYS ALA GLY ALA LYS ASN
SEQRES 18 A 719 PRO VAL VAL ARG ILE PHE ILE ILE ASP THR THR TYR PRO
SEQRES 19 A 719 ALA TYR VAL GLY PRO GLN GLU VAL PRO VAL PRO ALA MET
SEQRES 20 A 719 ILE ALA SER SER ASP TYR TYR PHE SER TRP LEU THR TRP
SEQRES 21 A 719 VAL THR ASP GLU ARG VAL CYS LEU GLN TRP LEU LYS ARG
SEQRES 22 A 719 VAL GLN ASN VAL SER VAL LEU SER ILE CYS ASP PHE ARG
SEQRES 23 A 719 GLU ASP TRP GLN THR TRP ASP CYS PRO LYS THR GLN GLU
SEQRES 24 A 719 HIS ILE GLU GLU SER ARG THR GLY TRP ALA GLY GLY PHE
SEQRES 25 A 719 PHE VAL SER THR PRO VAL PHE SER TYR ASP ALA ILE SER
SEQRES 26 A 719 TYR TYR LYS ILE PHE SER ASP LYS ASP GLY TYR LYS HIS
SEQRES 27 A 719 ILE HIS TYR ILE LYS ASP THR VAL GLU ASN ALA ILE GLN
SEQRES 28 A 719 ILE THR SER GLY LYS TRP GLU ALA ILE ASN ILE PHE ARG
SEQRES 29 A 719 VAL THR GLN ASP SER LEU PHE TYR SER SER ASN GLU PHE
SEQRES 30 A 719 GLU GLU TYR PRO GLY ARG ARG ASN ILE TYR ARG ILE SER
SEQRES 31 A 719 ILE GLY SER TYR PRO PRO SER LYS LYS CYS VAL THR CYS
SEQRES 32 A 719 HIS LEU ARG LYS GLU ARG CYS GLN TYR TYR THR ALA SER
SEQRES 33 A 719 PHE SER ASP TYR ALA LYS TYR TYR ALA LEU VAL CYS TYR
SEQRES 34 A 719 GLY PRO GLY ILE PRO ILE SER THR LEU HIS ASP GLY ARG
SEQRES 35 A 719 THR ASP GLN GLU ILE LYS ILE LEU GLU GLU ASN LYS GLU
SEQRES 36 A 719 LEU GLU ASN ALA LEU LYS ASN ILE GLN LEU PRO LYS GLU
SEQRES 37 A 719 GLU ILE LYS LYS LEU GLU VAL ASP GLU ILE THR LEU TRP
SEQRES 38 A 719 TYR LYS MET ILE LEU PRO PRO GLN PHE ASP ARG SER LYS
SEQRES 39 A 719 LYS TYR PRO LEU LEU ILE GLN VAL TYR GLY GLY PRO CYS
SEQRES 40 A 719 SER GLN SER VAL ARG SER VAL PHE ALA VAL ASN TRP ILE
SEQRES 41 A 719 SER TYR LEU ALA SER LYS GLU GLY MET VAL ILE ALA LEU
SEQRES 42 A 719 VAL ASP GLY ARG GLY THR ALA PHE GLN GLY ASP LYS LEU
SEQRES 43 A 719 LEU TYR ALA VAL TYR ARG LYS LEU GLY VAL TYR GLU VAL
SEQRES 44 A 719 GLU ASP GLN ILE THR ALA VAL ARG LYS PHE ILE GLU MET
SEQRES 45 A 719 GLY PHE ILE ASP GLU LYS ARG ILE ALA ILE TRP GLY TRP
SEQRES 46 A 719 SER TYR GLY GLY TYR VAL SER SER LEU ALA LEU ALA SER
SEQRES 47 A 719 GLY THR GLY LEU PHE LYS CYS GLY ILE ALA VAL ALA PRO
SEQRES 48 A 719 VAL SER SER TRP GLU TYR TYR ALA SER VAL TYR THR GLU
SEQRES 49 A 719 ARG PHE MET GLY LEU PRO THR LYS ASP ASP ASN LEU GLU
SEQRES 50 A 719 HIS TYR LYS ASN SER THR VAL MET ALA ARG ALA GLU TYR
SEQRES 51 A 719 PHE ARG ASN VAL ASP TYR LEU LEU ILE HIS GLY THR ALA
SEQRES 52 A 719 ASP ASP ASN VAL HIS PHE GLN ASN SER ALA GLN ILE ALA
SEQRES 53 A 719 LYS ALA LEU VAL ASN ALA GLN VAL ASP PHE GLN ALA MET
SEQRES 54 A 719 TRP TYR SER ASP GLN ASN HIS GLY LEU SER GLY LEU SER
SEQRES 55 A 719 THR ASN HIS LEU TYR THR HIS MET THR HIS PHE LEU LYS
SEQRES 56 A 719 GLN CYS PHE SER
SEQRES 1 B 719 MET ARG ALA LEU THR LEU LYS ASP ILE LEU ASN GLY THR
SEQRES 2 B 719 PHE SER TYR LYS THR PHE PHE PRO ASN TRP ILE SER GLY
SEQRES 3 B 719 GLN GLU TYR LEU HIS GLN SER ALA ASP ASN ASN ILE VAL
SEQRES 4 B 719 LEU TYR ASN ILE GLU THR GLY GLN SER TYR THR ILE LEU
SEQRES 5 B 719 SER ASN ARG THR MET LYS SER VAL ASN ALA SER ASN TYR
SEQRES 6 B 719 GLY LEU SER PRO ASP ARG GLN PHE VAL TYR LEU GLU SER
SEQRES 7 B 719 ASP TYR SER LYS LEU TRP ARG TYR SER TYR THR ALA THR
SEQRES 8 B 719 TYR TYR ILE TYR ASP LEU SER ASN GLY GLU PHE VAL ARG
SEQRES 9 B 719 GLY ASN GLU LEU PRO ARG PRO ILE GLN TYR LEU CYS TRP
SEQRES 10 B 719 SER PRO VAL GLY SER LYS LEU ALA TYR VAL TYR GLN ASN
SEQRES 11 B 719 ASN ILE TYR LEU LYS GLN ARG PRO GLY ASP PRO PRO PHE
SEQRES 12 B 719 GLN ILE THR PHE ASN GLY ARG GLU ASN LYS ILE PHE ASN
SEQRES 13 B 719 GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU MET LEU ALA
SEQRES 14 B 719 THR LYS TYR ALA LEU TRP TRP SER PRO ASN GLY LYS PHE
SEQRES 15 B 719 LEU ALA TYR ALA GLU PHE ASN ASP THR ASP ILE PRO VAL
SEQRES 16 B 719 ILE ALA TYR SER TYR TYR GLY ASP GLU GLN TYR PRO ARG
SEQRES 17 B 719 THR ILE ASN ILE PRO TYR PRO LYS ALA GLY ALA LYS ASN
SEQRES 18 B 719 PRO VAL VAL ARG ILE PHE ILE ILE ASP THR THR TYR PRO
SEQRES 19 B 719 ALA TYR VAL GLY PRO GLN GLU VAL PRO VAL PRO ALA MET
SEQRES 20 B 719 ILE ALA SER SER ASP TYR TYR PHE SER TRP LEU THR TRP
SEQRES 21 B 719 VAL THR ASP GLU ARG VAL CYS LEU GLN TRP LEU LYS ARG
SEQRES 22 B 719 VAL GLN ASN VAL SER VAL LEU SER ILE CYS ASP PHE ARG
SEQRES 23 B 719 GLU ASP TRP GLN THR TRP ASP CYS PRO LYS THR GLN GLU
SEQRES 24 B 719 HIS ILE GLU GLU SER ARG THR GLY TRP ALA GLY GLY PHE
SEQRES 25 B 719 PHE VAL SER THR PRO VAL PHE SER TYR ASP ALA ILE SER
SEQRES 26 B 719 TYR TYR LYS ILE PHE SER ASP LYS ASP GLY TYR LYS HIS
SEQRES 27 B 719 ILE HIS TYR ILE LYS ASP THR VAL GLU ASN ALA ILE GLN
SEQRES 28 B 719 ILE THR SER GLY LYS TRP GLU ALA ILE ASN ILE PHE ARG
SEQRES 29 B 719 VAL THR GLN ASP SER LEU PHE TYR SER SER ASN GLU PHE
SEQRES 30 B 719 GLU GLU TYR PRO GLY ARG ARG ASN ILE TYR ARG ILE SER
SEQRES 31 B 719 ILE GLY SER TYR PRO PRO SER LYS LYS CYS VAL THR CYS
SEQRES 32 B 719 HIS LEU ARG LYS GLU ARG CYS GLN TYR TYR THR ALA SER
SEQRES 33 B 719 PHE SER ASP TYR ALA LYS TYR TYR ALA LEU VAL CYS TYR
SEQRES 34 B 719 GLY PRO GLY ILE PRO ILE SER THR LEU HIS ASP GLY ARG
SEQRES 35 B 719 THR ASP GLN GLU ILE LYS ILE LEU GLU GLU ASN LYS GLU
SEQRES 36 B 719 LEU GLU ASN ALA LEU LYS ASN ILE GLN LEU PRO LYS GLU
SEQRES 37 B 719 GLU ILE LYS LYS LEU GLU VAL ASP GLU ILE THR LEU TRP
SEQRES 38 B 719 TYR LYS MET ILE LEU PRO PRO GLN PHE ASP ARG SER LYS
SEQRES 39 B 719 LYS TYR PRO LEU LEU ILE GLN VAL TYR GLY GLY PRO CYS
SEQRES 40 B 719 SER GLN SER VAL ARG SER VAL PHE ALA VAL ASN TRP ILE
SEQRES 41 B 719 SER TYR LEU ALA SER LYS GLU GLY MET VAL ILE ALA LEU
SEQRES 42 B 719 VAL ASP GLY ARG GLY THR ALA PHE GLN GLY ASP LYS LEU
SEQRES 43 B 719 LEU TYR ALA VAL TYR ARG LYS LEU GLY VAL TYR GLU VAL
SEQRES 44 B 719 GLU ASP GLN ILE THR ALA VAL ARG LYS PHE ILE GLU MET
SEQRES 45 B 719 GLY PHE ILE ASP GLU LYS ARG ILE ALA ILE TRP GLY TRP
SEQRES 46 B 719 SER TYR GLY GLY TYR VAL SER SER LEU ALA LEU ALA SER
SEQRES 47 B 719 GLY THR GLY LEU PHE LYS CYS GLY ILE ALA VAL ALA PRO
SEQRES 48 B 719 VAL SER SER TRP GLU TYR TYR ALA SER VAL TYR THR GLU
SEQRES 49 B 719 ARG PHE MET GLY LEU PRO THR LYS ASP ASP ASN LEU GLU
SEQRES 50 B 719 HIS TYR LYS ASN SER THR VAL MET ALA ARG ALA GLU TYR
SEQRES 51 B 719 PHE ARG ASN VAL ASP TYR LEU LEU ILE HIS GLY THR ALA
SEQRES 52 B 719 ASP ASP ASN VAL HIS PHE GLN ASN SER ALA GLN ILE ALA
SEQRES 53 B 719 LYS ALA LEU VAL ASN ALA GLN VAL ASP PHE GLN ALA MET
SEQRES 54 B 719 TRP TYR SER ASP GLN ASN HIS GLY LEU SER GLY LEU SER
SEQRES 55 B 719 THR ASN HIS LEU TYR THR HIS MET THR HIS PHE LEU LYS
SEQRES 56 B 719 GLN CYS PHE SER
MODRES 1Z68 ASN A 49 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN A 92 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN A 227 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN A 314 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN B 49 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN B 92 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN B 227 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN B 314 ASN GLYCOSYLATION SITE
MODRES 1Z68 ASN B 679 ASN GLYCOSYLATION SITE
HET NAG A4901 14
HET NAG A9201 14
HET NAG A9202 14
HET NAG A2271 14
HET NAG A2272 14
HET NAG A3141 14
HET NAG B4901 14
HET NAG B9201 14
HET NAG B9202 14
HET NAG B2271 14
HET NAG B3141 14
HET NAG B6791 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 NAG 12(C8 H15 N1 O6)
FORMUL 12 HOH *628(H2 O1)
HELIX 1 1 THR A 43 GLY A 50 1 8
HELIX 2 2 SER A 91 SER A 97 1 7
HELIX 3 3 ASP A 198 MET A 205 1 8
HELIX 4 4 TYR A 271 GLY A 276 1 6
HELIX 5 5 PRO A 283 SER A 288 1 6
HELIX 6 6 PRO A 333 THR A 335 5 3
HELIX 7 7 GLU A 414 TYR A 418 5 5
HELIX 8 8 ASP A 457 LYS A 460 5 4
HELIX 9 9 ASN A 491 LEU A 498 1 8
HELIX 10 10 ASN A 556 LYS A 564 1 9
HELIX 11 11 GLY A 581 TYR A 586 1 6
HELIX 12 12 ALA A 587 TYR A 589 5 3
HELIX 13 13 GLY A 593 GLU A 609 1 17
HELIX 14 14 SER A 624 ALA A 635 1 12
HELIX 15 15 ALA A 657 GLY A 666 1 10
HELIX 16 16 ASN A 673 SER A 680 1 8
HELIX 17 17 VAL A 682 ARG A 690 5 9
HELIX 18 18 PHE A 707 ALA A 720 1 14
HELIX 19 19 GLY A 738 SER A 757 1 20
HELIX 20 20 THR B 43 ASN B 49 1 7
HELIX 21 21 SER B 91 SER B 97 1 7
HELIX 22 22 ASP B 198 MET B 205 1 8
HELIX 23 23 TYR B 271 GLY B 276 1 6
HELIX 24 24 PRO B 283 SER B 288 1 6
HELIX 25 25 PRO B 333 THR B 335 5 3
HELIX 26 26 THR B 383 ALA B 387 5 5
HELIX 27 27 GLU B 414 TYR B 418 5 5
HELIX 28 28 ASP B 457 ALA B 459 5 3
HELIX 29 29 ASN B 491 LEU B 498 1 8
HELIX 30 30 LYS B 499 ILE B 501 5 3
HELIX 31 31 ASN B 556 LYS B 564 1 9
HELIX 32 32 GLY B 581 TYR B 586 1 6
HELIX 33 33 ALA B 587 TYR B 589 5 3
HELIX 34 34 VAL B 594 MET B 610 1 17
HELIX 35 35 SER B 624 ALA B 635 1 12
HELIX 36 36 ALA B 657 GLY B 666 1 10
HELIX 37 37 ASN B 673 SER B 680 1 8
HELIX 38 38 VAL B 682 ARG B 690 5 9
HELIX 39 39 PHE B 707 ALA B 720 1 14
HELIX 40 40 SER B 737 PHE B 756 1 20
SHEET 1 A 4 ASN A 60 TRP A 61 0
SHEET 2 A 4 GLU A 66 GLN A 70 -1 O LEU A 68 N ASN A 60
SHEET 3 A 4 ILE A 76 ASN A 80 -1 O TYR A 79 N TYR A 67
SHEET 4 A 4 SER A 86 LEU A 90 -1 O TYR A 87 N LEU A 78
SHEET 1 B 4 ASN A 102 LEU A 105 0
SHEET 2 B 4 PHE A 111 LYS A 120 -1 O GLU A 115 N ASN A 102
SHEET 3 B 4 TYR A 126 ASP A 134 -1 O THR A 129 N SER A 116
SHEET 4 B 4 GLU A 139 PHE A 140 -1 O GLU A 139 N ASP A 134
SHEET 1 C 4 LEU A 153 TRP A 155 0
SHEET 2 C 4 LEU A 162 TYR A 166 -1 O ALA A 163 N CYS A 154
SHEET 3 C 4 ASN A 169 LYS A 173 -1 O TYR A 171 N TYR A 164
SHEET 4 C 4 PHE A 181 GLN A 182 -1 O PHE A 181 N LEU A 172
SHEET 1 D 3 ILE A 192 ASN A 194 0
SHEET 2 D 3 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 D 3 LEU A 212 TRP A 214 -1 N TRP A 213 O ALA A 222
SHEET 1 E 4 ILE A 192 ASN A 194 0
SHEET 2 E 4 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 E 4 VAL A 261 ASP A 268 -1 O ARG A 263 N GLU A 225
SHEET 4 E 4 GLN A 278 GLU A 279 -1 O GLN A 278 N ILE A 266
SHEET 1 F 2 VAL A 233 TYR A 238 0
SHEET 2 F 2 ARG A 246 PRO A 251 -1 O ILE A 248 N TYR A 236
SHEET 1 G 4 TYR A 291 TRP A 298 0
SHEET 2 G 4 ARG A 303 LYS A 310 -1 O CYS A 305 N THR A 297
SHEET 3 G 4 VAL A 315 PHE A 323 -1 O SER A 319 N LEU A 306
SHEET 4 G 4 TRP A 330 ASP A 331 -1 O ASP A 331 N ASP A 322
SHEET 1 H 4 TYR A 291 TRP A 298 0
SHEET 2 H 4 ARG A 303 LYS A 310 -1 O CYS A 305 N THR A 297
SHEET 3 H 4 VAL A 315 PHE A 323 -1 O SER A 319 N LEU A 306
SHEET 4 H 4 GLU A 337 GLU A 341 -1 O GLU A 340 N SER A 316
SHEET 1 I 4 VAL A 356 PHE A 357 0
SHEET 2 I 4 TYR A 364 SER A 369 -1 O TYR A 365 N VAL A 356
SHEET 3 I 4 LYS A 375 ILE A 380 -1 O HIS A 376 N PHE A 368
SHEET 4 I 4 ILE A 388 GLN A 389 -1 O ILE A 388 N TYR A 379
SHEET 1 J 4 ALA A 397 VAL A 403 0
SHEET 2 J 4 SER A 407 SER A 412 -1 O PHE A 409 N PHE A 401
SHEET 3 J 4 ASN A 423 SER A 428 -1 O TYR A 425 N TYR A 410
SHEET 4 J 4 LYS A 436 CYS A 438 -1 O LYS A 437 N ARG A 426
SHEET 1 K 4 TYR A 451 PHE A 455 0
SHEET 2 K 4 TYR A 462 CYS A 466 -1 O ALA A 463 N SER A 454
SHEET 3 K 4 ILE A 473 HIS A 477 -1 O THR A 475 N LEU A 464
SHEET 4 K 4 GLU A 484 GLU A 489 -1 O ILE A 485 N LEU A 476
SHEET 1 L 8 LYS A 505 VAL A 513 0
SHEET 2 L 8 ILE A 516 LEU A 524 -1 O LEU A 524 N LYS A 505
SHEET 3 L 8 VAL A 568 ASP A 573 -1 O ASP A 573 N TRP A 519
SHEET 4 L 8 TYR A 534 VAL A 540 1 N PRO A 535 O VAL A 568
SHEET 5 L 8 ILE A 613 TRP A 623 1 O ALA A 619 N LEU A 536
SHEET 6 L 8 CYS A 643 VAL A 647 1 O VAL A 647 N GLY A 622
SHEET 7 L 8 ASP A 693 GLY A 699 1 O LEU A 695 N ALA A 646
SHEET 8 L 8 GLN A 725 TYR A 729 1 O GLN A 725 N TYR A 694
SHEET 1 M 3 GLU B 66 HIS B 69 0
SHEET 2 M 3 VAL B 77 ASN B 80 -1 O TYR B 79 N TYR B 67
SHEET 3 M 3 SER B 86 THR B 88 -1 O TYR B 87 N LEU B 78
SHEET 1 N 4 ASN B 102 LEU B 105 0
SHEET 2 N 4 PHE B 111 LYS B 120 -1 O GLU B 115 N ASN B 102
SHEET 3 N 4 TYR B 126 ASP B 134 -1 O TYR B 131 N LEU B 114
SHEET 4 N 4 GLU B 139 PHE B 140 -1 O GLU B 139 N ASP B 134
SHEET 1 O 4 TYR B 152 TRP B 155 0
SHEET 2 O 4 LEU B 162 TYR B 166 -1 O VAL B 165 N TYR B 152
SHEET 3 O 4 ASN B 169 LYS B 173 -1 O TYR B 171 N TYR B 164
SHEET 4 O 4 PHE B 181 GLN B 182 -1 O PHE B 181 N LEU B 172
SHEET 1 P 3 ILE B 192 ASN B 194 0
SHEET 2 P 3 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 P 3 LEU B 212 TRP B 214 -1 N TRP B 213 O ALA B 222
SHEET 1 Q 4 ILE B 192 ASN B 194 0
SHEET 2 Q 4 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 Q 4 VAL B 261 ASP B 268 -1 O ARG B 263 N GLU B 225
SHEET 4 Q 4 GLN B 278 GLU B 279 -1 O GLN B 278 N ILE B 266
SHEET 1 R 2 VAL B 233 TYR B 238 0
SHEET 2 R 2 ARG B 246 PRO B 251 -1 O ILE B 250 N ILE B 234
SHEET 1 S 4 TYR B 291 TRP B 298 0
SHEET 2 S 4 ARG B 303 LYS B 310 -1 O CYS B 305 N THR B 297
SHEET 3 S 4 VAL B 315 ARG B 324 -1 O SER B 319 N LEU B 306
SHEET 4 S 4 THR B 329 ASP B 331 -1 O ASP B 331 N ASP B 322
SHEET 1 T 4 TYR B 291 TRP B 298 0
SHEET 2 T 4 ARG B 303 LYS B 310 -1 O CYS B 305 N THR B 297
SHEET 3 T 4 VAL B 315 ARG B 324 -1 O SER B 319 N LEU B 306
SHEET 4 T 4 GLU B 337 GLU B 341 -1 O GLU B 340 N SER B 316
SHEET 1 U 4 VAL B 356 PHE B 357 0
SHEET 2 U 4 TYR B 364 SER B 369 -1 O TYR B 365 N VAL B 356
SHEET 3 U 4 LYS B 375 ILE B 380 -1 O ILE B 380 N TYR B 364
SHEET 4 U 4 ILE B 388 GLN B 389 -1 O ILE B 388 N TYR B 379
SHEET 1 V 4 ALA B 397 VAL B 403 0
SHEET 2 V 4 SER B 407 SER B 412 -1 O SER B 411 N ASN B 399
SHEET 3 V 4 ASN B 423 SER B 428 -1 O TYR B 425 N TYR B 410
SHEET 4 V 4 LYS B 436 CYS B 438 -1 O LYS B 437 N ARG B 426
SHEET 1 W 4 CYS B 448 PHE B 455 0
SHEET 2 W 4 TYR B 461 PRO B 469 -1 O TYR B 467 N TYR B 450
SHEET 3 W 4 ILE B 473 ASP B 478 -1 O HIS B 477 N TYR B 462
SHEET 4 W 4 GLU B 484 GLU B 489 -1 O LYS B 486 N LEU B 476
SHEET 1 X 8 LYS B 505 GLU B 512 0
SHEET 2 X 8 THR B 517 LEU B 524 -1 O LEU B 518 N LEU B 511
SHEET 3 X 8 VAL B 568 ASP B 573 -1 O ILE B 569 N ILE B 523
SHEET 4 X 8 TYR B 534 VAL B 540 1 N LEU B 537 O ALA B 570
SHEET 5 X 8 ILE B 613 TRP B 623 1 O ALA B 619 N LEU B 536
SHEET 6 X 8 CYS B 643 VAL B 647 1 O VAL B 647 N GLY B 622
SHEET 7 X 8 ASP B 693 GLY B 699 1 O ILE B 697 N ALA B 646
SHEET 8 X 8 GLN B 725 TYR B 729 1 O GLN B 725 N TYR B 694
SSBOND 1 CYS A 321 CYS A 332
SSBOND 2 CYS A 438 CYS A 441
SSBOND 3 CYS A 448 CYS A 466
SSBOND 4 CYS A 643 CYS A 755
SSBOND 5 CYS B 321 CYS B 332
SSBOND 6 CYS B 438 CYS B 441
SSBOND 7 CYS B 448 CYS B 466
SSBOND 8 CYS B 643 CYS B 755
LINK ND2 ASN A 49 C1 NAG A4901
LINK ND2 ASN B 49 C1 NAG B4901
LINK ND2 ASN B 227 C1 NAG B2271
LINK ND2 ASN B 314 C1 NAG B3141
LINK ND2 ASN A 92 C1 NAG A9201
LINK ND2 ASN B 92 C1 NAG B9201
LINK O4 NAG A9201 C1 NAG A9202
LINK O4 NAG B9201 C1 NAG B9202
LINK ND2 ASN B 92 O5 NAG B9201
LINK C1 NAG A2271 ND2 ASN A 227
LINK C1 NAG A3141 ND2 ASN A 314
LINK C1 NAG B6791 ND2 ASN B 679
LINK O3 NAG A2271 C1 NAG A2272
CISPEP 1 GLY A 468 PRO A 469 0 -0.14
CISPEP 2 GLY B 468 PRO B 469 0 2.50
CRYST1 70.295 152.580 214.855 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014226 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004654 0.00000
TER 5890 SER A 757
TER 11806 SER B 757
MASTER 418 0 12 40 97 0 0 612600 2 193 112
END |